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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

Interleukin-35 (IL-35) is a novel IL-12 family cytokine produced by regulatory T cells (Treg) but not by resting or activated effector T cells (Teff). IL-35 is a heterodimeric protein composed of EBI3 (Epstein-Barr-Virus-induced gene 3) and IL-12a (p35). EBI3 is a downstream target of Foxp3, a transcription factor required for Treg-cell development and function, and thus Treg-cell restriction of IL35 occurs. Regulatory T cells are essential for maintaining self tolerance and preventing autoimmunity, and IL-35 is identified as a molecule that mediates the immune suppression function of Treg-cell. As an inhibitory cytokine, IL-35 induces proliferation of Treg-cell populations but suppresses Th17 cell development. Studies in mice show the absence of either IL-35 chain from Treg-cell reduces the cells' ability to suppress inflammation using an experimental model for inflammatory bowel disease. IL-35 is suggested as a potential target of immunotherapy.

Supplier: Anaspec Inc

Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-12 (macrophage elastase) is involved in smoke-induced emphysema, tumor and other diseases. MMP-12 is secreted as a 54-kDa zymogen and becomes the mature 45-kDa active form after proteolytic cleavage. MMP-12 has a broad range of substrates, including α-1 proteinase inhibitor, α-2 antiplasmin, plasminogen activator inhibitor-2, collagen IV, laminin, fibronectin, elastin, but not interstitial collagens.

The sequence (Accession # NP_002417) corresponding to the catalytic domain (aa 106-267) of Human MMP-12 was expressed in E. coli. The recombinant human MMP-12 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-12 Catalytic Domain is 18 kDa.

Supplier: Anaspec Inc

Matrix metalloproteinases (MMP’s) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-1 (collagenase-1) is involved in tumor development and metastasis and rheumatoid arthritis. It is proposed as a therapeutic target for these diseases. Native pro-MMP-1 is prepared from culture medium of human rheumatoid synovial fibroblasts. MMP-1 is secreted as pro-enzyme, which consists of a propeptide of 80 amino acids, a catalytic domain of 162 amino acids, a 16-residue linker region, and a hemopexin domain of 189 amino acids. The native pro-MMP-1 has a major Mr 52-kDa unglycosylated and a minor Mr 57-kDa glycosylated form. The proteolytic activation of the 57/52-kDa species will form 47/42-kDa active collagenase, and a 22-kDa C-terminal fragment
The apparent Mr on SDS-PAGE is approximately 56kDa/52 kDa. The pro-MMP-1 can be fully activated by incubating with 1 mM APMA at 37°C for 3 hr. Its activity can be measured by FRET peptides. 10-20 ng of enzyme is sufficient for FRET-based assay

Supplier: STEMCELL Technologies

Interleukin 33 (IL-33) is a pro-inflammatory cytokine from the IL-1 family. It binds to the ST2 receptor and activates NF-kB and MAPK pathways. IL-33 is expressed by epithelial cells, smooth muscle cells, and fibroblasts in various tissues and organs, as well as resting basophils, mast cells, eosinophils, natural helper cells, group 2 innate lymphoid cells, dendritic cells, and activated macrophages (Schmitz et al.; Yasuda et al.). It contributes to allergic inflammation by stimulating production of the cytokines IL-4, IL-5, and IL-13 in Th2 cells, and stimulates host defense against microbial and viral infections (Liew; Yasuda et al.). In the central nervous system, IL-33 is produced by endothelial cells and astrocytes. It induces proliferation of microglia and mediates production of pro-inflammatory cytokines (Yasuoka et al.).

Supplier: STEMCELL Technologies

Nerve growth factor (NGF)-beta is a prototypical member of the neurotrophin family and has a role in the survival and growth of neural cells, regulating cell growth, promoting differentiation into neurons, and neuron migration. The beta subtype of NGF is biologically active in comparison to the alpha-2 and gamma-2 subtypes. NGF-beta in its secreted form can bind to tyrosine kinase A (trkA) receptor with high affinity and to p75 (NTR) with low affinity (Levi and Alemà; Sofroniew et al.). NGF has been shown to possess pro-inflammatory and pro-fibrogenic properties (Micera et al.). It has also been shown that overexpression of NGF-beta promotes differentiation of bone marrow mesenchymal stem cells into neurons through regulation of AKT and MAPK pathways (Yuan et al.). This product is animal component-free.

