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Goat polyclonal antibody against mouse IgG (H+L).

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Goat polyclonal antibody against rabbit IgG (H+L).

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Count cells manually at a fraction of the cost and footprint of automated cell counters by using the Hausser Scientific™ Bright-Line hemocytometer.

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Rabbit polyclonal antibody against human, mouse, rat chromogranin A.

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Rabbit polyclonal antibody against human, mouse, rat TBR1 (IDDAS).

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Stimulating T cells with HHV6 (U90) Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. HHV6 (U90) Peptide pool is a lyophilised mixture of 267 peptides from protein U90 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 1078 on U90. U89 - U90 RNA expression occurs under immediate-early conditions of infection (Mirandola et al.), and the associated protein exhibits peri-nuclear and cytoplasmic localization (Nikolaou et al.). Also known as immediate-early protein IE1, latency-associated transcripts of HHV6 may function as a source of IE1 during viral reactivation (Kondo 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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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.). This product is animal component-free.

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Interleukin 1 alpha (IL-1α) is a member of the IL-1 family and a dual-function cytokine. Both the unprocessed precursor and a processed IL-1α protein signal through IL-1 receptor type 1 (IL-1R1). Various cells, including keratinocytes, thymic epithelium, hepatocytes, endothelial cells, fibroblasts, and the epithelial cells of mucous membranes, have high levels of intracellular IL-1α precursor. The precursor is also expressed on the surface of monocytes and B lymphocytes (Netea et al.). IL-1α recruits infiltrating cells to a site of injury during necrosis and plays an important role during processes of sterile inflammation (Cohen et al.; Rider et al.). During hypoxia, IL-1α contributes to angiogenesis (Carmi et al.). Studies in mice show that IL-1α is produced by microglia-like cells after ischemic brain injury, which contributes to the inflammation (Luheshi et al.).

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Interleukin 1 beta (IL-1β) is synthesized as an inactive precursor protein or pro-IL-1β. This precursor is cleaved intracellularly by caspase 1 (IL-1β convertase) to form the active form of the protein that is later secreted (Allan et al.). IL-1β binds to IL-1 receptor and activates intracellular signaling via the MAPK or NF-κB pathway. IL-1β is released by monocytes, tissue macrophages, and dendritic cells in response to infection or injury and induces expression of acute-phase proteins. It also promotes the infiltration of inflammatory and immunocompetent cells from the circulation into the extravascular space and affected tissues, by stimulating the expression of adhesion molecules on endothelial cells. IL-1β also affects other immune cells; for example, it co-stimulates T cell functions together with an antigen or mitogen. It also stimulates Th17 differentiation and B cell proliferation in an IL-6-dependent manner.

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Lipocalin-2 (LCN2) is a member of the lipocalin superfamily, which share a highly conserved fold containing an eight-stranded antiparallel beta barrel (Flower), and transport small hydrophobic molecules. Playing a role in innate immunity, Lipocalin-2 acts as a potent bacteriostatic reagent by sequestering iron-containing siderophores (Flo et al.). It is mainly expressed in activated neutrophils, but is also secreted by other immune cells in response to infection. Lipocalin-2 has been implicated in multiple cellular processes, such as differentiation (Yang et al.), migration (Du et al.), and apoptosis (Devireddy et al.). In vitro studies suggest that lipocalin-2 is a potential therapeutic target for certain cancers, including colorectal cancer (CRC; Zhang et al.) and chronic lymphocytic leukemia (Bauvois et al.). This protein product contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, lipocalin-2 from STEMCELL comes lyophilised with ≥94% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

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Stimulating T cells with HPV16 (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 116 peptides from minor capsid protein L2 of human papillomavirus type 16 (HPV16), HPV16 (L2) Peptide Pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 473 on L2. L2 is equipped with multiple nuclear retention signals (Darshan et al.; Mamoor et al.), and enters the nuclei of host cells via several import pathways mediated by Kapα2β1 heterodimers, Kapβ2, and Kapβ3 (Darshan 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 BKV (LT) Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. BKV Peptide pool is a lyophilised mixture of 171 peptides from the Large T (LT) antigen of BK polyomavirus (BKV), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 695 on LT antigen. LT antigen is an early viral protein (Low et al.) that contributes to the transformation and maintenance of host cells (Nakshatri et al.). It has been found to bind to a subset of tumor suppressor proteins (Harris et al.), and its co-expression with p53 has been observed in polyomavirus-associated nephropathy (Seemayer 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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A member of the pentraxin family of proteins, C-reactive protein (CRP) plays important roles in host defenses, including regulating complement activation in vivo (Sjoberg et al.), decreasing nitric oxide production, and inhibiting angiogenesis in vitro (Verma et al., 2002). At specific concentrations, CRP directly inhibits endothelial progenitor cell (EPC) differentiation, survival, and function, and is thus implicated in the development of cardiovascular diseases (Verma et al., 2004). CRP is primarily synthesized by liver hepatocytes, but also by other immune cells, such as macrophages and lymphocytes (Sproston and Ashworth). The expression of this acute-phase protein is induced by IL-6 and IL-1 secretion of macrophages and T-cells during inflammation. For consistency and reproducibility across your applications, C-reactive protein from STEMCELL comes lyophilised with ≥87% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.

