2778 Résultats pour : "STEMCELL Technologies"

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Immunomagnetic depletion of human CD25+ cells.

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Immunomagnetic isolation of untouched rat B cells

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Immunomagnetic isolation of untouched human CD8+ T cells.

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cGMP, human T cell activation and expansion reagent.

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Immunomagnetic isolation of untouched human naïve CD8+ T cells

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Immunodensity isolation of untouched plasma cells for multiple myeloma research.

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Mouse monoclonal IgG2b antibody against human CD32, FITC-conjugated.

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Mouse monoclonal IgG1 antibody against human, chimpanzee CD22, APC­conjugated.

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Base methylcellulose medium for mouse cells.

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A non-integrating, self-replicating RNA reprogramming vector for generating iPS cells.

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Medium for maintenance and expansion of neural progenitor cells derived from human ES and iPS cells.

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Basal medium for human mesenchymal stem cells.

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Medium for long-term culture of human cells.

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For culture and evaluation of mouse mammary epithelial cells.

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Low-density lipoproteins pre-screened for hematopoietic cell growth.

Supplier: STEMCELL Technologies

Stimulating T cells with SARS-CoV-2 (Spike Protein) Omicron BA.4/BA.5 Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. This pool is provided as two lyophilised mixtures (subpools) from the spike glycoprotein of SARS-CoV-2 Omicron BA.4/BA.5 subvariant. The subpools contain 158 and 157 peptides, respectively, for a total of 315 peptides, and they consist of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 1270 on 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.

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Stimulating T cells with CMV (IE-1) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. CMV (IE-1) peptide pool is a lyophilised mixture of 120 peptides from the immediate early protein IE1 (IE1) of human cytomegalovirus (CMV; strain AD169), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 491 on IE1. CMV IE1 is a transcriptional transactivator and autoregulator (Cherrington and Mocarski). Studies show that IE1 promotes viral transcription by antagonizing histone deacetylation (Nevels et al.) and, along with IE2, may contribute to the survival of CMV-infected cells by blocking tumor necrosis factor alpha (TNF-α)-induced apoptosis (Zhu 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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Myostatin is a member of transforming growth factor beta (TGF-β) superfamily that signals by binding to activin type II receptor, resulting in the recruitment of either ALK3 or ALK4 coreceptor, and activation of SMAD2/3 (Kondás et al.). It is released by myocytes and inhibits muscle growth and ability to regenerate (Lee and Lee). Myostatin appears to affect the lipid catabolic metabolism of adipocytes and inhibits preadipocyte differentiation, as demonstrated in the 3T3-L1 cell line (Li et al.).

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Tumor necrosis factor-beta (TNF-β), also known as lymphotoxin-alpha, is a member of the TNF family. It is a pro-inflammatory cytokine that activates NF-kB, MAPK, and PI3K/AKT pathways upon binding to TNF receptors 1 and 2. It is produced mainly by T cells, though other cells can express TNF-β at lower levels (Chu). TNF-β is involved in autoimmune disorders, lymph node development, and mediating the inflammatory demyelination process (Seleznik et al.; McCarthy et al.).

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Stimulating T cells with CMV (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. CMV Peptide pool is a lyophilised mixture of 14 peptides from the human cytomegalovirus (CMV) 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 pools from STEMCELL are formulated as lyophilised trifluoroacetate salts, with a purity ≥95%.

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Human (Actin) peptide pool is a lyophilised mixture of 92 peptides from human actin, alpha skeletal muscle, and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 377 on actin. It is frequently used as a negative control. Actin, alpha skeletal muscle, is part of the highly conserved actin protein family and is the predominant isoform found in adult skeletal muscle (Laing et al.). Peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

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A member of the SIBLING family of glycoproteins (Rangaswami et al.), Osteopontin (OPN) functions as T-helper 1 cytokine, and plays an important role in cell signaling, migration, and activation (Weber et al., 2002). Osteopontin has been shown to regulate inflammation both in vitro and in vivo (Agnholt et al.; Kiefer et al.), and has been implicated in the pathophysiology of numerous cancers, including prostate (Thalmann et al.), lung (Chambers et al.), ovarian (Kim et al.), and breast etiologies (Weber et al., 2015). In humans, OPN is initially secreted as a 317 amino acid protein which is subject to tissue-specific post-translational modifications by glycosylation, phosphorylation, and transglutamination (Kazanecki et al.; Sodek 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, Osteopontin from STEMCELL comes lyophilised with ≥92% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.