Supplier: BioVendor

FGF-23 is a secreted, nonglycosylated monomeric protein belonging to the FGF family. Full-lenght FGF-23 is a phosphaturic hormone which blocks neural phosphate reabsorbtion. Upon processing, biologically inactive N- and C- terminal fragments are generated. Defects in FGF-23 is associated with autosomal dominant hypophosphatemic rickets. The FGF-23 gene encodes a member of the fibroblast growth factor family that is mutant in autosomal dominant hypophosphatemic rickets (ADHR). Tumor-induced osteomalacia is one of the paraneoplastic disorders characterized by hypophosphatemia caused by renal phosphate wasting. The fact that removal of responsible tumors normalizes phosphate metabolism is evidence that a humoral phosphaturic factor, sometimes called phosphatonin, is the basis of tumor-induced osteomalacia. Thus, overproduction of FGF-23 causes tumor-induced osteomalacia, whereas mutations in the FGF-23 gene result in autosomal hypophosphatemic rickets possibly by preventing proteolytic cleavage, which enhances the biologic activity of FGF-23. The mutations in FGF-23 found in ADHR lie within 3 nucleotides of each other in the proprotein convertase cleavage site. Jonsson et al. (2003) showed that FGF-23 is readily detectable in the plasma or serum of healthy persons and can be markedly elevated in those with oncogenic osteomalacia or X-linked hypophosphatemia, suggesting that this growth factor has a role in phosphate homeostasis.

Supplier: BioVendor

Visinin like protein 1 (VILIP-1, VLP-1 or VSNL-1) is a cytoplasmic protein of low molecular weight (approximately 22 kDa) consisting of 191 amino acid residues. It belongs to the visinin/recoverin subfamily of neuronal calcium sensor proteins involved in calcium-dependent signal transduction mechanisms in neurons. It is found primarily in the brain, in nerve cells, but it also has a peripheral distribution in liver, lung, kidney, spleen, pancreas and colon. When localized at the membrane, it modulates various cellular signal transduction pathways, including cyclic adenosine monophosphate (cAMP)- and cyclic guanosine monophosphate (cGMP)-signaling in neural cells, human embryonic kidney cells, the pancreatic β cell line MIN6, and various skin tumor cell lines. It contains four internal repeats of 36–38 amino-acids, each containing a potential EF-hand domain. Two of the four EF-hand Ca2+-binding motifs of VILIP-1 are able to bind either Ca2+ or Mg2+in a non-cooperative manner. Binding of Ca2+ leads to specific conformational changes in the protein and this may regulate the interaction of VILIP with intracellular target molecules. VILIP-1 has been identified as a potential biomarker for brain injury and several neurodegenerative diseases. VILIP-1-expressing cells appear to be vulnerable to neurotoxic insults. As a result, the protein is released into the cerebrospinal fluid (CSF), and can be used as a biomarker for stroke and Alzheimer’s disease.

Supplier: STEMCELL Technologies

Interleukin 9 (IL-9) has pleiotropic functions in the immune system and signals through its specific IL-9 receptor (IL-9R) (Renauld et al.). IL-9/IL-9R signaling pathway mainly targets the downstream activation of JAK/STAT (janus kinase/signal transducer and activator of transcription) and subsequent phosphorylation cascades initiated by multiple kinases including IRS–PI3K–PKB (insulin receptor substrate, phosphatidyl-inositol 3-kinases, protein kinase-B) and ERK (Knoops and Renauld; Fontaine et al.). IL-9 has been shown to have a role in Th1/Th17-mediated inflammation and in regulatory T cell responses (Singh et al.; Goswami and Kaplan). IL-9/IL-9R signaling pathway represents a novel endogenous anti-apoptotic mechanism for cortical neurons (Fontaine et al.). IL-9 secreting T cells, termed Th9 cells, contribute to both effective immunity and immunopathological disease, and have been shown to have a role in the treatment of allergic and autoimmune disease (Kaplan et al.).

Supplier: Adipogen

CD80 (B7-1) and CD86 (B7-2) together with their receptors CD28 and CTLA-4 constitute one of the dominant costimulatory pathways that regulate T cell and B cell responses. 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 and is involved in the down-regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells, and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through interferon-gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. It has been observed that both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.

Supplier: ADVANCED BIOMATRIX, INC. MS

Fibronectin is a widely used broad range natural cell attachment factor. This product has been purified from human plasma where it is found as a dimer and has a size of 440-500 kDa with two similar subunits (220-250 kDa ) linked by two disulfide bonds.

Fibronectin’s primary function is related to cell adhesion and attachment to extracellular matrix. Certain domains of Fibronectin have been found to play important roles that involve interactions with collagen, heparin and other cell surface glycosaminoglycans (GAGs).

