You searched for: Proteins and Peptides

Supplier: STEMCELL Technologies

Vascular endothelial growth factor (VEGF) is a heparin-binding homodimeric glycoprotein involved in vasculogenesis and angiogenesis. VEGF binds to FLT1 (VEGFR-1) and KDR (VEGFR-2), and activates Raf/MEK/ERK and PI3K/AKT pathways (Ferrara et al.). VEGF exists in multiple isoforms that result from alternative splicing of VEGF mRNA in the terminal exon. Proximal splice-site selection in exon 8 results in pro-angiogenic VEGFxxx isoforms (xxx is the number of amino acids), whereas distal splice-site selection results in anti-angiogenic VEGFxxxb isoforms (Nowak et al.). VEGF plays an important role in neurogenesis both in vitro and in vivo (Storkebaum et al.). It has neurotrophic effects on neurons of the central nervous system, and it promotes growth and survival of dopaminergic neurons and astrocytes. VEGF also promotes growth and survival of vascular endothelial cells, monocyte chemotaxis, and colony formation by granulocyte-macrophage progenitor cells (Ferrara et al.). Various splice variants of VEGF exist, with different functions. For example, it has been shown that VEGF isoform VEGF-164(165) and not VEGF-120(121) induces inflammation, stimulates intracellular adhesion molecule (ICAM)-1 expression on endothelial cells, and induces chemotaxis of monocytes (Usui et al.).

Supplier: Adipogen

Epidermal growth factor (EGF) is a growth factor and the founding member of the EGF family. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. These receptors undergo a complex pattern of ligand induced homo or heterodimerization to transduce EGF family signals. EGF binds to the receptor EGFR stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity initiates a signal transduction cascade that results in a variety of biochemical changes within the cell, including a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR, which lead to DNA synthesis, cell growth, proliferation and differentiation. Other biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture. Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4), also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes.

Supplier: STEMCELL Technologies

Betacellulin is a member of the epidermal growth factor (EGF) family, and signals through EGF receptor and ERBB4. It activates ERK and AKT pathways, which induces neural stem cell proliferation and prevents spontaneous differentiation in culture. Betacellulin stimulates the expansion of neural stem cells, transit-amplifying cells, and neuroblasts derived from subventricular zone and dentate gyrus (Gómez-Gaviro et al.). It is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Betacellulin down-regulates E-cadherin expression in ovarian cancer cell lines via MEK/ERK1/2 and PI3K/AKT signaling pathways, thus increasing cell migration (Zhao et al.). It is a modulator of interferon (IFN) response and enhances anti-viral effects of IFN (Al-Yahya et al.). Betacellulin is expressed in pancreatic α cells, β cells, and duct cells. It induces the proliferation of pancreatic cancer cell lines, inhibits apoptosis, promotes the neogenesis of β cells, and converts non-β cells into insulin-producing cells (Kawaguchi et al.; Miyagawa al.; Saito et al.).

Supplier: Adipogen

CD152 and CD28, together with their ligands B7-1 and B7-2, constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD152 and CD28 are structurally homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD152 and CD28 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an intracellular domain. CD152 and CD28 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. CD152 was originally identified as a gene that was specifically expressed by cytotoxic T lymphocytes. However, CD152 transcripts have since been found in both Th1 and Th2, and CD4+ and CD8+ T cell clones. Whereas, CD28 expression is constitutive on the surfaces of 95% of CD4+ T cells and 50% of CD8+ T cells and is down regulated upon T cell activation, CD152 expression is upregulated rapidly following T cell activation and peaks approximately 24 hours following activation. Although both CD152 and CD28 can bind to the same ligands, CD152 binds to B71 and B72 with 20-100-fold higher affinity than CD28.

