You searched for: Proteins and Peptides

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, 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: 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 progenitors (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 mobilisation 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.). This product is animal component-free.

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: 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.

Supplier: Serva

Pepstatin A

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Bovine aprotinin (from Lung)

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Bovine serum albumin (BSA)

Supplier: Serva

Bovine serum albumin (BSA), Fraction V

Supplier: Roth Carl

Bovine serum albumin (BSA), Fraction V

Supplier: Roth Carl

Bovine serum albumin (BSA), Fraction V

Supplier: STEMCELL Technologies

A cellular protein for detection of apoptotic cells, FITC-conjugated.

Supplier: STEMCELL Technologies

Stimulating T cells with EBV (HLA Class I Control) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. EBV (HLA Class I Control) Peptide Pool is a lyophilised mixture of 26 peptides from Epstein-Barr virus (EBV), and consists of defined HLA class I-restricted T cell epitopes. Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development. For consistency and reproducibility across your applications, CMV peptide pool from STEMCELL has a purity ≥95%.

Supplier: STEMCELL Technologies

Stimulating T cells with HHV1 (gD) Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. HHV1 (gD) Peptide pool is a lyophilised mixture of 96 peptides from envelope glycoprotein D of human herpesvirus 1 (HHV1; strain Patton), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 394 on gD. gD is required at the first stage of virus-induced membrane fusion (Subramanian and Geraghty), which likely occurs via binding to receptors such as nectin-1 (Giovine et al.) and HVEM (Connolly et al.) on cell surfaces. Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

Supplier: STEMCELL Technologies

Stimulating T cells with EBV (EBNA-3B) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. EBV (EBNA-3B) Peptide Pool is a lyophilised mixture of 234 peptides from Epstein-Barr nuclear antigen 3B (EBNA-3B) of Epstein-Barr virus (EBV; strain AG876) and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 946 on EBNA-3B. EBNA-3B is considered non-essential for B cell growth transformation (Chen et al., 2005; Tomkinson and Kieff), but has been shown to regulate the expression of cellular genes in EBV-infected cells (Chen at al., 2006). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

Supplier: STEMCELL Technologies

Transforming growth factor-alpha (TGF-α) a member of the epidermal growth factor (EGF) family that is expressed in normal epithelial cells, monocytes, macrophages, brain cells, keratinocytes, and cancer cells. TGF-α binds EGF receptor (EGFR) and activates tyrosine kinase signaling. In epidermal and epithelial cells, this results in proliferation and differentiation. TGF-α is not structurally or genetically related to TGF-β, and the two ligands act through different signaling pathways. In vitro, TGF-α was shown to stimulate anchorage-independent growth (Singh and Coffey).

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Bone morphogenetic protein 2 (BMP-2) is a member of the transforming growth factor beta (TGF-β) superfamily. BMP-2 is a disulfide-linked homodimer, acts as a ligand for complexes of type I and II BMP receptors, and primarily activates SMAD1/5/8 signaling (Nohe et al.). BMP-2 is a potent differentiation factor and directs human pluripotent stem cells (hPSCs) towards various cell types including extra-embryonic endoderm, mesenchymal cells, and chondrocytes (Pera et al.). Although BMP-2 expression is low in healthy cartilage, its expression is upregulated at the site of cartilage damage (Blaney Davidson et al.). BMP-2 induces bone and cartilage formation in vitro and is able to induce chondrogenesis in human mesenchymal stem cells (Schmitt et al.).

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R-Spondin-3 is a member of thrombospondin type 1 repeat (TSR-1) superfamily that is involved in the canonical Wnt/β-catenin signaling pathway (de Lau et al.). R-spondin proteins are characterized by two furin-like repeats at the amino terminus and thrombospondin domain located near the carboxyl terminus (de Lau et al.). R-spondin-3 expression is associated with ovarian cancer (Gu et al.), prostate cancer (Mesci et al.), and differentiation of intestinal epithelial cells in diabetes mellitus (Shan et al.). In a transgenic mice model, the expression of R-Spondin-3 induces the expansion of Lgr5+ stem cells, Paneth cells, and Lgr4+ cells, promoting the intestinal stem cell compartment (Hilkens et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain.

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Fibroblast growth factor 8A (FGF-8A) is a member of the fibroblast growth factor (FGF) family and is an isoform of FGF-8. FGF-8A binds the FGF receptor (FGFR) and activates Ras/MAPK signaling (Hulstrand and Houston). The FGF family possesses broad mitogenic and cell survival activities (Folkman and Klagsbrun; Kimelman and Kirschner) and is involved in a variety of biological processes, including cell proliferation, differentiation, survival, and apoptosis (Folkman and Klagsbrun; Klagsbrun; Rifkin and Moscatelli). FGF-8 RNA is spliced to produce 4 protein isoforms in humans: FGF-8A, FGF-8B, FGF-8E, and FGF-8F. The functional differences are not fully understood; however, studies in zebrafish and Xenopus show that FGF-8A is required for endoderm morphogenesis and neurogenesis (Choe and Crump; Hulstrand and Houston).

