2421 Results for: "STEMCELL Technologies"

Supplier: STEMCELL Technologies

Butyrophilin 1A1 (BTN1A1) is a glycoprotein belonging to the butyrophilin (BTN) family which collectively modulates immune responses, through excitatory and inhibitory signals targeting immune cells. Butyrophilins are composed of two extracellular immunoglobulin domains and a transmembrane region, with a conserved B30.2 domain (PRYSPRY) that is present in most members (Malinowska et al.). BTN1A1, along with BTN2A2, has been shown to inhibit the proliferation of CD4+ and CD8+ T cells, modify T cell metabolism, and affect the expression of IL-2 and IFN-γ (Smith et al.). Due to these modulatory effects on T cells, BTN1A1 may have a role in inhibiting the development of autoimmune diseases (Stefferl et al.). BTN1A1 is also expressed in mammary glands and is required for the secretion of milk lipids during lactation (Ogg et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, Serpin A12 from STEMCELL comes lyophilised with ≥92% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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 hepassocin to bind to lymphocyte-activation gene 3 (LAG-3) in an MHC class II independent manner, and inhibit antigen-specific T-cell activation (Wang et al.). Hepassocin is known to play a restorative role in the liver, reducing apoptosis and accelerating hepatocyte proliferation in vivo (Li et al.). In addition to these hepatoprotective effects, studies have shown that hepassocin expression is upregulated in gastric cancer tissues (Zhang et al.) and in breast cancer cells (Du et al.), suggesting it has potential to predict cancer disease progression. Hepassocin is a member of the fibrinogen superfamily, whose members share a fibrinogen domain at their C-terminus. It is predominantly expressed in the liver, and weakly in the pancreas (Hara et al.), and is secreted as a homodimer that consists of 312 amino acids. Hepassocin is an acute-phase reactant whose expression in HepG2 cells has been shown to be regulated by IL-6 (Liu and Ukomadu). This protein product contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, hepassocin from STEMCELL comes lyophilised with ≥87% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.

Supplier: STEMCELL Technologies

Apolipoprotein H (apo H) has been shown to promote the coagulation of blood platelets by inhibiting thrombomodulin complex and inactivating protein C (Keeling et al.), but can also act as an anticoagulant by binding thrombin and inhibiting its procoagulant effects (Pozzi et al.). Belonging to the lipid-binding apolipoprotein family, within the lipocalin superfamily, apo H is a protein constituent of plasma, with a high affinity for negatively charged phospholipids. The structure of apo H reveals four N-terminal complement control protein (CCP) modules, also known as 'sushi' domains, and a distinct fifth C-terminal domain with four antiparallel beta sheets, two alpha-helices, and an extended loop (Schwarzenbacher et al.). Apo H is the main antigen implicated in antiphospholipid syndrome (APS), an autoimmune condition involving pregnancy complications and vascular thrombosis (Brusch). Studies have also reported that Apo H is involved in the progression of atherosclerosis (Harats and George). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, apolipoprotein H from STEMCELL comes lyophilised with ≥93% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

Supplier: STEMCELL Technologies

Stimulating T cells with HPV18 (L2) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. A lyophilised mixture of 113 peptides from minor capsid protein L2 of human papillomavirus type 18 (HPV18), HPV18 (L2) peptide pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 462 on L2. With two nuclear localization signals, L2 may enter the nuclei of host cells via several import pathways mediated by Kap α2β1 heterodimers, Kap β2, and Kap β (Klucevsek et al.). L2 can also assemble into virus-like particles, and may have a role in encapsidation (Stauffer et al.). 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 SARS-CoV-2 (Spike Protein) Omicron/B.1.1.529 WT reference peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. This peptide pool is a lyophilised mixture of 82 peptides from the spike glycoprotein of the wild-type SARS-CoV-2 virus. Consisting of the wild-type peptides that correspond to the mutated portions of the spike protein found in the SARS-CoV-2 Omicron variant (B.1.1.529), this pool is recommended to be used as a reference for the SARS-CoV-2 (Spike Protein) Omicron/B.1.1.529 mutation peptide pool. Through interactions with the angiotensin-converting enzyme 2 (ACE2) receptor, the spike protein enables the virus to attach to the cell membrane, and plays a critical role in viral entry (Hoffmann et al.; Walls et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

Supplier: STEMCELL Technologies

For detection and measurement of mouse interleukin 12 and mouse interleukin 23 (p40) subunit.

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For detection and measurement of human interleukin 12 (p70) subunit.

Supplier: STEMCELL Technologies

For detection and measurement of mouse tumor necrosis factor-alpha.