Supplier: Adipogen

Interleukin-21 receptor (IL-21R) is a type I transmembrane glycoprotein within the class I cytokine receptor family, type 4 subfamily. Complex formation between IL-21R and the common gamma chain (gammac) is required for signaling. IL-21R is expressed mainly on B cells (highest on mature, activated, follicular and germinal center B cells), NK cells and activated T cells, but is also found on dendritic cells, alternatively activated macrophages, intestinal lamina propria fibroblasts and epithelial cells and keratinocytes. B cell IL-21R engagement induces Blimp1 (which mediates plasma cell differentiation) and is important for memory responses. IL-21R engagement on mouse NK cells enhances their cytotoxic activity and IFN-gamma production. IL-21R engagement on CD8+ T cells aids control of viral infection and tumor growth; IL-21R is also necessary for sufficient numbers of regulatory T cells to combat chronic inflammation. IL-21R expression is often upregulated in allergic skin inflammation, systemic lupus erythematosus and diffuse large B cell lymphoma (DLBCL).

Supplier: STEMCELL Technologies

Interferon-gamma (IFN-γ), also known as type II interferon, is produced by T and NK cells, and in smaller amounts by dendritic cells and macrophages. IFN-γ is controlled by cytokines such as IL-12 and IL-18 secreted in response to infection (Schroder et al.). IFN-γ binds to a receptor complex and initiates signal transduction via the JAK/STAT pathway; this culminates in the transcription and activation of many genes that control a diverse array of immunological functions (de Weerd and Nguyen; Krause et al.). IFN-γ stimulates the antimicrobial and anti-tumor activity of macrophages, NK cells, and neutrophils (Billiau and Matthys) by promoting the activation of microbial effector functions such as production of reactive oxygen species, NO intermediates, and complement (Schroder et al.). IFN-γ enhances MHC class I and II expression in dendritic cells and mononuclear phagocytes, as well as the production of IL-12 by dendritic cells. In B cells, IFN-γ stimulates survival and growth in both mouse and human cells, and redirects B cells from proliferation towards differentiation. IFN-γ favors the development of Th1 vs Th2 cells and stimulates monocyte differentiation and function (Schroder et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Interleukin 11 (IL-11) is a pleiotropic cytokine with effects on various tissues including the bone marrow, brain, and intestinal mucosa (Du and amp; Williams). It belongs to the IL-6 family of cytokines that share a common signal transducer, gp130. Culture of mouse bone marrow cells with IL-11 in combination with IL-3, IL-6, and stem cell factor induces significant expansion and proliferation of colony-forming cells in vitro (Peters et al.). In addition, in combination with IL-3, IL-11 significantly enhances the growth of megakaryocytic colonies in vitro, suggesting its role in augmenting mouse megakaryopoiesis (Yonemura et al.). IL-11 is expressed in a wide range of normal adult mouse tissues, including the central nervous system, thymus, lung, and bone. The mouse IL-11 cDNA was cloned using an expression library generated from the lipopolysaccharide-induced mouse fetal thymic cell line, T2 (Morris et al.). The binding of IL-11 to its receptor induces heterodimerization with the gp130 subunit and activation of JAK tyrosine kinases. IL-11 also plays a role in cancer progression by inducing the proliferation of epithelial cancer cells and the survival of metastatic cells at distant organs. Recently, IL-11 has gained interest for its role in the pathogenesis of diseases in dysregulated mucosal homeostasis associated with STAT3 upregulation, including gastrointestinal cancers (Putoczki et al.).

Supplier: STEMCELL Technologies

Platelet-derived growth factor (PDGF) is a dimeric glycoprotein consisting of two disulfide bridge-stabilized polypeptide chains, A and B, which are assembled as heterodimers (PDGF-AB) or homodimers (PDGF-AA and PDGF-BB) (Fretto et al.; Westermark and Heldin). PDGF signals through the receptor tyrosine kinases PDGFRalpha and PDGFRbeta. PDGF-induced migration has been shown to involve MEK/ERK, EGFR, Src, and PI3K/Akt signaling pathways (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin- like fibroblasts, glial cells, and vascular smooth muscle cells. PDGF has been implicated in pathogenesis of atherosclerosis, glomerulonephritis, cancer, and in the contraction of vascular smooth muscle cells of rat aortic tissues (Fretto et al.; Sachinidis et al.). PDGF-BB is secreted by osteoblasts to induce mesenchymal stem cell migration and angiogenesis. It has also been shown that PDGF-BB is secreted by preosteoclasts during bone modeling and remodeling to induce angiogenesis and thus proper osteogenesis (Xie et al.). This product is animal component-free.

