| Description | Native carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine from polypeptides. Inhibited by EDTA and other Zn2+ chelators.Native carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine fromNative carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine from polypeptides. Inhibited by EDTA and other Zn2+ chelators.Native carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine from polypeptides. Inhibited by EDTA and other Zn2+ chelators. Has an optimal pH of 7.0-9.0 and a pI of 6.0... Read More | Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.631 at 1.0 mg/ml for pure C1qMolecular Weight400,000 Da (18 chains)General DescriptionRat C1q is purified from pooled normal rat serum. C1q is part of the C1 complex, which is the first complement component in the classical pathway of Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.631 at 1.0 mg/ml for pure C1qMolecular Weight400,000 Da (18 chains)General DescriptionRat C1q is purified from pooled normal rat serum. C1q is part of the C1 complex, which is the first complement component in the classical pathway of complement. The C1 complex is a non-covalent assembly of three different proteins (C1q, C1r, and C1s) bound together in a calcium-dependent complex. C1q has six extended arms with domains at the end of each arm that bind to the Fc domains of immunoglobulins such as IgG or IgM. When antibodies bind toantigens, forming immune complexes, they cluster allowing two or more of the six C1q arms to bind to the Fc domains of antibodies. Rat IgG2 is very efficient when compared to IgG1 in activating complement (Medgyesi, G.A et., al., 1981). This is in contrast to the human system in which IgG1 activates complement but not IgG2 (Redpath, S. et. al., 1998). The binding of multiple arms of C1q to immune complexes causes the two C1r proteins in the complex (protease zymogens) to auto-activate. The activated C1r proteases cleave and activate the two C1s protease zymogens in the complex. The activated C1s cleaves complement component C4 releasing C4a and initiating covalent attachment of C4b to the activating surface. Activated C1s also cleaves C2 and the larger fragment of C2 binds to the surface-attached C4b forming C4b,C2a, the C3/C5 convertase of the classical pathway.Rat IgG1 cannot activate complement whereas rat IgG2 does.Physical Characteristics & StructureThe apparent molecular weight of rat C1q as determined by gel filtration has been reported to be 400,000 by Veerhuis, R. et al., (1985) and is calculated to be 420,000 based on its amino acid sequence. Rat C1q is a high molecular weight complex of 18 polypeptide chains. Each of the six arms of rat C1q contains three chains, an A chain (~30,000 daltons), a B chain (~28,000 daltons) and a C chain (~26,000 daltons) as determined by SDS/polyacrylamide gel electrophoresis (Wing, M.G. et al., (1993)).FunctionThe biological functions of C1q are described above in the General Description and Physical Characteristics sections.ApplicationsRat C1q can be used to coat ELISA plates to capture and quantitate immune complexes in samples from rat models used for studying immune complex related diseases and conditions.GeneticsNCBI Gene ID numbers for rat C1q are: C1q A chain (298566), C1q B chain (29687), and C1q C chain (362634). The genes for C1q chains A, B and C are all located on chromosome 5. The UniprotKB primary accession numbers for rat C1q are: C1q A chain (P31720), C1q B chain (P31721), and C1q C chain (P31722).Precautions/Toxicity/HazardsThis protein is purified from animal plasma/serum and therefore precautions appropriate for handling any animal blood-derived product must be used.ReferencesMedgyesi, G.A et., Miklos, K., Kulics, J., Fust, G., and Gergely, J. Bazin, H. (1981). Classes and subclasses of rat antibodies: reaction with the antigen and interaction of the complex with the complement system. Immunology 43, 171-176.Redpath, S., Michaelsen, T., Sandlie, I. and Clark, M. R. (1998). Activation of complement by human IgG1 and human IgG3 antibodies against the human leucocyte antigen CD52. Immunology 93, 595–600.Veerhuis, R., Van Es, L.A. and Daha, M.R. (1985). In vivo degradation of rat C1q induced by intravenous injection of soluble IgG aggregates. Immunology 54, 801-810.Wing, M.G., Seilly, D. J., Bridgman, D.J. and Harrison, R.A. (1993). Rapid isolation and biochemical characterization of rat C1 and C1q. Molecular Immunology 30, 433-440... Read More | Inquire | Purity≥ 95% SDS-PAGE; HPLCRelevanceHuman erythropoietin is member of the EPO/TPO family and encodes a secreted, glycosylated cytokine hormone composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and Purity≥ 95% SDS-PAGE; HPLCRelevanceHuman erythropoietin is member of the EPO/TPO family and encodes a secreted, glycosylated cytokine hormone composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types. It is produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals... 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 |