Supplier: STEMCELL Technologies

Stimulating T cells with VZV (gE) Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. VZV (gE) Peptide pool is a lyophilised mixture of 153 peptides from the envelope glycoprotein E (gE) of Varicella-zoster virus (VZV; strain Dumas), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 623 on gE. gE is essential for VZV replication (Mo et al., 2002) and may contribute to viral pathogenesis by facilitating epithelial cell-cell contacts (Mo et al., 2000). 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 Clostridium (Tetanus Toxin) Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. Clostridium Peptide pool is a lyophilised mixture of 326 peptides from tetanus toxin of Clostridium tetani (strain Massachusetts/E88), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 1315 on tetanus toxin. Tetanus toxin entry into central neurons is mediated by the synaptic vesicle-binding protein SV2 (Yeh et al.), where it selectively cleaves synaptobrevin (Link et al.; Schiavo et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

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 T regulatory 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 STAT-5-dependent proliferation and survival in vitro (Clark et al.; Corfe and Paige).

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Stimulating T cells with HHV6 (U54) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. HHV6 (U54) peptide pool is a lyophilised mixture of 112 peptides from protein U54 of human herpesvirus 6B (HHV-6B; strain Z29), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 459 on U54. U54 is a tegument transactivator and is suggested to be a homolog of the CMV UL82/83 (pp65/72K) protein (Isegawa et al.; Nicholas). In infected T cells, U54 has been shown to inhibit gene transcription of interleukin 2 (IL-2), the T cell growth factor, which likely contributes to viral persistence (Iampietro et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

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

Stimulating T cells with VZV (IE63) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. VZV (IE63) peptide pool is a lyophilised mixture of 67 peptides from the transcriptional regulator ICP22 homolog (IE63) of Varicella-zoster virus (VZV; strain Oka vaccine), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 278 on IE63. Expressed during VZV latency and reactivation (Lungu et al.), IE63 demonstrates repressive activity in both the cytoplasm and nucleus of infected cells (Bontems et al.). Host interferon alpha (IFN-α) activity is inhibited by VZV IE63, which likely contributes to VZV pathogenesis (Ambagala and Cohen). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

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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. 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- 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.). It has been shown that PDGF-AB together with 5-Azacytidine (Catalog #72012), induces the conversion of mature bone and fat cells into tissue-regenerative multipotent stem cells (Chandrakanthan et al.).

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Follistatin, a glycosylated monomeric protein, is a modulator of transforming growth factor beta (TGF-β) superfamily signaling. It binds to and inhibits the function of activin, myostatin, growth differentiation factors, and bone morphogenetic proteins (BMP) (Hansen and Plomgaard). Follistatin inhibits mesoderm induction, suppresses synthesis and secretion of pituitary follicle-stimulating hormone, regulates liver regeneration, and causes infertility (Guo et al.; Iemura et al.). Follistatin exhibits anti-inflammatory effects, and it could be used as a biomarker in cancer (Hansen and Plomgaard).

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Insulin-like growth factor 1 (IGF-I) is a polypeptide that belongs to the family of insulin-like growth factors that are similar in molecular structure to proinsulin. IGF-I binds to the IGF-I receptor and is a potent activator of the PI3K/AKT pathway and also activates ERK1/2 signaling. IGF-I is required for embryonic development, and it is produced mainly in the liver in response to a hepatocyte growth hormone. In the absence of insulin, IGF-I is necessary for the maintenance of human pluripotent stem cells (Wang et al.). Together with IL-3, IGF-I stimulates differentiation and proliferation of myeloid cells and has been shown to regulate lymphopoiesis by stimulating proliferation and differentiation of T and B cells in lymphoid organs (Heemskerk et al.). This product is animal component-free.

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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.

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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 mobilisation of hematopoietic progenitor cells and used to treat 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.).

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Human Interleukin 4 (IL-4) is important for immune responses to helminth infection as well as in allergic responses (Olpihant et al.). The IL-4 receptor consists of a heterodimer of IL-4Ra and common gamma chain. IL-4 receptor engagement leads to the activation of JAK1/3 and the recruitment of STAT6 and IRS1/2 (Nelms et al.). IL-4 drives immunoglobulin class switching in B cells (to IgE, IgG4), mast cell hyperplasia, mucus production, and the differentiation of naïve T cells into T helper type 2 (Th2) cells, which produce IL-4, IL-5, IL-10, and IL-13 (Bao et al.; Olpihant et al.; Nelms et al.). In addition to Th2 T cells, IL-4 is produced by CD4+ NK T cells, γ/δ T cells, activated basophils, eosinophils, and mast cells. IL-4 consists of 130 amino acids with a predicted molecular weight of 15.1 kDa. Human IL-4 does not cross-react with mouse cells (Park et al.). This product is animal component-free.

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).

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Rat monoclonal IgG1 antibody against mouse CD25, PE-conjugated.

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Rat monoclonal IgG2a antibody against mouse CD138 (syndecan-1), unconjugated.

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Mouse monoclonal IgG1 antibody against human, rhesus, cynomolgus CD2, biotin-conjugated.

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Rat monoclonal IgM, kappa isotype control antibody, PE-conjugated.

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Rat monoclonal IgG2a, kappa isotype control antibody, PE-conjugated.

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Matrix for maintenance of human ES and iPS cells in combination with TeSR™ maintenance media.

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Mouse monoclonal IgG1 antibody against human MUC1 (CD227), unconjugated.

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Rat monoclonal IgG2b, kappa isotype control antibody, APC-conjugated.