Supplier: Adipogen

Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important homeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens. IL-2 promotes T cell proliferation and particularly naive T cells. IL-2 signaling on activated T cells is effected through a quaternary high-affinity receptor complex consisting of IL-2, IL-2Ralpha (CD25), IL-2Rbeta and IL-2Rgamma. Naive T cells are relatively insensitive to IL-2 as they only express small amounts of IL-2Rbeta and IL-2Rgamma. They only acquire sensitivity after CD25 expression, which captures the cytokine and presents it to the IL-2Rbeta and IL-2Rgamma receptors. IL-2 Superkine (Fc) is an artificial variant of IL-2 containing mutations at positions L80F / R81D / L85V / I 86V / I92F. These mutations are located in the molecule's core that acts to stabilize the structure and to give it a receptor-binding conformation mimicking native IL-2 bound to CD25. These mutations effectively eliminate the functional requirement of IL-2 for CD25 expression and elicit proliferation of T cells. Compared to IL-2, the IL-2 superkine induces superior expansion of cytotoxic T cells, leading to improved antitumour responses in vivo, and elicits proportionally less toxicity by lowering the expansion of Tregulatory cells and reducing pulmonary oedema.

Supplier: STEMCELL Technologies

Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf andamp; Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilization of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways.

Supplier: ADVANCED BIOMATRIX, INC. MS

Advanced BioMatrix VitroCol® collagen is the first widely available, naturally produced purified human collagen for research purposes. VitroCol® sets the standard for purity (>99% collagen content), functionality and represents the only native-like human collagen offered.

VitroCol® collagen is naturally secreted from human neo-natal fibroblast cells. The human fibroblasts are cultured in optimal conditions allowing the fibroblast to naturally and efficiently secret extracellular matrix. The extracellular matrix is then processed and purified to yield the naturally produced human collagen.

VitroCol® is approximately 97% Type I human collagen with the remainder being comprised of Type III collagen. It contains a high monomer content as measured by gel permeation chromatography.

VitroCol® is supplied at approximately 3 mg/ml concentration. The concentration for each specific lot is provided on a Certificate of Analysis that is available with the purchase of each product. VitroCol® is soluble atelo-collagen in 0.01 N HCI, therefore, the pH is approximately 2.0.

VitroCol® is especially ideal for human cell culture systems when coating of surfaces, providing preparations of thin layers of culturing cells, or use as a solid gel. VitroCol® human collagen is provided in user-friendly packaging for use and storage. VitroCol® is sterile filtered and is supplied as a ready to use solution.

Supplier: Adipogen

NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappaB p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3.

Supplier: ADVANCED BIOMATRIX, INC. MS

FibriCol® collagen is known as the standard of all collagens for purity (>99% collagen content), functionality, and the most native-like collagen available. FibriCol® is isolated from bovine hides sourced from the only controlled, closed herd in the United States. Advanced BioMatrix’s manufacturing processes comply with stringent quality standards that have proven to yield unsurpassed lot-to-lot consistency.

FibriCol® collagen is approximately 97% Type I collagen with the remainder being comprised of Type III collagen. It contains a high monomer content as measured by gel permeation chromatography.

FibriCol® collagen is supplied at approximately a 10 mg/mL concentration. The concentration for each specific lot is provided on a Certificate of Analysis that is available with the purchase of each product. FibriCol® is soluble atelo-collagen in 0.01 N HCI, therefore, the pH is approximately 2.0.