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Stimulating T cells with HPV16 (E6) Peptide Pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. HPV16 (E6) Peptide Pool is a lyophilised mixture of 37 peptides from the E6 protein of human papillomavirus type 16 (HPV16). The pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 158 on protein E6. E6 binds to the tumor suppressor protein p53 and stimulates its degradation (Scheffner et al.; Werness et al. ), which is thought to cause an increase in spontaneous mutagenesis in host cells (Havre et al.). E6 together with E7 demonstrated the ability to immortalize human keratinocytes in vitro, which likely has significance for HPVs oncogenic potential (Hawley-Nelson 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 sclerostin to alter bone remodeling homeostasis, where it inhibits bone formation in vivo and in vitro, likely through Wnt/β-catenin signaling cascades (Ellies et al.; Lin et al.). Sclerostin is a member of the cerberus/DAN family of glycoproteins whose members share a C-terminal cysteine-knot-like (CTCK) domain. Highly expressed in bone and cartilage, as well as in kidney, and liver tissues (Weivoda et al.), this osteoclast-derived BMP antagonist binds BMP6 and BMP7 with high affinity, and binds BMP2 and BMP4 with a lower affinity (Kusu et al.). Mutations in the SOST gene have been associated with sclerosteosis (Brunkow et al.), van Buchem disease (Staehling-Hampton et al.), and bone dysplasia disorders, characterized by increased bone density. This protein product contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, sclerostin from STEMCELL comes lyophilised with ≥87% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

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Modulate prostaglandin metabolism with 15-hydroxyprostaglandin dehydrogenase (15-PGDH). 15-PGDH catalyses the reversible oxidation of the 15-hydroxyl group in prostaglandins, resulting in inactivated metabolites (Ensor and Tai), it can act on a variety of prostaglandins as substrates in a NAD+ dependent manner (Cho et al.). As prostaglandins can have a range of effects on cellular processes, 15-PGDH is of considerable importance in drug development. In vitro and in vivo studies suggest 15-PGDH has tumor suppressive activity and is downregulated in certain cancers (Na et al.).15-PGDH belongs to the short-chain dehydrogenases/reductases (SDR) family; its primary structure indicates 20% homology with other SDRs, with some conserved amino acid residues (Krook et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, apo M from STEMCELL comes lyophilised with ≥89% purity.

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Fetuin B is thought to have functions in female fertility, metabolism, and liver disease. A protease inhibitor belonging to the fetuin family of proteins, within the cystatin superfamily, fetuin b’s structure includes two cystatin domains (CY1 and CY2) connected by a linker, with a CPDCP-trunk and a C-terminal region (CTR) (Cuppari et al.). This plasma protein originates in the liver (Denecke et al.) and acts to inhibit the activity of ovastacin, a metalloprotease that causes the zona pellucida to harden, leading to female infertility (Karmilin et al.). Fetuin B has also been reported to increase apoptosis, and inhibit migration and invasion of prostate cancer cells, in in vitro and in vivo settings (Zhan et al.). Elevated serum fetuin B has been linked to non-alcoholic fatty liver disease (NAFLD) (Zhu et al.). 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 ≥92% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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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 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.

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Insulin-like growth factor-binding protein 4 (IGFBP-4) inhibits the actions of IGF-I and IGF-II. The distribution of IGFBP-4 in tissues is dependent on its glycosylation state, however it preferentially targets connective tissue (Firth and Baxter; Qin et al.). IGFBP-4 is also produced in liver, adrenal glands, Leydig cells, developing embryos, spinal cord, and thymic cortex. IGFBP-4 inhibits WNT/β-catenin signaling, which downregulates prostate cancer proliferation (Zhu et al.). In vitro studies suggest that IGFBP-4 inhibits proliferation of neuroblastoma and glioma, while promoting bone loss in osteosarcoma and multiple myeloma (Durai et al.).

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Interleukin 6 (IL-6) is a pleiotropic growth factor with the wide range of biological activities in immune regulation, hematopoiesis, and oncogenesis. IL-6 is produced by a variety of cell types including T cells, B cells, monocytes and macrophages, fibroblasts, hepatocytes, vascular endothelial cells, and various tumor cell lines. On its own or in combination with other factors such as IL-2 and interferon-γ, IL-6 stimulates the proliferation of B cells, T cells, and hybridoma cells (Hirano et al.; Mihara et al.; Tanaka et al). In combination with cytokines such as IL-3, GM-CSF and SCF, IL-6 has been shown to promote hematopoietic progenitor cell proliferation and differentiation in vitro. IL-6 signals through a cell surface type I cytokine receptor complex consisting of the ligand-binding IL-6α (CD126) and the signal-transducing gp130 subunits. The binding of IL-6 to its receptor system includes activation of JAK/STAT signaling pathway (Mihara et al.; Peters et al.; Tanaka et al.). This product is animal component-free.

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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.