2421 Results for: "STEMCELL Technologies"

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Immunomagnetic isolation of untouched mouse neutrophils

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Stimulating T cells with EBV (LMP1) Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. EBV (LMP1) Peptide pool is a lyophilised mixture of 94 peptides from latent membrane protein 1 (LMP1) of Epstein-Barr virus (EBV; strain B95-8), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 386 on LMP1. LMP1 is essential for EBV-mediated growth transformation of B cells (Kaye et al.) and has been shown to downregulate toll-like receptor 9 (TLR9) expression in infected cells, a mechanism the virus may use to escape host innate immune recognition (Fathallah et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

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Use resistin to modulate various cellular responses, such as promoting neutrophil extracellular trap (NET) formation (Jiang et al.) and regulating anti-inflammatory signaling pathways through toll-like receptor 4 (TLR4) (Jang et al., 2017). A member of the resistin-like molecule (RELM) family, resistin is produced by adipocytes in mice, and has been implicated in insulin resistance, reducing glucose tolerance, and insulin sensitivity in vivo (Li et al.). In humans, resistin is expressed predominantly in leukocytes, modulating inflammation in numerous diseases (Jamaluddin et al.; Jang et al., 2015; Mantula et al.). Studies also show that resistin facilitates vascular endothelial growth factor (VEGF)-A-dependent angiogenesis in human chondrosarcoma cells, highlighting it as a promising target for chondrosarcoma angiogenesis (Chen et al.). For consistency and reproducibility across your applications, resistin from STEMCELL comes lyophilised with ≥95% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.

Supplier: STEMCELL Technologies

Commonly known as vaspin, Serpin A12 is an adipokine that is thought to perform insulin-sensitizing functions, such as the regulation of kallikrein 7 (KLK7), an insulin-inhibiting protease (Heiker et al.). The Serpin A12 glycoprotein belongs to the serine protease inhibitor family (serpin), and is mainly associated with obesity, insulin resistance, and glucose metabolism, but may also protect against high fat-induced bone loss (Wang et al.). Serpins share a highly conserved core structure with multiple α-helices, β-strands, and a reactive site loop (RCL) to interact with the target protease (Huntington). It is expressed predominantly in visceral adipose tissue and at significantly higher amounts in obese individuals (Kurowska 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 ≥94% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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Use angiopoietin-like protein 2 (ANGPTL2) to regulate tissue remodeling through integrin α5β signaling and activation of p38 mitogen-activated protein kinases (MAPK) (Odagiri et al.; Tabata et al.). Highly expressed in the heart, small intestine, and stomach, ANGPTL2 is a glycosylated secretory protein that contains a coiled domain and a fibrinogen-like domain (Kim et al.). Studies have shown that the coiled-coil domain of ANGPTL2 functions as a growth factor, enhancing the survival of hematopoietic stem cells (HSCs) ex vivo (Broxmeyer et al.). ANGPTL2 is also known to play a role in obesity and metabolic diseases, promoting local inflammation in adipose tissue and systemic insulin resistance in mice models (Tabata et al.). By activating an inflammatory cascade in endothelial cells and increasing macrophage infiltration, ANGPTL2 accelerates vascular inflammation which may lead to endothelial dysfunction and atherosclerosis progression (Horio et al.). This protein product contains a His-residue tag at the amino end of the polypeptide chain. For consistency and reproducibility across your applications, sclerostin from STEMCELL comes lyophilised with ≥92% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

Supplier: STEMCELL Technologies

Stimulating T cells with SARS-CoV-2 (Spike Protein) Delta/B.1.617.2 Mutation 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 27 peptides from the spike glycoprotein of the SARS-CoV-2 Delta variant (B.1.617.2) that selectively cover the mutated regions in the spike protein. 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

Stimulating T cells with SARS-CoV-2 (Spike Protein) Omicron/B.1.1.529 Mutation 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 80 peptides of the spike glycoprotein of SARS-CoV-2 Omicron variant (B.1.1.529), these peptides selectively cover the mutated regions in the spike protein of the SARS-CoV-2 Omicron variant, compared to wild-type. 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

Stimulating T cells with JCV (LT) 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 170 peptides from large T antigen (LT) of JC polyomavirus (JCV), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 688 on LT. LT is detectable during JCV latency (Rossi et al.), and in immunocompromised patients with JVC-associated pathologies such as progressive multifocal leukoencephalopathy (PML) (Delbue et al.). In PML, LT has been associated with activating the promoter of survivin, an anti-apoptotic protein (Del Valle et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

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Methylcellulose-based medium with recombinant cytokines for human cells. 1×100 ml bottle.