FibriCol® collagen is ideal for applications where high concentrations of collagen are needed. FibriCol® collagen is provided in a 20 mL volume and is contained in user-friendly packaging for use and storage. FibriCol® is sterile filtered and is supplied as a ready to use solution.

Supplier: STEMCELL Technologies

Glial cell line-derived neurotrophic factor (GDNF) is a neurotrophic factor and a member of the tumor growth factor (TGF)-beta superfamily. The GDNF family of growth factors also includes neurturin, persephin, and artemin, which have seven conserved cysteine residues called cysteine-knots (Treanor et al.). GDNF family ligands signal through binding to specific GDNF-family receptor-α (GFRα) co-receptors and activate the RET receptor tyrosine kinase (Durbec et al.). Four different forms of GFRα co-receptors have been characterized (GFRα 1-4); GDNF binds specifically to GFRα1 prior to forming a complex with RET (Airaksinen and Saarma). GDNF is known to promote survival and morphological differentiation of midbrain dopaminergic neurons in both in vivo and in vitro studies and increases their high-affinity dopamine uptake (Granholm et al.; Lin et al.). GDNF has also been shown to have restorative effects on dying dopaminergic neurons in response to degenerative toxins (Aoi et al.). GDNF, together with Human Recombinant BDNF (brain-derived neurotrophic factor; MSPP-78005), BrainPhys™ Neuronal Medium (MSPP-05790), and other supplements, can be used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Bardy et al.).

Supplier: STEMCELL Technologies

Granulocyte-macrophage colony-stimulating factor (GM-CSF) promotes the proliferation and differentiation of hematopoietic progenitor cells and the generation of neutrophils, eosinophils, and macrophages. In synergy with other cytokines such as stem cell factor, IL-3, erythropoietin, and thrombopoietin, it also stimulates erythroid and megakaryocyte progenitor cells (Barreda et al.). GM-CSF is produced by multiple cell types, including stromal cells, Paneth cells, macrophages, dendritic cells (DCs), endothelial cells, smooth muscle cells, fibroblasts, chondrocytes, and Th1 and Th17 T cells (Francisco-Cruz et al.). The receptor for GM-CSF (GM-CSFR) is composed of two subunits: the cytokine-specific α subunit (GMRα; CD116) and the common subunit βc (CD131) shared with IL-3 and IL-5 receptors (Broughton et al.). GM-CSFR is expressed on hematopoietic cells, including progenitor cells and immune cells, as well as non-hematopoietic cells. Recombinant human GM-CSF (rhGM-CSF) promotes the production of myeloid cells of the granulocytic (neutrophils, eosinophils and basophils) and monocytic lineages in vivo. It has been tested for mobilization of hematopoietic progenitor cells and for treating chemotherapy-induced neutropenia in patients. GM-CSF is able to stimulate the development of DCs that ingest, process, and present antigens to the immune system (Francisco-Cruz et al.).

Supplier: ADVANCED BIOMATRIX, INC. MS

Type III Collagen provides structure and strength to connective tissue, is found many places in the body, especially skin, lung, intestinal walls and the walls of blood vessels. Collagen III is initially produced as procollagen, a protein consisting of three pro-alpha1(III) chains that form the triple-stranded, rope-like molecule. After being synthesized, the procollagen molecule is modified by the cell. Enzymes modify the amino acids lysine and proline in the protein strands by adding chemical groups that are necessary for the strands to form a stable molecule and then later to crosslink to other molecules outside the cell. The Type III procollagen molecules are released from the cell and are processed by enzymes that clip small segments off either end of the molecules to form mature collagen. The mature collagen molecules assemble into fibrils. Cross-linking between molecules produces a very stable fibril, contributing to collagen’s tissue strengthening function.