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Vascular endothelial growth factor D (VEGF-D) is a member of the VEGF/platelet-derived growth factor (PDGF) family of proteins. VEGF-D is a potent angiogenic factor and promotes lymphangiogenesis, endothelial cell growth and survival, and can affect blood vessel permeability. VEGF-D is expressed in the lung, heart, small intestine, fetal lung, and at lower levels in the pancreas, colon, and skeletal muscle (Otrock et al.; Roy et al.; Stacker et al.; Yamada et al.). VEGF-D is a ligand for VEGF receptors 2 (Flk1) and 3 (Flt4) (Baldwin et al.). VEFGR-3 is highly expressed in lymphatic endothelial cells and is essential for their growth and differentiation (Otrock et al.; Roy et al.). Binding of VEGF-D to neuropilins contributes to VEGFR-3 signaling during lymphangiogenesis, whereas binding to integrin α9β1 promotes endothelial cell adhesion and migration (Roy et al.; Otrock et al.). During embryogenesis, VEGF-D also plays a role in the formation of the venous and lymphatic systems.

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Heparin-binding epidermal growth factor (EGF)-like growth factor (HBEGF) is a member of the EGF family (Nishi and Klagsbrun). HBEGF promotes blastocyst adhesion to the uterine wall (Iwamoto and Mekada). It also plays a role in smooth muscle cell hyperplasia and brain injury (Nishi and Klagsburn). HBEGF produced by CD4+ T cells promotes wound healing by stimulating migration and proliferation of keratinocytes, fibroblasts, and smooth muscle cells (Blotnick et al.). It binds to EGFR, ErbB4, ErbB2, and ErbB3, activating the PI3K/AKT signaling cascade (Iwamoto and Mekada). HBEGF is produced in a variety of cells, where it contributes to physiological and pathological processes. HBEGF is overexpressed in ovarian, breast, gastric, colorectal, pancreatic, and endometrial cancers, which likely contributes to pathogenesis (Miyata et al.). This product is animal component-free.

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Stimulating T cells with the HPV18 (L1) 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 140 peptides from major capsid protein L1 of human papillomavirus type 18 (HPV18), HPV18 (L1) Peptide pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 568 on L1. L1 enters the nuclei of host cells and can assemble into virus-like particles (Stauffer 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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Perform total nucleic acid extraction from a variety of sample types using the ErythroClear™ magnet.

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For detection and measurement of mouse interferon-gamma.

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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, such as 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 suggested that PDGF-AA is an important autocrine regulator of vascular endothelial growth factor (VEGF) expression in non-small cell lung carcinomas (Shikada et al.). PDGF-AA also mediates proliferation of oligodendrocyte progenitor cells and oligodendrocyte lineage differentiation through the activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) (Hu et al.). PDGF-AA is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into oligodendrocyte precursor cells (Piao et al.).

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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 mobilisation 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. Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways. This product is animal component-free.

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Transforming growth factor (TGF) beta 3 is a member of the TGF-β superfamily and regulates diverse cellular phenotypes. TGF-beta 3 binds to serine-threonine kinase type I and II receptors and activates signal transduction through SMAD2/3 proteins, thus regulating a variety of functions, including cell proliferation, differentiation, wound healing, apoptosis, and metabolism (Massagué; McDowell et al.). TGF-beta 3 enhances glycosaminoglycan production by mesenchymal stromal cells, stimulates scar-free healing, and improves glucose tolerance and phenotypic changes in adipocyte morphology (Hall et al.; Holton et al.). TGF-beta 3 induces proliferation of posterofrontal suture-derived mesenchymal stromal cells, and stimulates expression of fibroblast growth factors 2 and 18 (James et al.). This product is animal component-free.

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Interleukin 19 (IL-19) is a member of the IL-10 cytokine family and is produced by keratinocytes, B cells, and monocytes (Romer et al.; Wolk et al.). Expression of IL-19 can be induced by granulocyte-macrophage colony-stimulating factor (GM-CSF) or lipopolysaccharide (LPS; Gallagher et al.). IL-19 is considered to be a proinflammatory cytokine, as it upregulates IL-6 and tumor necrosis factor alpha (TNF-α; Liao et al. 2002). IL-19 binds the IL-20 receptor complex (IL-20R) which comprises IL-20R alpha and IL-20R beta to activate the STAT3 pathway (Dumoutier et al.). IL-19 also induces T-helper cell differentiation towards a Th2 response, resulting in the production of IL-10 and additional IL-19 (Liao et al. 2002; Liao et al. 2004). IL-19 has been implicated in aging, vascular disease, Type I diabetes, and rheumatoid arthritis.

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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 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.).

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Interleukin 31 (IL-31), a four-helix bundle inflammatory cytokine, belongs to the IL-6 cytokine family which includes IL-6, oncostatin M, leukemia inhibitory factor (LIF), and cardiotrophin-1 ( Dillon et al.). IL-31 signals through a heterodimer composed of IL-31RA (also known as gp130-like receptor or GPL) and the oncostatin-M receptor (OSMR), both of which are expressed on monocytes (Diveu et al.; Ghilardi et al.), epithelial cells (Ip et al.), and keratinocytes (Kato et al.). Signaling through the GPL/OSMR complex activates the JAK/STAT, RAS/ERK, and PI3K/AKT signaling pathways, resulting in the downstream activation of STAT1, STAT3, and STAT5 transcription factors (Cornelissen et al.; Dambacher et al.; Dillon et al.; Ip et al.). IL-31 responses have been associated with allergic responses and inflammatory skin diseases including atopic dermatitis (Cornelissen et al.; Gangemi et al.).

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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; Fretto et al.; 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, 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-DD promotes growth and survival of renal artery smooth muscle cells and lens epithelial cells, and can act as a macrophage chemoattractant (Changsirikulchai et al.; Lokker et al.; Ray et al.; Uutela et al.).

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Immunomagnetic positive selection of human EGFR+ cells.

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Immunomagnetic negative isolation of untouched T cells from leukopaks.

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Hamster (Armenian) monoclonal antibody against mouse CD69, PE-Cy7-conjugated.

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Cell culture medium for establishment and maintenance of human colorectal cancer organoids.

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Serum-free medium for efficient and reproducible generation of lung progenitor cells from human ES and iPS cells.