| Description | Neuregulin/Heregulin is a family of structurally related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). HRG1-β1 (heregulin-β1, also referred to as NRG1-β1) contains an Ig (immunoglobulin) domain and an EGF (epidermal growth factor)-Neuregulin/Heregulin is a family of structurally related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). HRG1-β1 (heregulin-β1, also referred to as NRG1-β1) contains an Ig (immunoglobulin) domain and an EGF (epidermal growth factor)-like domain that is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. The gene HRG1-β1 is mapped to human chromosome 8p12. Recombinant human Heregulin-β1 is a 7.5 kDa polypeptide consisting of only the EGF domain of heregulin-β1 (65 amino acid residues).Application:Heregulin beta -1 human has been used to enhance proliferation of human dermal fibroblasts (hDFs).Heregulin-β1 human has been used in the culture medium for the maintenance of Schwann cells. It has been used to study P-Rex1 (PI(3,4,5)P3-dependent Rac exchanger 1)-driven fibroblast invasiveness... Read More | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulinPurity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulin, troponin C and tropomyosin. Prevention of actomyosin Mg-ATPase activity is a result of interaction between calponin and actin... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：The HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C)expressed in and purified from Escherichia coli. HRV 3C Protease cleaves protein substrates with the recognition Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：The HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C)expressed in and purified from Escherichia coli. HRV 3C Protease cleaves protein substrates with the recognition sequence Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro between the Gln and Gly residues. The high specificity and affinity tags( 6xHis) of the protease make it an ideal choice for the removal of purification and detection tags on recombinant proteins and allows for flexibility in protease removal.Source：HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C) expressed in and purified from Escherichia coli.HRV 3C enzyme digestion of His-GST-IL33 protein, according to the mass ratio (HRV 3C: target protein) 1:25 and 1:50 enzyme digestion, overnight at 4℃ enzyme digestion results are as follows: completely clean enzyme digestion... 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 | Background：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisitsBackground：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 179 aa extracellular domain (ECD). Within the ECD, rat TNF-alpha shares 94% aa sequence identity with mouse and 69%-76% with bovine, canine, cotton rat, equine, feline, human, porcine, and rhesus TNF-alpha. TNF-alpha is produced by a wide variety of immune, epithelial, endothelial, and tumor cells. TNF-alpha is assembled intracellularly to form a noncovalently linked homotrimer which is expressed on the cell surface. Cell surface TNF-alpha can induce the lysis of neighboring tumor cells and virus infected cells, and it can generate its own downstream cell signaling following ligation by soluble TNFR I. Shedding of membrane bound TNF-alpha by TACE/ADAM17 releases the bioactive cytokine, a 55 kDa soluble trimer of the TNF-alpha extracellular domain. TNF-alpha binds the ubiquitous 55-60 kDa TNF RI and the hematopoietic cell-restricted 80 kDa TNF RII, both of which are also expressed as homotrimers. Both type I and type II receptors bind TNF-alpha with comparable affinity, although only TNF RI contains a cytoplasmic death domain which triggers the activation of apoptosis. Soluble forms of both types of receptors are released and can neutralize the biological activity of TNF-alpha. Post-translational modificationsThe soluble form derives from the membrane form by proteolytic processing.The membrane form, but not the soluble form, is phosphorylated on serine residues.Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid... Read More |