This Type III Collagen product is isolated from human placenta and is purified using a multi-step process with approximately 85% Type III collagen with the remainder being comprised of Type I collagen. The product is supplied as a sterile solution with 10 mg at approximately 1 mg/ml in 0.01 N HCl, pH 2. A Certificate of Analysis is available with the purchase of each product. Type III collagen product is provided in a user-friendly packaging for use and storage. This Type III collagen product is sterile filtered and is supplied as a ready to use solution.

Type III Collagen is typically used as a thin coating on tissue culture surfaces or as a control. Specific instructions are found in the Directions for Use. This product is generally used in vitro as a substrate scaffold to enhance cell attachment, adherence and proliferation. Type III collagen may be used to culture a variety of cell types.

Supplier: STEMCELL Technologies

Glial cell line-derived neurotrophic factor (GDNF) is a neurotrophic factor and a member of the tumor growth factor (TGF)-beta superfamily. The GDNF family of growth factors also includes neurturin, persephin, and artemin, which have seven conserved cysteine residues called cysteine-knot (Treanor et al.). GDNF family ligands signal through binding to specific GDNF-family receptor-α (GFRα) co-receptors and activate the RET receptor tyrosine kinase (Durbec et al.). Four different forms of GFRα co-receptors have been characterized (GFRα 1-4) out of which GDNF binds specifically to GFRα1 prior to forming a complex with RET (Airaksinen and Saarma). GDNF is known to promote survival and morphological differentiation of midbrain dopaminergic neurons in both in vivo and in vitro studies and increase their high-affinity dopamine uptake (Granholm et al.; Lin et al.). GDNF has also been shown to have restorative effects on dying dopaminergic neurons in response to degenerative toxins (Aoi et al.). GDNF, together with Human Recombinant BDNF (brain-derived neurotrophic factor; Catalog #78005), BrainPhys™ Neuronal Medium (Catalog #05790), and other supplements, can be used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Bardy et al.). This product is animal component-free.

Supplier: ADVANCED BIOMATRIX, INC. MS

Type III Collagen provides structure and strength to connective tissue, is found many places in the body, especially skin, lung, intestinal walls and the walls of blood vessels. Collagen III is initially produced as procollagen, a protein consisting of three pro-alpha1(III) chains that form the triple-stranded, rope-like molecule. After being synthesized, the procollagen molecule is modified by the cell. Enzymes modify the amino acids lysine and proline in the protein strands by adding chemical groups that are necessary for the strands to form a stable molecule and then later to crosslink to other molecules outside the cell. The Type III procollagen molecules are released from the cell and are processed by enzymes that clip small segments off either end of the molecules to form mature collagen. The mature collagen molecules assemble into fibrils. Cross-linking between molecules produces a very stable fibril, contributing to collagen’s tissue strengthening function.

This Type III Collagen product is isolated from human placenta and is purified using a multi-step process with approximately 85% Type III collagen with the remainder being comprised of Type I collagen. The product is supplied as a non-sterile powder. A Certificate of Analysis is available with the purchase of each product. Type III collagen product is provided in a user-friendly packaging for use and storage.

Type III Collagen is typically used as a thin coating on tissue culture surfaces or as a control. Specific instructions are found in the Directions for Use. This product is generally used in vitro as a substrate scaffold to enhance cell attachment, adherence and proliferation. Type III collagen may be used to culture a variety of cell types.

Supplier: BioVendor

Visceral adipose tissue – derived serpin A12 (vaspin), also named OL-64, an adipocytokine, is structurally a member of the serine protease family. Serpins are the most diverse family of protease inhibitors. Their typical structural feature is the core domain composed from 3 beta-sheets and 9 alpha-helixes. The inhibitory activity of vaspin has not been described up to now, but its reactive site loop is typical for this proteinase family. Human Vaspin protein is composed of 395 amino acids and has a molecular weight of approximately 45.2 kDa and predicted pI 9.26. The cDNA was first isolated from white adipose tissue of Otsuka Long-Evans Tokushima Fatty (OLETF) rats. Vaspin mRNA expression is specific for visceral adipose tissues and it is also found circulating in the serum. The level of serum vaspin increased with age up to the peak of obesity, body weight and insulin resistance in OLETF rats and decreases with worsening of diabetes. Vaspin expression is missing in the diabetes-resistant lean rats, LETO, in comparison to OLEFT rats, animal model of metabolic syndrome. Expression was also absent in the subdermal, brown fatty tissue and other non-adipose tissues in OLEFT rats. These findings lead to the conclusion that the target tissue for insulin sensitising effect of vaspin is white adipose tissue. In humans, elevated serum concentration of vaspin is associated with obesity and impaired insulin sensitivity.

