| Description | Adrenomedullin (16-31), human is amino acid residues 16-31 fragment of human adrenomedullin (hADM). Adrenomedullin has appreciable affinity for the CGRP1 receptor. Adrenomedullin (16-31), human possesses pressor activity in the systemic vascular bed of the rat, but not the cat.Form:Solid | description：Bovine pancreatic deoxyribonuclease I produced recombinantly in yeast, Pichia pastoris, to decrease levels of contaminating RNase and eliminate potential pathogens associated with animal based materials.Bovine pancreas is a rich source of RNase A which is often found in many description：Bovine pancreatic deoxyribonuclease I produced recombinantly in yeast, Pichia pastoris, to decrease levels of contaminating RNase and eliminate potential pathogens associated with animal based materials.Bovine pancreas is a rich source of RNase A which is often found in many commercial DNase preparations. Producing DNase I by recombinant means in an organism with much lower levels of endogenous RNase greatly facilitates purification of an enzyme with undetectable levels of RNase. The processes involved in the production and isolation of recombinant DNase I are completely devoid of animal based components which eliminates the possibility of introducing animal derived pathogens into bioprocessing procedures.Animal Free/AF. Recombinant Bovine pancreatic deoxyribonuclease 1 produced in Pichia pastoris. Chromatographically purified. Free of animal derived components, RNases & proteases. A liquid preparation in 5mM Calcium Acetate, 4mg/ml glycine, pH 5.0 and 50% glycerol. Supplied with 10x reaction buffer.Storage Buffer : 5mM calcium acetate, 4mg/ml glycine, pH 5.0 and 50% glycerol.DNase I Reaction Buffer (10X): 500mM Tris-HCl, 10mM MgSO4, 1mM CaCl2, pH 7.8, provided.application：Recombinant DNase I is suitable for such applications as:• Removing genomic DNA from RNA preparations prior to RT-PCR• Degradation of DNA templates after transcription reactions• Removing unwanted DNA from samples prior to Northern blotting• Removing DNA during biopharma and bioprocessing procedures... 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% SDS-PAGE.FunctionProbable cell adhesion protein | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More |