Fibronectin is ideal for coating of surfaces and is typically used at a concentration of 1-5 µg/cm2 . It is provided in user-friendly packaging for use and storage. Fibronectin is sterile filtered and is supplied as a sterile, lyophilized product.

Supplier: STEMCELL Technologies

Basic fibroblast growth factor (bFGF) is a prototypic member of the fibroblast growth factor family. Cytokines in the FGF family possess broad mitogenic and cell survival activities (Folkman and Klagsbrun; Kimelman and Kirschner) and are involved in a variety of biological processes including cell proliferation, differentiation, survival, and apoptosis (Folkman and Klagsbrun; Klagsbrun; Rifkin and Moscatelli). bFGF has the β-trefoil structure (Ponting and Russell), binds to the four FGF receptor (FGFR) family members, and activates JAK/STAT, PI3K, ERK1/2, and other receptor tyrosine kinase (RTK) signaling pathways. It supports the maintenance of undifferentiated human embryonic stem cells (Xu et al.; Kang et al.), stimulates human embryonic stem cells to form neural rosettes (Zhang et al.), and improves proliferation of human mesenchymal stem cells and enhances chondrogenic differentiation (Solchaga et al.).

Supplier: Adipogen

CD86 (B7-2) is a 60-100 kDa variably glycosylated protein in the B7 family. B7 family members are transmembrane cell surface molecules that play important roles in immune activation and the maintenance of immune tolerance. B7-2 is highly expressed on activated antigen presenting cells (APC), e.g. B cells, dendritic cells and monocytes as well as on vascular endothelial cells. B7-2 and the closely related CD80 (B7-1) exhibit overlapping but distinct functional properties. Their binding to CD28, which is constitutively expressed on T cells, enhances T cell receptor signaling and also provides TCR-independent costimulation. B7-1 and B7-2 additionally bind the CD28-related protein CTLA-4, which is up-regulated and recruited to the immunological synapse (IS) at the onset of T cell activation. CTLA-4 ligation inhibits the T cell response and supports regulatory T cell function. B7-2 is expressed earlier than B7-1 following APC activation and both proteins bind with higher affinity to CTLA-4 than to CD28. B7-2 promotes the stabilization of CD28 in the IS, while B7-1 is primarily responsible for promoting CTLA-4 recruitment and accumulation in the IS. The relative participation of B7-1 and B7-2 in T cell costimulation can also alter the Th1/Th2 bias of the immune response. Both B7-1 and B7-2 serve as cellular receptors for B species adenoviruses.

Supplier: Adipogen

Human CD137 (4-1BB) is a costimulatory molecule of the tumor necrosis factor (TNF) receptor superfamily. The glycoprotein 4-1BB is expressed mainly on activated CD4+ and CD8+ T cells and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor receptor-associated factors (TRAF), the adaptor protein and mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T cell activation and growth as well as monocyte proliferation and B cell survival, and plays a important role in the amplification of T cell-mediated immune responses. In contrast, it can also enhance activation-induced T cell apoptosis when triggered by engagement of the TCR/CD3 complex. In addition, the 4-1BB/4-1BBL costimulatory pathway has been shown to augment secondary CTL responses to several viruses and increase antitumor immunity. 4-1BB is therefore a promising candidate for immunotherapy of human cancer.

Supplier: STEMCELL Technologies

Oncostatin M (OSM) is a member of interleukin 6 (IL-6) family of cytokines and bears close resemblance to leukemia inhibitory factor (LIF) and granulocyte colony-stimulating factor (G-CSF) in amino acid sequence and its modulation of differentiation in a variety of cell types (Rose and Bruce). OSM signals through type I receptor (consisting of gp130 and LIF receptor [LIFR]) and type II receptor (consisting of gp130 and OSM receptor [OSMR]), which eventually activate the JAK/STAT pathway (Auguste et al.; Gómez-Lechón). OSM is primarily produced by activated T cells and monocytes, and also by activated macrophages, neutrophils, mast cells, and dendritic cells. OSM is also produced within the bone microenvironment by cells of both hematopoietic and mesenchymal origin, including osteocytes and osteoblasts. OSM is involved in differentiation, cell proliferation, hematopoiesis, and inflammation, and also has been shown to have implications in liver development and bone formation and resorption (Sims and Quinn; Tanaka and Miyajima). This product is animal component-free.