Supplier: STEMCELL Technologies

The platelet-derived growth factor (PDGF) family has five heparin-binding members that assemble into four homodimers (PDGF-AA, PDGF-BB, PDGF-CC, and PDGF-DD) and one heterodimer (PDGF-AB; Li and Eriksson). PDGF signals through the receptor tyrosine kinases PDGFRα and PDGFRβ. It has been shown that PDGF-induced migration involves signaling pathways involving MEK/ERK, EGFR, Src and PI3K/AKT (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin such as fibroblasts and vascular smooth muscle cells. PDGF has been implicated in pathogenesis of atherosclerosis, glomerulonephritis, cancer, and in the contraction of vascular smooth muscle cells of rat aortic tissues (Fretto et al.; Sachinidis et al.). PDGF-CC is secreted as a latent growth factor and requires activation by proteolytic processing (Li and Eriksson). PDGF-CC binds to PDGFRα homodimers and PDGFRαβ heterodimers, but not to PDGFRβ homodimers (Li and Eriksson). PDGF-CC is an angiogenic factor that stimulates coronary artery smooth muscle cell proliferation and plays a role in cardiovascular development (Gilbertson et al.). PDGF-CC is also expressed in many tumors and plays a role in tumorigenesis (Zwerner and May).

Supplier: Adipogen

CD28 and CTLA-4 together with their ligands, CD80 (B7-1) and CD86 (B7-2), constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD28 and CTLA-4 are structurally homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD28 and CTLA-4 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an intracellular domain. CD28 and CTLA-4 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. The genes encoding these two molecules are closely linked on human chromosome 2 and mouse chromosome 1. Mouse CD28 is expressed constitutively on virtually 100% of mouse T cells and on developing thymocytes. Cell surface expression of mouse CD28 is downregulated upon ligation of CD28 in the presence of PMA or PHA. In contrast, CTLA-4 is not expressed constitutively but is upregulated rapidly following T cell activation and CD28 ligation. Cell surface expression of mouse CTLA-4 peaks approx.y 48 hours after activation. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28. CD28/B7 interaction has been shown to prevent apoptosis of activated T cells via the upregulation of bcl-XL. CD28 ligation has also been shown to regulate Th1/Th2 differentiation.

Supplier: Adipogen

CD28 and CTLA-4 together with their ligands, CD80 (B7-1) and CD86 (B7-2), constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD28 and CTLA-4 are structurally homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD28 and CTLA-4 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an intracellular domain. CD28 and CTLA-4 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. The genes encoding these two molecules are closely linked on human chromosome 2 and mouse chromosome 1. Mouse CD28 is expressed constitutively on virtually 100% of mouse T cells and on developing thymocytes. Cell surface expression of mouse CD28 is downregulated upon ligation of CD28 in the presence of PMA or PHA. In contrast, CTLA-4 is not expressed constitutively but is upregulated rapidly following T cell activation and CD28 ligation. Cell surface expression of mouse CTLA-4 peaks approx.y 48 hours after activation. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28. CD28/B7 interaction has been shown to prevent apoptosis of activated T cells via the upregulation of bcl-XL. CD28 ligation has also been shown to regulate Th1/Th2 differentiation.