Supplier: STEMCELL Technologies

Activin A is a member of the transforming growth factor beta (TGF-β) family of proteins produced by many cell types throughout development (Gurdon et al.). It is a disulfide-linked homodimer (two beta-A chains) that binds to heteromeric complexes of a type I (Act RI-A and Act RI-B) and a type II (Act RII-A and Act RII-B) serine-threonine kinase receptor (Attisano et al.). Activins primarily signal through SMAD2/3 proteins to regulate a variety of functions, including cell proliferation, differentiation, wound healing, apoptosis, and metabolism (McDowell et al.). Activin A maintains the undifferentiated state of human embryonic stem cells (James et al.; Xiao et al.) and also facilitates differentiation of human embryonic stem cells into definitive endoderm (D’Amour et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Growth differentiation factor 11 (GDF-11) is a member of transforming growth factor beta (TGF-β) family. It binds to the TGF-β receptors ALK4, ALK5, and ALK7 and activates the SMAD signaling pathway (Ho et al.). GDF-11 regulates the development of the olfactory system, retina, and pancreas, as well as anterior/posterior patterning of the axial skeleton (Lee and Lee). GDF-11 is an endocrine factor expressed in skeletal muscle, brain, and dental pulp (Kondás et al.). Studies in mice showed that GDF-11 regulates muscle and cardiac aging, and stimulates neurogenesis by remodeling blood vessels (Katsimpardi et al.; Loffredo et al.; Sinha et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Macrophage inflammatory protein-4 (MIP-4) plays a role in adaptive and innate immune responses, acting as a chemoattractant for T and B lymphocytes, and natural killer cells (Krohn et al.). MIP-4 can also induce immune tolerance through its effects on dendritic cells and macrophages (Azzaoui et al., Schraufstatter et al.). In breast cancer, MIP-4 has been shown to promote the invasiveness and metastasis of cancer cells in vivo by binding PITPNM3 (Chen et al.).This small cytokine belongs to the chemokine family found only in primates. Based on amino acid sequence, MIP-4 is closely related to MIP-1 alpha (CCL3) and MIP-1 beta (CCL4) (Liang et al.). MIP-4 is produced by antigen-presenting immune cells including dendritic cells, macrophages, and monocytes (Lieshout et al.). For consistency and reproducibility across your applications, macrophage inflammatory protein-4 from STEMCELL comes lyophilised with ≥95% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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Interferon-alpha (IFN-α) is a type I interferon, produced by virus-infected cells, and is released as a soluble factor to initiate antiviral responses (Isaacs and Lindenmann). IFN-α2 is the most potent IFN-α used in fundamental research and in most clinical applications. The best-known IFN-α2 subvariants, 2A and 2B, differ by only one or two amino acids at positions 23 and/or 34 of the mature protein (von Gabain et al.). Type I IFNs exert potent antitumor activity by increasing the cytotoxic activity of NK and T cells, as well as by inhibiting the proliferation of cancer cells (Paul et al.). Additionally, it has been shown that proinflammatory IFN-α modulates the function of B cells in patients with systemic lupus erythematosus (Chang et al.), and pegylated forms of IFN-alpha 2A and 2B have implications in the treatment of hepatitis C (Foster et al.).

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 pluripotent stem cells (Xu et al.; Kang et al.), stimulates human pluripotent stem cells to form neural rosettes (Zhang et al.), and improves proliferation of human mesenchymal stem cells and enhances chondrogenic differentiation (Solchaga et al.). This version of bFGF is the full-length bFGF protein encoded by the human FGF2 gene consisting of 154 amino acid residues. This product is animal component-free.

