| Description | Inquire | 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≥97% (SDS-PAGE) Endotoxin level<1.0 EU/µgFunctionSupports IL-2 independent and IL-4 independent growth of helper T-cells | Purity>90% SDS-PAGE.Background:Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha and beta chains. The alpha subunit (CG alpha ) is also a component of Follicle-Stimulating Hormone (FSH), ThyroidPurity>90% SDS-PAGE.Background:Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha and beta chains. The alpha subunit (CG alpha ) is also a component of Follicle-Stimulating Hormone (FSH), Thyroid-Stimulating Hormone, and Chorionic Gonadotropin. The unique beta subunit confers the protein’s specific biological action and is responsible for the interaction with its receptor. The approximately 20 kDa human CG alpha subunit shares 73% and 72% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively. The approximately 18 kDa human LH beta subunit shares 71% and 72% aa sequence identity with the mouse and rat orthologs, respectively. Multiple isoforms of LH exist due to differences in the post-translational glycosylation, sialylation, and sulphation modifications of its subunits. The composition, longevity, and activity of the different LH isoforms vary throughout a woman’s menstrual cycle and reproductive life cycle. LH is produced and secreted by the anterior pituitary gland. Its secretion is controlled by Gonadotropin-Releasing Hormone from the hypothalamus; however, LH secretion can also be stimulated by estradiol. LH works in concert with FSH to regulate female reproduction; FSH stimulates follicular growth and LH induces ovulation. LH also drives formation of the corpus luteum by promoting progesterone production. Additionally, LH has been suggested to stimulate the adrenal gland in postmenopausal women to induce secretion of sulfated DHEA, a precursor to androgens. In the testis, LH induces Leydig cell production of testosterone. Hypersecretion of LH has been shown to occur in women with polycystic ovary syndrome and is associated with an increased risk of infertility and miscarriage. Additionally, increased serum LH levels are associated with decreased cognition and have been implicated in the development and progression of Alzheimer’s disease. receptor into an A-frame... Read More | As the most abundant protein in human plasma, human serum albumin (HSA) is the transporter of hormones, lipids and other substances. Its main physiological function is to regulate plasma pH and maintain plasma osmotic pressure.Osrhsa (recombinant human serum albumin from Oryza sativa) is a As the most abundant protein in human plasma, human serum albumin (HSA) is the transporter of hormones, lipids and other substances. Its main physiological function is to regulate plasma pH and maintain plasma osmotic pressure.Osrhsa (recombinant human serum albumin from Oryza sativa) is a recombinant human serum albumin developed by using rice endosperm cell expression platform (oryzhiexp) and purification platform (oryzpur). It does not contain animal derived ingredients and can eliminate the risk of blood derived virus infection. Compared with fetal bovine serum (FBS), plasma derived albumin (pHSA) and bovine serum albumin (BSA), osrhsa has higher purity and better batch stability. It can be used in various research fields, including biopharmaceutical, cell therapy and cell culture of gene therapy. It can replace serum and promote cell growth. At the same time, osrhsa is also widely used in biomedical production as drug carrier, vaccine protector, cell cryoprotectant and medical device embedding agent.ApplicationBiopharmaceuticals, human vaccines, cell culture, cell storage, chemical drug molecular carriers, medical devices, in vitro diagnosis, etc.Comparison of physical and chemical properties between OsrHSA and natural human white pHSAphysicochemical propertiespHSAOsrHSAamino acid sequenceagreementN-terminal amino acidsDAHKSEVDAHKSEVC-terminal amino acidsKLVAASQAALGLKLVAASQAALGLGlycoside modificationnothingmolecular weight (MALDl)66.554 (kDa)66.550 ( a)Isoelectric point (pl)4.84.8Drug binding activityclosethermal stabilitymp 65℃mp 65℃esterase activityidenticalcrystal structureidenticalRestrictions on use:The above products are only suitable for scientific research, laboratory and production use, and cannot be directly used in human body... Read More |