Supplier: Adipogen

Interleukin-15 (IL-15) has a broad spectrum of biological activities. It is crucial for the development, proliferation, survival and differentiation of multiple cells from both innate and adaptive immune systems. IL-15 up-regulation has a central role in the development of several autoimmune or chronic inflammatory disorders. Targeting IL-15 or its receptor may have a valuable impact on the treatment of immune-mediated diseases. IL-15 participates in the development of important immune antitumor mechanisms. It activates CD8(+) T cells, natural killer (NK) cells, NK T cells, and can promote the formation of antitumor antibodies. IL-15 can also protect T effector cells from the action of T regulatory cells and reverse tolerance to tumor-associated antigens. In pre-clinical studies IL-15 has been found to demonstrate potentiated antitumor effects following pre-association with IL-15Ralpha, or when used in combination with chemotherapy, adoptive therapy, monoclonal antibodies, and tumor vaccines. Application: Useful for immunofluorescent staining and flow cytometric analysis to identify and enumerate IL-15Ralpha expressing cells within mixed cell populations.

Supplier: ADVANCED BIOMATRIX, INC. MS

Type IV Collagen is the primary collagen found in the extracellular basement membranes separating a variety of epithelial and endothelial cells. It is a major component of the dermal-epidermal junction where it is mostly found in the lamina densa. It is a heterotrimeric molecule containing two Alpha 1-like and one Alpha 2-like chains.

This Type IV Collagen is isolated from human placenta and is purified using a multi-step process. The product is supplied as a non-sterile powder containing 5 mg of Type IV collagen per vial. A Certificate of Analysis is available with the purchase of each product.

Type IV Collagen is typically used as a thin coating on tissue culture surfaces. Specific instructions are found in the Directions for Use. This product is generally used in vitro as a substrate scaffold to enhance cell attachment, adherence and proliferation. Type IV collagen may be used to culture epithelial, endothelial, muscle, nerve and many other cell types. Additionally, this product is suitable for use as a substrate for collagenase assays and positive controls.

Supplier: ADVANCED BIOMATRIX, INC. MS

Type IV Collagen is the primary collagen found in the extracellular basement membranes separating a variety of epithelial and endothelial cells. It is a major component of the dermal-epidermal junction where it is mostly found in the lamina densa. It is a heterotrimeric molecule containing two Alpha 1-like and one Alpha 2-like chains.

This Type IV Collagen is isolated from human placenta and is purified using a multi-step process. The product is supplied as a sterile, lyophilized powder containing 5 mg of Type IV collagen per vial. A Certificate of Analysis is available with the purchase of each product.

Type IV Collagen is typically used as a thin coating on tissue culture surfaces. Specific instructions are found in the Directions for Use. This product is generally used in vitro as a substrate scaffold to enhance cell attachment, adherence and proliferation. Type IV collagen may be used to culture epithelial, endothelial, muscle, nerve and many other cell types. Additionally, this product is suitable for use as a substrate for collagenase assays and positive controls.

Supplier: ADVANCED BIOMATRIX, INC. MS

VitroCol® collagen is the first widely available, naturally produced purified human collagen for research purposes. VitroCol® sets the standard for purity (>99% collagen content), functionality and represents the only native-like human collagen offered.

VitroCol® collagen is naturally secreted from human neo-natal fibroblast cells. The human fibroblasts are cultured in optimal conditions allowing the fibroblasts to naturally and efficiently secret extracellular matrix. The extracellular matrix is then processed and purified to yield the naturally produced human collagen.

VitroCol® is approximately 97% Type I human collagen with the remainder being comprised of Type III collagen. It contains high monomer content as measured by gel permeation chromatography.

This product is supplied as a lyophilized powder with 15 mg of human collagen. When reconstituted with 5 ml of sterile 0.01 N HCl, a concentration of approximately 3 mg/ml is achieved.

VitroCol® is especially ideal for human cell culture systems when coating of surfaces and providing preparations of thin layers of culturing cells. VitroCol®, lyophilized form is not recommend for the formation of a solid gel. VitroCol® human collagen is provided in user-friendly packaging for use and storage. VitroCol® is supplied as a sterile, lyophilized powder.

