| Description | Hemopexin is a single-chain protein belonging to the family of blood transport proteins. It binds to heme released into the bloodstream during the degradation process. Recent studies have demonstrated that hemopexin acts as an extracellular antioxidant against hemoglobin-mediated damage in Hemopexin is a single-chain protein belonging to the family of blood transport proteins. It binds to heme released into the bloodstream during the degradation process. Recent studies have demonstrated that hemopexin acts as an extracellular antioxidant against hemoglobin-mediated damage in inflammation. Hemopexin protects against heme toxicity and conserves and recycles iron. Abnormal levels of hemopexin are associated with hemolytic anemia, chronic neuromuscular disease, and acute intermittent porphyria.EU: <1.0 EU/mg by fluorogenic assay, Lonza, 50-658UPrepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.Ref:Strop, P., et al. 1981. J. Chromat. 214, 317; Miller, Y.I., et al. 1996. Biochem. 35, 13112... Read More | Inquire | Purity>95% as determined by SDS-PAGE and Coomassie blue stainingFunctionThe heparin-binding fibroblast growth factors play important roles in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. They are potent mitogens in vitro.Sequence Purity>95% as determined by SDS-PAGE and Coomassie blue stainingFunctionThe heparin-binding fibroblast growth factors play important roles in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. They are potent mitogens in vitro.Sequence similaritiesBelongs to the heparin-binding growth factors family.Cellular localizationSecreted. Cytoplasm. Cytoplasm > cell cortex. Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1... Read More | Purity>97% by SDS-PAGE and HPLC analyses.FunctionMay be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptors with higher affinity than EGF itself and is a far more potent mitogen for Purity>97% by SDS-PAGE and HPLC analyses.FunctionMay be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptors with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor.Background:Human HB-EGF (Heparin-Binding EGF-like growth factor) is a 12-16 kDa member of the EGF family of peptide growth factors (1-3). Also known as the DTR (diphtheria toxin receptor), it is further classified as a group 2 ErbB ligand based on its ability to activate both the EGF/ErbB1 and ErbB4 receptors (4, 5). HB-EGF is synthesized as a 208 amino acid (aa) type I transmembrane preproprecursor (1, 6). It contains a 19 aa signal sequence, a 43 aa prosegment, an 86 aa mature region (aa 63-148), an 11 aa juxtamembrane cleavage peptide, a 24 aa transmembrane segment, and a 25 aa cytoplasmic tail (aa 184-208). As an integral membrane protein, HB-EGF is expressed as a 19-27 kDa protein in mammalian cells (7-9). The variability in molecular weight (MW) is attributed to heterogeneity in glycosylation and/or the utilization of multiple proteolytic cleavage sites during maturation. Mature HB-EGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. It possesses an EGF-like domain between aa 104-144, and a heparin-binding motif between aa 93‑113. Although the aa range for "mature" HB-EGF is typically stated to be Asp63-Leu148, potential N-terminal start (cleavage) sites also exist at Gly32, Arg73, Val74, Ser77 and Ala82 (8, 10-12). Thus, differential processing (in part) likely accounts for the 16-23 kDa range in MW noted for mammalian-derived mature HB-EGF. Proteases suggested to contribute to HB-EGF processing include TACE, MMP-3 and -7, ADAM-17 and ADAM-12 (11, 13-16). When expressed recombinantly in E.coli, HB-EGF (aa 73-148) runs at 14 kDa in SDS-PAGE; when expressed in Baculovirus, HB-EGF (aa 63-148, 77-148 and 32-148) runs at 18 kDa, 15 kDa, and 19 kDa respectively (8, 12, 17). Over aa 63-148, human HB-EGF- shares 76% and 73% aa sequence identity with rat and mouse HB-EGF, respectively (1, 18). Cells known to express HB-EGF include bronchial epithelium (19), visceral and vascular smooth muscle (20, 21), CD4+ T cells (22), cardiac muscle (23), glomerular podocytes (24), keratinocytes (13) and IL-10-secreting regulatory macrophages (25). As noted earlier, HB-EGF is known to bind to both 170 kDa EGFR and 180 kDa ErbB4, and through heterodimerization, ErbB2 (13, 26). Activity associated with ErbB4 binding appears to be limited to non-mitogenic actions, while EGFR binding induces both mitogenic and non-mitogenic activity... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： KLK3 (Kallikrein Related Peptidase 3) is a Protein Coding gene. The gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. It encodes a single-chain glycoprotein, a Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： KLK3 (Kallikrein Related Peptidase 3) is a Protein Coding gene. The gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. It encodes a single-chain glycoprotein, a protease that is synthesized in the epithelial cells of the prostate gland and is present in seminal plasma. KLK3, also known as Prostate Specific Antigen (PSA), kallikrein-related peptidase 3, Gamma-seminoprotein, is a secreted protein of the glandular kallikrein subfamily of serine proteases. KLK3 contains one peptidase S1 domain. KLK3 is a glycoprotein produced almost exclusively by the prostate gland. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers... Read More |