111517 Results for: "5-Chloro-DL-tryptophan&pageNo=10&view=easy"

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).

Supplier: STEMCELL Technologies

Interleukin 6 (IL-6) is a pleiotropic growth factor with a 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 (Nordan et al.; Van Snick et al.; Gauldie 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 the JAK/STAT signaling pathway (Mihara et al.; Peters et al; Tanaka et al.).

Supplier: OMEGA BIO-TEK

Plasmid isolated with traditional purification procedures normally contain high levels of endotoxins that can significantly interfere with transfection experiments downstream. The E.Z.N.A.® Endo-Free Plasmid kits integrate an efficient endotoxin removal step into the plasmid purification procedure to produce high quality transfection grade plasmid.

Supplier: ProSci Inc.

BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers. Processed human BAFF can either remain as a trimer, which is usual for TNF family ligands or assemble into 60-mer composed of 20 trimers. Mouse BAFF 60-mer has been identified in the serum of BAFF transgenic mice. Oligomerisation of BAFF 3-mer into 60-mer in human BAFF is prevented by mutation of His218, a residue critical for 3-mer-to-3-mer interactions, but not for receptor binding. Despite the predominant functional role of processed BAFF in vivo, membrane-bound BAFF might also play a role. Indeed, soluble BAFF (3-mer) can trigger BAFF-R but not TACI or BCMA, whereas oligomeric forms of BAFF (BAFF 60-mer), which mimic membrane-bound BAFF, activate all BAFF receptors.

Supplier: STEMCELL Technologies

Interleukin 9 (IL-9) has pleiotropic functions in the immune system and signals through its specific IL-9 receptor (IL-9R) (Renauld et al.). IL-9/IL-9R signaling pathway mainly targets the downstream activation of JAK/STAT (janus kinase/signal transducer and activator of transcription) and subsequent phosphorylation cascades initiated by multiple kinases including IRS–PI3K–PKB (insulin receptor substrate, phosphatidyl-inositol 3-kinases, protein kinase-B) and ERK (Knoops and Renauld; Fontaine et al.). IL-9 has been shown to have a role in Th1/Th17-mediated inflammation and in regulatory T cell responses (Singh et al.; Goswami and Kaplan). IL-9/IL-9R signaling pathway represents a novel endogenous anti-apoptotic mechanism for cortical neurons (Fontaine et al.). IL-9 secreting T cells, termed Th9 cells, contribute to both effective immunity and immunopathological disease, and have been shown to have a role in the treatment of allergic and autoimmune disease (Kaplan et al.).

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.).

Supplier: STEMCELL Technologies

Betacellulin is a member of the epidermal growth factor (EGF) family, and signals through EGF receptor and ERBB4. It activates ERK and AKT pathways, which induces neural stem cell proliferation and prevents spontaneous differentiation in culture. Betacellulin stimulates the expansion of neural stem cells, transit-amplifying cells, and neuroblasts derived from subventricular zone and dentate gyrus (Gómez-Gaviro et al.). It is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Betacellulin down-regulates E-cadherin expression in ovarian cancer cell lines via MEK/ERK1/2 and PI3K/AKT signaling pathways, thus increasing cell migration (Zhao et al.). It is a modulator of interferon (IFN) response and enhances anti-viral effects of IFN (Al-Yahya et al.). Betacellulin is expressed in pancreatic α cells, β cells, and duct cells. It induces the proliferation of pancreatic cancer cell lines, inhibits apoptosis, promotes the neogenesis of β cells, and converts non-β cells into insulin-producing cells (Kawaguchi et al.; Miyagawa al.; Saito et al.).

Supplier: STEMCELL Technologies

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.

Supplier: STEMCELL Technologies

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.).

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 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.

Supplier: Portwest

This jacket offers exceptional weather protection, comfort, and warmth while utilising the latest innovations in recycled fabrics. The outer shell, lining, and wadding are certified recycled polyester, and the packaging is derived from sugarcane, allowing the wearer to champion sustainability without compromising on performance.

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).

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 andamp; 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.