Supplier: BioVendor

Regenerating (Reg) gene family belongs to the calcium depending lectin gene super family. It represents a group of small, multi‑functional secreted proteins, which can function as acute phase reactants, lectins and anti‑apoptotic or growth agents. These agents play an important role in proliferation and differentiation in the entire GI tract. The Reg family consists of seven members in mice (Reg I, Reg II, Reg IIIa, Reg IIIb, Reg IIId and Reg IIIge and Reg IV). Four members are recognized in humans (Reg Ia, Reg Ib, Reg III and Reg IV), but there are most probably a few more. Reg genes are up‑regulated following tissue injury, and play a major role in the healing of gastrointestinal mucosal lesions. Different members of the Reg gene family were shown to be expressed in pancreatic, gastric and colorectal cancers, and may serve as markers for poor prognosis. Reg IV, a novel member of the family, was suggested to play an important role in initiating the multi‑step process of colorectal cancer carcinogenesis, at the level of adenoma, by increasing the resistance for programmed cell death. Regenerating gene family member 4 (REG4) was originally identified by sequencing of a cDNA library derived from patients with inflammatory bowel disease.

Supplier: ADVANCED BIOMATRIX, INC. MS

RatCol® Type I Acid Soluble Rat Tail Collagen contains 100 mg at a concentration of approximately 4 mg/mL in a 0.02M acetic acid solution (pH 2 to 3). RatCol® collagen is soluble telo-collagen. Each product includes a bottle containing 100 mg of collagen solution accompanied with a bottle of pre-formulated neutralizing solution for the formation of a collagen gel. This collagen product is provided in user-friendly packaging for use and storage. This product is sterile filtered and is supplied as a ready to use solution. The concentration for each specific lot is provided on the product label and on a Certificate of Analysis that is available with the purchase of each product.

This product is ideal for coating of surfaces, providing preparation of thin layers for culturing cells, or use as a solid gel. RatCol® collagen is suitable for applications using a variety of cell lines including hepatocytes, fibroblasts and epithelial cells.

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 Sjögren’s syndrome, Rheumatoid Arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE) . BAFF is also increased levels in some lymphoid cancers.

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: STEMCELL Technologies

Interleukin 15 (IL-15) is a four-alpha helix bundle cytokine with many similar properties to IL-2, with which it shares components of its receptor. The IL-15 receptor is a heterotrimeric receptor composed of IL-15Ra, the high-affinity receptor for IL-15, as well as IL-2/15Rb (CD122) and common gamma chain (CD132). IL-15 binds to IL-15Rα receptor and can then be presented in trans to IL-2/15Rb and common gamma chain on other cells. Trans-presentation is thought to be the major mechanism by which IL-15-mediated responses occur in mice, although may not be necessary in humans (Castillo et al.). The cytoplasmic domains of IL-2/15Rb and common gamma chain mediate signaling to activate JAK/STAT and PI3K pathways. IL-15 supports the survival and proliferation of naive CD4+ and CD8+ T cells, and promotes homeostasis of memory T cells. IL-15 also promotes the survival and differentiation of NK cells and regulates their cytolytic activity (Ma et al.).

Supplier: Adipogen

Interleukin-21 (IL-21) is a key factor in the transition between innate and adaptive immune responses secreted by activated T cells. The IL-21 receptor (IL-21R) is expressed in lymphoid tissue, in particular by NK, B, T and dendritic cells, macrophages and endothelial cells. Recent evidence suggests that IL-21 plays a supportive role in the proliferation of T and B cells and influences the cytolytic activity of natural killer cells. IL-21 has been shown to up-regulate genes associated with innate immunity and to inhibit the differentiation of naïve T helper cells. IL-21 specifically inhibits IFN-gamma production from developing TH1 cells and is preferentially expressed by TH2 cells. Furthermore IL-21 has been identified as a growth and survival factor for human myeloma cells. IL-21/IL-21R interactions have a unique role in sequentially activating both innate and adaptive immune responses against poorly immunogenic tumors, leading to tumor rejection that is perforin dependent but IFN-gamma independent.

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: Adipogen

Interleukin-27 (IL-27) is a heterodimeric group 2 receptor ligand molecule that belongs to the IL-6/IL-12 family of long type I cytokines. It is composed of EBI3 (EBV-induced gene 3), a 34 kDa glycoprotein that is related to the p40 subunit of IL-12 and IL-23, and p28, the cloned 28 kDa glycoprotein that is related to the p35 chain of IL-12. IL-27 is expressed by monocytes, endothelial cells and dendritic cells. IL-27 binds to and signals through a heterodimeric receptor complex composed of WSX1 (TCCR) and gp130. Evidence suggests IL-27 interacts only with WSX-1. IL-27 has both anti- and proinflammatory properties. As an antiinflammatory, IL-27 seems to induce a general negative feedback program that limits T and NK-T cell activity. At the onset of infection, IL-27 induces an IL-12 receptor on naïe CD4+ T cells, making them susceptible to subsequent IL-12 activity (and possible Th1 development). Notably, IL-12 family cytokines are both induced and inhibited by bacterial products. Microbes promote IL-27 secretion through TLR4, and also block IL-27 production via C5a induction.