Supplier: STEMCELL Technologies

Receptor activator of nuclear factor kappa-B ligand (RANKL) is a member of the tumor necrosis factor (TNF) superfamily (Anderson et al.). Cytokines in the TNF superfamily are involved in a variety of long-term cellular activities such as differentiation, proliferation, and cell death (MacEwan). RANKL is a type II homotrimeric transmembrane protein expressed in both a membrane-bound and secreted form (Ikeda et al.). RANKL binds to the receptor activator of nuclear factor kappa-B (RANK). Upon binding to its receptor, RANKL activates the AKT signaling pathway (Moon et al.). Osteoprotegerin (OPG) may also bind RANKL, and this binding competes with RANKL-RANK binding (Lacey et al.). RANKL is involved in osteoclastogenesis (Lacey et al.; Yasuda et al.) and T cell activation (Wong et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Use omentin for the maintenance of insulin sensitivity and metabolism, decreasing levels of this adipokine have been associated with obesity, insulin resistance, and diabetes (Tan et al.). Studies have suggested that omentin may have protective effects against atherosclerosis, arterial calcification, and myocardial injury through AMP-activated protein kinase (AMPK) and Akt-dependent mechanisms (Xu et al., Kataoka et al.). Through regulation of Sirt1-dependent p53 deacetylation, omentin can inhibit proliferation and induce apoptosis in hepatocellular carcinoma cells (Zhang and Zhou). Omentin is mainly produced by visceral adipose tissue, but is also expressed in the small intestine, colon, mesothelial cells, vascular cells, and plasma (Watanabe et al). Protein sequence analysis has shown that omentin comprises 313 amino acids, with a secretory signal sequence and fibrinogen-related domain (Yang et al.). For consistency and reproducibility across your applications, Omentin from STEMCELL comes lyophilised with ≥90% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤5,0 EU/μg protein.

Supplier: STEMCELL Technologies

Interleukin 7 (IL-7) is a member of the type I cytokine family that is critical for T and B cell development and survival. It is produced by non-hematopoietic cells in the thymus, lymphoid organs, and by bone marrow stromal cells (Lundström et al.). IL-7 binds to a receptor (IL-7R) composed of common gamma chain and IL-7Ra (CD127) and signals through the JAK/STAT and PI3K pathways. IL-7 regulates the survival of naïve and memory CD4+ and CD8+ T cells, γδ T cells, NK T cells, innate lymphoid cells, and regulatory T cells (Carrette and Surh). Although a deficiency in IL-7R still permits the generation of normal numbers of peripheral B cells in humans, stimulation of human B cell precursors with IL-7 could promote STAT5-dependent proliferation and survival in vitro (Clark et al.; Corfe and Paige). This product is animal component-free.

Supplier: STEMCELL Technologies

Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils, and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation, and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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Interleukin 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to a heterotrimeric receptor consisting of CD25, CD122, and CD132. Upon binding, it activates JAK3-, STAT5-, and AKT-dependent signaling pathways, which results in cellular proliferation and survival (Ma et al.). The majority of IL-2 is secreted by activated CD4+ and CD8+ T cells, although B cells and dendritic cells were found to produce IL-2 in small amounts. IL-2 downregulates immune responses to prevent autoimmunity during thymic development, influences the development of CD4+CD25+ regulatory T cells, and affects development of follicular helper T cells. IL-2 also controls inflammation by inhibiting Th17 differentiation (Banchereau et al.). Targeted deletions of the IL-2 gene in mice resulted in development of autoimmune hemolytic anemia, followed by ulcerative colitis. Similar effects were observed in mice that were deficient in IL-2 receptor α (Gaffen and Liu).

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Fibroblast growth factor 21 (FGF-21) is a member of the FGF family. Using β-Klotho as a cofactor, FGF-21 signals through FGF receptor 1c and 4 to activate PI3K and MAPK pathways (Mattila and Härkönen; Kharitonenkov et al.). FGF-21 expression is regulated by tissue-specific peroxisome proliferator-activated receptors (PPARs). Upon PPAR-α stimulation FGF-21 is produced in the liver, and activation of PPAR-γ leads to FGF-21 production in adipose tissue. FGF-21 promotes insulin-independent glucose uptake and lipid accumulation in primary human adipocytes and in mouse 3T3-L1 cells. In pancreatic islets and INS-1 cells it inhibits glucose-mediated glucagon release and stimulates insulin production. FGF-21 does not induce proliferation in immortalized cell lines, unlike other FGFs (Kharitonenkov and Shanafelt). FGF-21 regulates thermogenesis in white and brown adipose tissue, and metabolic processes in cells of pancreatic origin (Kharitonenkov et al.).

Supplier: STEMCELL Technologies

Interleukin 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to heterotrimeric receptors consisting of CD25, CD122, and CD132. Upon binding, it activates JAK3-, STAT5-, and AKT-dependent signaling pathways, which results in cellular proliferation and survival (Ma et al.). The majority of IL-2 is secreted by activated CD4+ and CD8+ T cells, although B cells and dendritic cells were found to produce IL-2 in small amounts. IL-2 downregulates immune responses to prevent autoimmunity during thymic development, influences the development of CD4+CD25+ regulatory T cells, and affects development of follicular helper T cells. IL-2 also controls inflammation by inhibiting Th17 differentiation (Banchereau et al.). High IL-2 levels in serum are associated with progression of scleroderma, rheumatoid arthritis, and gastric and non-small cell lung cancer, though no known disease can be directly attributed to the lack or excess of IL-2 (Gaffen and Liu).