Supplier: Quantabio

Ultra-Plex™ 1-Step ToughMix® is a ready-to-use, 4X-concentrated master mix for reverse transcription quantitative PCR (RT-qPCR) of RNA templates using hybridisation probe detection chemistries such as TaqMan® 5’-hydrolysis probes on Real-Time PCR systems that utilise ROX passive reference with 490 nM excitation. First-strand cDNA synthesis and PCR amplification are carried out in the same tube without opening between procedures. It is ideal for highly sensitive quantification of RNA viruses or low abundance RNA targets in uni- or multiplexed RT-qPCR applications as well as high throughput gene-expression studies. The system has been optimised to deliver maximum RT-qPCR efficiency, sensitivity, and specificity in reduced reaction volumes and fast cycle times. Ultra-Plex™ 1-Step ToughMix® contains all required components for RT-qPCR except RNA template and probe. It is compatible with all dual-labeled probe chemistries.

Supplier: STEMCELL Technologies

Interleukin 21 (IL-21) is a pleiotropic cytokine that is composed of four α-helical bundles and primarily produced by natural killer T (NKT) cells, T follicular helper (Tfh) cells, and Th17 cells (Spolski and Leonard 2008). IL-21 signals via heterodimers of the IL-21 receptor (IL-21R) and the IL2RG encoded common cytokine receptor γ-chain (Parrish-Novak et al.; Ozaki K et al. 2000), and utilizes the JAK/STAT, MAPK, and PI3K pathways (Spolski and Leonard 2014). IL-21 has been shown to have a critical role in regulating immunoglobulin production and differentiation of the pro-inflammatory Th17 population of cells (Ozaki et al. 2002; Nurieva et al.). Additionally, IL-21 specifically sustains CD8+ T cell effector activity and provides a mechanism of CD4+ T cell help during chronic viral infection (Elsaesser et al.). IL-21 signaling was also found critical for the development of type 1 diabetes in NOD mice (Sutherland et al.) and control of T cell autoimmunity by regulatory B cells (Yoshizaki et al.).

Supplier: STEMCELL Technologies

Interleukin 21 (IL-21) is a pleiotropic cytokine that is composed of four α-helical bundles and primarily produced by natural killer T (NKT) cells, T follicular helper (Tfh) cells, and Th17 cells (Spolski and Leonard 2008). IL-21 signals via heterodimers of the IL-21 receptor (IL-21R) and the IL2RG-encoded common cytokine receptor γ-chain (Parrish-Novak et al.; Ozaki K et al. 2000), and utilizes the JAK/STAT, MAPK, and PI3K pathways (Spolski and Leonard 2014). IL-21 has been shown to have a critical role in regulating immunoglobulin production and differentiation of the pro-inflammatory Th17 population of cells (Ozaki et al. 2002; Nurieva et al.). Additionally, IL-21 specifically sustains CD8+ T cell effector activity and provides a mechanism of CD4+ T cell help during chronic viral infection (Elsaesser et al.). IL-21 signaling was also found critical for the development of type 1 diabetes in NOD mice (Sutherland et al.) and control of T cell autoimmunity by regulatory B cells (Yoshizaki et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Neurotrophin-3 (NT-3) is a neurotrophic factor and a member of the nerve growth factor (NGF) family of proteins that includes neuron growth factor (NGF), brain-derived neurotrophic factor (BDNF), and neurotrophin-4/5. NT-3 signals a number of trophic effects through its transducing receptor tyrosine kinase TrkC. NT-3 is known to promote survival, development, and differentiation of neurons, and modulates transmitter release at several types of synapses in the peripheral and central nervous systems (Chalazonitis 1996). NT-3 has been shown to have an important role in the overall development of enteric neurons, which are crucial for gut peristalsis (Chalazonitis 2004). Studies in rats have shown the potential of NT-3 in dorsal column axonal regeneration (Bradbury et al.). NT-3 was shown to protect neurons against amyloid-β toxicity (Lesne et al.). NT-3 has applications in neuronal differentiation protocols to generate β-tubulin III+ peripheral neurons from neural crest stem cells (Menendez et al.) and oligodendrocyte precursor cells from human embryonic stem (ES) and induced pluripotent stem (iPS) cells (Douvaras et al.).