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Animal component-free, defined cryopreservation medium with 10% DMSO.

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Dulbecco's Phosphate Buffered Saline with 2% fetal bovine serum is recommended for use as a buffer to dilute or wash nucleated cells.

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Immunomagnetic isolation of untouched mouse CD8+ T cells

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Serum-free medium for culture and expansion of hematopoietic cells.

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Immunomagnetic isolation of untouched human CD4+CD127lowCD49d- T cells

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Immunodensity isolation of untouched T cells.

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Immunomagnetic isolation of untouched non-human primate T cells

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cGMP, stabilized feeder-free maintenance medium for human ES and iPS cells.

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Immunomagnetic cell isolation kit using particle release technology.

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Immunomagnetic positive selection of human cells labeled with PE-conjugated antibodies.

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Immunomagnetic positive selection of human cells labeled with FITC-conjugated antibodies.

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Mouse monoclonal IgG1 antibody against human, rhesus, cynomolgus CD138 (syndecan-1), APC-conjugated.

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Immunomagnetic isolation of untouched mouse epithelial cells

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Culture supplement for the differentiation of human naïve CD4+ T cells into Th1 cells.

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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.).

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Immunomagnetic positive selection of human CD33+ and CD66+ cells (e.g. myeloid cells).

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Serum- and BPE-free medium for human small airway epithelial cells cultured at the air-liquid interface.

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R-Spondin-1 (RSPO1) is the prototype member of the R-Spondin (RSPO) protein subfamily of a superfamily of thrombospondin type 1 repeat (TSR-1)-containing proteins (Chen et al.; Kamata et al.; Kazanskaya et al.; Kim et al.). Although unable to initialize signaling, RSPO family members are potent enhancers of WNT signaling (Cruciat and Niehrs; de Lau et al.; Kamata et al.; Kazanskaya et al.). They are characterized by a TSR-1 domain, a carboxy-terminal region with positively charged amino acids, and two N-terminal furin-like cysteine-rich repeats (Glinka et al.; Kazanskaya et al.). R­-Spondin-1 activates β­-catenin signaling via the WNT signaling cascade and by indirectly increasing low-density lipoprotein receptor-related protein 6 (LRP6) on the cell surface. It does this by binding leucine-rich repeat-containing G-protein-coupled receptor 5 (LGR5), and competing with WNT antagonist DKK­1 for binding to the WNT co­receptors, Kremen and LRP­6, which reduces DKK­1-­mediated internalization of LRP6 (Binnerts et al.). RSPO1 is involved in a wide range of pleiotropic roles during embryogenesis, it is required for the specification of hematopoietic stem cells, and it has been shown to be important in the growth, survival, and migration of ovarian cancer cells (Cruciat and Niehrs; de Lau et al.; Genthe and Clements; Liu et al.).

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Bone morphogenetic protein 4 (BMP-4) is a member of the highly conserved transforming growth factor β (TGF-β) superfamily. Mature BMP-4 is a disulfide-linked homodimeric protein consisting of two 116-amino-acid residue subunits, and is generated by the proteolytic removal of the signal peptide and propeptides (Xiao et al.). BMP-4 binds to type I and type II receptors on cells. This binding results in the phosphorylation of receptor 1, which in turn results in the phosphorylation of Smad proteins, which then go on to act as transcription factors (Zhang et al.). BMPs have been shown to be key regulators of embryogenesis and are known to play a role in the growth and differentiation of various cell types, including embryonic stem (ES) cells, induced pluripotent stem (iPS) cells, mesenchymal cells, epithelial cells, hematopoietic cells, and neuronal cells (Chadwick et al.; Graham et al.; Jones et al.; Lengerke et al.; Zhang et al.).

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Amine-labelling fluorescent dye for live/dead staining of mammalian cells - 100 tests.

Supplier: STEMCELL Technologies

Column-free immunomagnetic positive selection of human B cells for HLA analysis.