Supplier: Adipogen

Interleukin-33 (IL-33; HF-NEV; IL-1F11), a member of the IL-1 family of cytokines, is expressed by many cell types following pro-inflammatory stimulation and is thought to be released upon cell lysis. IL-33 binds to and signals through ST2 (IL-1R1) and its stimulation recruits MYD88, IRAK, IRAK4 and TRAF6, followed by phosphorylation of ERK1 (MAPK3) / ERK2 (MAPK1), p38 (MAPK14) and JNK. The ability of IL-33 to target numerous immune cell types, like Th2-like cells, mast cells and B1 cells, and to induce cytokine and chemokine production underlines its potential in influencing the outcome of a wide range of diseases, such as arthritis, asthma, atopic allergy & anaphylaxis, cardiovascular disease/atherosclerosis, nervous system diseases and sepsis. IL-33 facilitates Treg expansion in vitro and in vivo. Recently, IL-33 has been involved in adipocyte differentiation. The biological activity of IL-33 at its receptor ST2 is rapidly terminated in the extracellular environment by its oxidation (formation of two disulfide bridges), resulting in an extensive conformational change that disrupts the ST2 binding site. Mutations at amino acids C208S/C232S protect IL-33 from oxidation and increase its activity.

Supplier: STEMCELL Technologies

Interleukin 21 (IL-21) is a pleiotropic cytokine that is composed of four α-helical bundles and primarily produced by natural killer T (NKT) cells, T follicular helper (Tfh) cells, and Th17 cells (Spolski and Leonard 2008). IL-21 signals via heterodimers of the IL-21 receptor (IL-21R) and the IL2RG encoded common cytokine receptor γ-chain (Parrish-Novak et al.; Ozaki K et al. 2000), and utilizes the JAK/STAT, MAPK, and PI3K pathways (Spolski and Leonard 2014). IL-21 has been shown to have a critical role in regulating immunoglobulin production and differentiation of the pro-inflammatory Th17 population of cells (Ozaki et al. 2002; Nurieva et al.). Additionally, IL-21 specifically sustains CD8+ T cell effector activity and provides a mechanism of CD4+ T cell help during chronic viral infection (Elsaesser et al.). IL-21 signaling was also found critical for the development of type 1 diabetes in NOD mice (Sutherland et al.) and control of T cell autoimmunity by regulatory B cells (Yoshizaki et al.).

Supplier: Adipogen

Recombinant human soluble vascular endothelial growth factor receptor-1 (sVEGFR-1) is the naturally occurring form and is a glycosylated monomeric protein. The biological function of sVEGFR-1 seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. VEGFR-1 is a tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis and cancer cell invasion. It may play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. It can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). It has a very high affinity for VEGFA and relatively low protein kinase activity. It may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of phospholipase C-gamma (PLCG) leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1 and may also phosphorylate CBL.

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 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. 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: 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 p65-c-Rel complexes are transcriptional activators. The NF-kappaB p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappaB complex.

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, nitric oxide, 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.).

Supplier: Adipogen

CD276 (B7-H3) is a member of the B7/CD28 superfamily of costimulatory molecules serving as an accessory modulator of T cell response. B7 family molecules, which are expressed on antigen-presenting cells and display extracellular regions containing immunoglobulin (Ig) variable (V)- and constant (C)-like domains, are known to modulate T cell receptor (TCR)-mediated T cell activation by providing co-signals that are either stimulatory or inhibitory. B7-H3 provides a stimulatory signal to T cells. However, recent studies suggest a negative regulatory role for B7-H3 in T cell responses. B7-H3 inhibited T cell proliferation mediated by antibody to T cell receptor or allogeneic antigen-presenting cells. B7-H3 is a negative regulator that preferentially affects T(H)1 responses. B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. Recently, B7-H3 expression has also been found in a variety of different human cancers, including prostate cancer, clear cell renal cell carcinoma (ccRCC), non-small-cell lung cancer (NSCLC), pancreatic cancer, gastric cancer, ovarian cancer, colorectal cancer (CRC) and urothelial cell carcinoma. B7-H3 was expressed in some human cancers and correlated with poor outcome of cancer patients.