Supplier: STEMCELL Technologies

Interleukin 1 beta (IL-1β) is synthesised 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-kB 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 antigen or mitogen. It also stimulates Th17 differentiation and B cell proliferation in an IL-6-dependent manner. Mice deficient in IL-1β do not show phenotypical differences from wild-type mice; however, they have a reduced response to inflammation, suggesting that IL-1β plays a key role in inflammatory diseases (Dinarello).

Supplier: STEMCELL Technologies

Interleukin 15 (IL-15) is a four-alpha helix bundle cytokine with many similar properties to IL-2. The IL-15 receptor is a heterotrimeric receptor composed of IL-15Ra (the high-affinity receptor for IL-15), as well as IL-2/15Rb (CD122) and common gamma chain (CD132). IL-15 binds to IL-15Rα receptor and can then be presented in trans to IL-2/15Rb and common gamma chain on other cells. Trans-presentation is thought to be the major mechanism by which IL-15-mediated responses occur in mice, although may not be necessary in humans (Castillo et al.). The cytoplasmic domains of IL-2/15Rb and common gamma chain mediate signaling to activate JAK/STAT and PI3K pathways. IL-15 supports the survival and proliferation of naïve CD4+ and CD8+ T cells, and promotes homeostasis of memory T cells. IL-15 also promotes the survival and differentiation of NK cells and regulates their cytolytic activity (Ma et al.). This product is animal component-free.

Supplier: Brand

PP. These 0,2 and 0,5 ml PCR tubes with attached caps are compatible with leading thermal cyclers with heated lids.

Supplier: OHAUS

Intuitive balances designed for routine weighing. Striking the ideal balance between inventive features and functional, uncomplicated weighing capabilities, the OHAUS Adventurer incorporates all of the applications necessary for routine weighing and measurement activities. With a colour touchscreen, three level user management to fulfill GLP/GMP compliance capabilities, two USB ports, and much more, Adventurer is the most complete balance in its class.

Supplier: STEMCELL Technologies

Leukemia inhibitory factor (LIF) is an interleukin 6 class cytokine that regulates a broad variety of developmental functions. After LIF binds to LIF receptor (LIFR), LIFR associates with gp130 and activates JAK/STAT and MAPK signaling (Auernhammer and Melmed; Suman et al.). LIFR activation of STAT3 is essential for maintaining the mouse embryonic stem cell phenotype (Niwa et al.). Produced by the endometrium, LIF plays an important autocrine and paracrine role in implantation by regulating proliferation, invasion, and differentiation of trophoblasts following blastocyst attachment (Auernhammer and Melmed; Suman et al.). Human LIF can be used for the maintenance of mouse embryonic stem cells, however mouse LIF cannot bind to the human receptor, thus rendering mouse LIF inactive (Dahéron et al.). LIF is produced by CD4+ and activated regulatory T cells, and promotes Foxp3 expression, while repressing Th17 lineage-specific genes (Metcalfe). LIF is also secreted by mesenchymal stromal cells, where it supports hematopoiesis and immune modulation (Nasef et al.).

Supplier: ProSci Inc.

This gene is a member of the protocadherin alpha gene cluster, one of three related gene clusters tandemly linked on chromosome five that demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The alpha gene cluster is composed of 15 cadherin superfamily genes related to the mouse CNR genes and consists of 13 highly similar and 2 more distantly related coding sequences. The tandem array of 15 N-terminal exons, or variable exons, are followed by downstream C-terminal exons, or constant exons, which are shared by all genes in the cluster. The large, uninterrupted N-terminal exons each encode six cadherin ectodomains while the C-terminal exons encode the cytoplasmic domain. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins that most likely play a critical role in the establishment and function of specific cell-cell connections in the brain. This gene is a member of the protocadherin alpha gene cluster, one of three related gene clusters tandemly linked on chromosome five that demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The alpha gene cluster is composed of 15 cadherin superfamily genes related to the mouse CNR genes and consists of 13 highly similar and 2 more distantly related coding sequences. The tandem array of 15 N-terminal exons, or variable exons, are followed by downstream C-terminal exons, or constant exons, which are shared by all genes in the cluster. The large, uninterrupted N-terminal exons each encode six cadherin ectodomains while the C-terminal exons encode the cytoplasmic domain. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins that most likely play a critical role in the establishment and function of specific cell-cell connections in the brain. Alternative splicing has been observed and additional variants have been suggested but their full-length nature has yet to be determined.