Supplier: Adipogen

BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers. Processed human BAFF can either remain as a trimer, which is usual for TNF family ligands or assemble into 60-mer composed of 20 trimers. Mouse BAFF 60-mer has been identified in the serum of BAFF transgenic mice. Oligomerization of BAFF 3-mer into 60-mer in human BAFF is prevented by mutation of His218, a residue critical for 3-mer-to-3-mer interactions, but not for receptor binding. Despite the predominant functional role of processed BAFF in vivo, membrane-bound BAFF might also play a role. Indeed, soluble BAFF (3-mer) can trigger BAFF-R but not TACI or BCMA, whereas oligomeric forms of BAFF (BAFF 60-mer), which mimic membrane-bound BAFF, activate all BAFF receptors.

Supplier: STEMCELL Technologies

Interleukin 34 (IL-34) is well known for its ability to induce the formation of colony-forming unit macrophages in human bone marrow cell cultures (Foucher et al.; Wei et al.). This dimeric glycoprotein is a member of the short-chain helical hematopoietic cytokine family (Baghdadi et al.; Foucher et al.), and exists in two isoforms that differ by a single glutamine (Chen et al.; Foucher et al; Wei et al.). IL-34 interacts with M-CSF to trigger tyrosine phosphorylation of the receptor and ERK1/2 pathways. (Wang et al.; Wei et al.). It is expressed in many tissues (heart, brain, lung, liver, kidney, thymus, testes, ovary, small intestine, prostate, and colon), with the highest expression in the spleen. In combination with RANKL (MSPP-78214), IL-34 induces osteoclast differentiation (Chen et al.; Foucher et al.). IL-34 expression is decreased in Alzheimer’s disease and atopic dermatitis, while high levels of IL-34 are found in many types of cancer correlated with poor prognosis, chronic heart failure or coronary artery disease, inflammatory bowel disease, influenza A infection, during acute liver transplant rejection or in non-alcoholic fatty liver disease, and with rheumatoid arthritis (Baghdadi et al.). It is therefore a possible pharmacological target for treating bone or inflammatory diseases (Chen et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain, and the protein was purified as a homodimer consisting of 39 kDa monomers (Lin et al.).

Supplier: ADVANCED BIOMATRIX, INC. MS

Type I bovine collagen, lyophilized fibrous powder is extracted from bovine flexor tendon with the raw material sourced from closed/controlled herds of animals. Because the collagen is extracted from tendon, the material is more naturally crosslinked. The collagen is polymeric insoluble collagen. The manufacturing processes comply with stringent quality standards that have proven to yield a high quality product with lot-to-lot consistency. This product has a purity of >96% with Type II and Type III collagens not detectable.

This product is supplied as a lyophilized fibrous powder in a 1 gram package size. Bioburden and endotoxin levels are tested – this product is not considered sterile.

This collagen product is naturally cross-linked yielding a robust material for applications which require structure and strength. This product can be readily prepared into such forms as tissue scaffolds, foams, sponges, suspensions, coatings, putties, films and sheets but does not form hydrogels. Using typical cross-linking methods, this material can be tuned for optimal in vivo resorption. This collagen product is ideal for tissue engineering applications and uses with inorganic and biomaterials.

The product is provided in user-friendly packaging for use and storage. Avoid extended exposure to ambient environment since this material is hygroscopic.

Supplier: STEMCELL Technologies

Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf and Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilization of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Mouse G-CSF was first purified from cultures of the WEHI-3B myelomonocytic leukemia cell line as the inducer of the terminal differentiation of WEHI-3B and other myeloid leukemia cell lines (Nicola et al.). It was later cloned in monkey COS cells from a cDNA library prepared with mRNA derived from mouse fibrosarcoma NFSA cells that produce G-CSF constitutively (Tsuchiya et al.). Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways.