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Allylpalladium(II)+chloride+dimer
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Allylpalladium(II)+chloride+dimer
Catalog Number:
(102979-290)
Supplier:
Adipogen
Description:
Tyrosine is one of the major targets of protein oxidation. Dityrosine (DT) is known to be formed when tyrosine is damaged by free radicals, such as reactive oxygen species (ROS), metal-catalyzed oxidation, ultraviolet irradiation, and peroxidases. Dityrosine has been found in atherosclerotic lesions, and lipofuscin of pyramidal neurons of aged human brains. Dityrosine is a specific biomarker for protein oxidation. Dityrosine is reported to exist in various tissues and was also recently detected in urine samples. It is expected to be a novel protein oxdation marker, which is non-invasively detectable.
Catalog Number:
(103285-314)
Supplier:
Novus Biologicals
Description:
The MGA Antibody from Novus Biologicals is a rabbit polyclonal antibody to MGA. This antibody reacts with human. The MGA Antibody has been validated for the following applications: Immunohistochemistry, Immunocytochemistry / Immunofluorescence, Immunohistochemistry-Paraffin.
Catalog Number:
(10481-564)
Supplier:
Bioss
Description:
The Lyl1 gene encodes a basic helix–loop–helix transcription factor involved in T-cell acute lymphoblastic leukemia. The expression of Lyl1 is at higher levels in the majority of cases of acute myeloblastic leukemia (AML) or myelodysplastic syndrome when compared to normal bone marrow. Lyl1 is highly expressed in most AML cell lines.Lyl-1, TAL1 and TAL2 are part of a family of basic helix-loop-helix (bHLH) proteins implicated in T cell acute leukemia. TAL1, also designated SCL, is a serine phosphoprotein and basic helix-loop-helix transcription factor known to regulate embryonic hematopoiesis. TAL2 is a protein involved in T cell acute lymphoblastic leukemia through a chromosomal translocation involving TAL2 and T cell receptor ∫ chain genes. TAL2 includes a helix-loop-helix protein dimerization and DNA-binding domain that is homologous to TAL1 and Lyl-1 proto-oncogenes. Lyl-1 (lymphoblastic leukemia-derived sequence 1) is a nuclear protein. Endogenous Lyl-1 exists in complex with E2å proteins. Lyl-1 and E2å protein can form heterodimeric complexes with distinctive DNA-binding properties in hematolymphoid cells. Lyl-1 is involved in a chromosomal aberration which causes a form of T cell acute lymphoblastic leukemia (T-ALL).
Catalog Number:
(10481-560)
Supplier:
Bioss
Description:
The Lyl1 gene encodes a basic helix–loop–helix transcription factor involved in T-cell acute lymphoblastic leukemia. The expression of Lyl1 is at higher levels in the majority of cases of acute myeloblastic leukemia (AML) or myelodysplastic syndrome when compared to normal bone marrow. Lyl1 is highly expressed in most AML cell lines.Lyl-1, TAL1 and TAL2 are part of a family of basic helix-loop-helix (bHLH) proteins implicated in T cell acute leukemia. TAL1, also designated SCL, is a serine phosphoprotein and basic helix-loop-helix transcription factor known to regulate embryonic hematopoiesis. TAL2 is a protein involved in T cell acute lymphoblastic leukemia through a chromosomal translocation involving TAL2 and T cell receptor ∫ chain genes. TAL2 includes a helix-loop-helix protein dimerization and DNA-binding domain that is homologous to TAL1 and Lyl-1 proto-oncogenes. Lyl-1 (lymphoblastic leukemia-derived sequence 1) is a nuclear protein. Endogenous Lyl-1 exists in complex with E2å proteins. Lyl-1 and E2å protein can form heterodimeric complexes with distinctive DNA-binding properties in hematolymphoid cells. Lyl-1 is involved in a chromosomal aberration which causes a form of T cell acute lymphoblastic leukemia (T-ALL).
Catalog Number:
(BDH7317-1)
Supplier:
Biotium
Description:
This MAb recognizes TGF beta 1, 2 and 3. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF beta requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF beta 3 protein has approximately 80% identity to the mature region of both TGF beta 1 and TGF beta 2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGF betas inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®405S is a blue fluorescent dye (Ex/Em 404/431 nm) with superior brightness compared to other blue dyes; it is also compatible with super-resolution imaging by SIM. Note: Conjugates of blue fluorescent dyes are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.
Supplier:
PeproTech, Inc.
Description:
The FGF family plays a central role during prenatal development and postnatal growth, and the regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. The FGF ligands bind to a family of type I transmembrane tyrosine kinase receptors, which leads to dimerization and activation by sequential autophosphorylation of specific tyrosine residues. Four genes encoding structurally related FGF receptors (FGFR-1 to -4) are known. Alternative splicing of the mRNAs generates numerous forms of FGFR-1 to -3. Alternate forms of FGF receptors can exhibit different specificities with respect to ligand binding. For example, the form designated as FGFR1a (IIc) interacts predominantly with FGF-acidic (FGF1) and FGF-basic (FGF2). A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the beta isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). Recombinant Human FGFR2a (IIIc) Fc is a 65.6 kDa protein containing 589 amino acids. Under reducing conditions, FGFR2a migrates between 100-110 kDa on SDS-PAGE gel.
Catalog Number:
(10285-294)
Supplier:
Bioss
Description:
Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.
Catalog Number:
(10389-482)
Supplier:
Bioss
Description:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
Supplier:
Biotium
Description:
CD309, also known as VEGFR2, KDR3, and Flk-1 (mouse), is a type I transmembrane glycoprotein. It is a member of the CSF-1/PDGF receptor family of type III tyrosine kinase receptors. Human VEGFR2 is mainly expressed by endothelial cells, embryonic tissues, and megakaryocytes. It plays an important role in the regulation of angiogenesis, vasculogenesis, and vascular permeability. The ligands of VEGFR2 include VEGF-A, VEGF-C, VEGF-D, and VEGF splice isoforms. Ligation of VEGFR2 with its ligands results in the receptor dimerization and auto-phosphorylation, stimulating endothelial cell proliferation and migration.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®405S is a blue fluorescent dye (Ex/Em 404/431 nm) with superior brightness compared to other blue dyes; it is also compatible with super-resolution imaging by SIM. Note: Conjugates of blue fluorescent dyes are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.
Supplier:
BioVendor
Description:
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26. Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulace glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs. Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. Recent studies have shown that human resistin is expressed also in macrophages and may be a novel link between inflammation and insulin resistance.
Catalog Number:
(101423-202)
Supplier:
BioVendor
Description:
A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa. Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994). Different isolates of Orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appears to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999; Wise et al., 1999). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E can not bind to VEGF receptor-1 (Flt-1). Furthermore VEGF-E can also not bind to VEGF receptor-3 (FLT-4). Therefore VEGF-E is a potent angiogenic factor selectively binding to VEGF receptor –2/KDR.
Catalog Number:
(76083-196)
Supplier:
Bioss
Description:
Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.
Catalog Number:
(10352-656)
Supplier:
Bioss
Description:
Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages.
Supplier:
Biotium
Description:
Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including ER-alpha and ER-beta, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. They are located in the nucleus, though some estrogen receptors associate with the cell surface membrane and can be rapidly activated by exposure of cells to estrogen. ER-alpha and ER-beta are differentially activated by various ligands. Receptor-ligand interactions trigger a cascade of events, including dissociation from heat shock proteins, receptor dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ER-alpha and ER-beta may be regulated by distinct mechanisms even though they share many functional characteristics.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®405S is a blue fluorescent dye (Ex/Em 404/431 nm) with superior brightness compared to other blue dyes; it is also compatible with super-resolution imaging by SIM. Note: Conjugates of blue fluorescent dyes are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.
Catalog Number:
(76085-290)
Supplier:
Bioss
Description:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
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is still displayed and you need assistance, please call us at 1-800-932-5000.
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