Supplier: ProSci Inc.

FUSIP1 is a member of the serine-arginine (SR) family of proteins, which is involved in constitutive and regulated RNA splicing. Members of this family are characterized by N-terminal RNP1 and RNP2 motifs, which are required for binding to RNA, and multiple C-terminal SR/RS repeats, which are important in mediating association with other cellular proteins. This protein can influence splice site selection of adenovirus E1A pre-mRNA. It interacts with the oncoprotein TLS, and abrogates the influence of TLS on E1A pre-mRNA splicing.This gene product is a member of the serine-arginine (SR) family of proteins, which is involved in constitutive and regulated RNA splicing. Members of this family are characterized by N-terminal RNP1 and RNP2 motifs, which are required for binding to RNA, and multiple C-terminal SR/RS repeats, which are important in mediating association with other cellular proteins. This protein can influence splice site selection of adenovirus E1A pre-mRNA. It interacts with the oncoprotein TLS, and abrogates the influence of TLS on E1A pre-mRNA splicing. Alternative splicing of this gene results in at least two transcript variants encoding different isoforms. In addition, transcript variants utilizing alternative polyA sites exist.This gene product is a member of the serine-arginine (SR) family of proteins, which is involved in constitutive and regulated RNA splicing. Members of this family are characterized by N-terminal RNP1 and RNP2 motifs, which are required for binding to RNA, and multiple C-terminal SR/RS repeats, which are important in mediating association with other cellular proteins. This protein can influence splice site selection of adenovirus E1A pre-mRNA. It interacts with the oncoprotein TLS, and abrogates the influence of TLS on E1A pre-mRNA splicing. Alternative splicing of this gene results in at least two transcript variants encoding different isoforms. In addition, transcript variants utilizing alternative polyA sites exist.

Supplier: STEMCELL Technologies

Leukemia inhibitory factor (LIF) is an interleukin 6 class cytokine that regulates a broad variety of developmental functions. After LIF binds to the LIF receptor (LIFR), LIFR associates with gp130 and activates JAK/STAT and MAPK signaling (Auernhammer and Melmed; Suman et al.). LIFR activation of STAT3 is essential for maintaining the mouse embryonic stem cell phenotype (Niwa et al.). Produced by the endometrium, LIF plays an important autocrine and paracrine role in implantation by regulating proliferation, invasion, and differentiation of trophoblasts following blastocyst attachment (Auernhammer and Melmed; Suman et al.). Human LIF can be used for the maintenance of mouse embryonic stem cells; however, mouse LIF cannot bind to the human receptor, thus rendering mouse LIF inactive (Dahéron et al.). LIF is produced by CD4+ and activated regulatory T cells, and promotes Foxp3 expression, while repressing Th17 lineage-specific genes (Metcalfe). LIF is also secreted by mesenchymal stromal cells, where it supports hematopoiesis and immune modulation (Nasef et al.).

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; 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.).

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 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.).

Supplier: Thermo Fisher Scientific

Pierce™ Boronic acid resin enables ribonucleotide and oligonucleotide RNA isolation.

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; 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-BB is secreted by osteoblasts to induce mesenchymal stem cell migration and angiogenesis. It has also been shown that PDGF-BB is secreted by preosteoclasts during bone modeling and remodeling to induce angiogenesis and thus proper osteogenesis (Xie et al.).

Supplier: Portwest

This superb 5-in-1 jacket system is adaptable for any work situation. Outer jacket features 2 large roomy pockets, stud adjustable cuffs and concealed attached roll-away hood. Inner jacket has fluorescent fleece sleeves, comfortable knitted cuffs and 2 side pockets. Both the inner and outer jacket have full EN ISO 20471 Class 3 certification for maximum high visibility protection and safety.