| Description | Esterase, also known as carboxyl ester hydrolases, are a member of the hydrolytic enzyme superfamily. Esterase is widely present in organisms, such as helping to digest esters in food in the digestive system, and also participating in biological processes such as fatty acid metabolism within cells. Esterase, also known as carboxyl ester hydrolases, are a member of the hydrolytic enzyme superfamily. Esterase is widely present in organisms, such as helping to digest esters in food in the digestive system, and also participating in biological processes such as fatty acid metabolism within cells. Esterase is widely used in industry, such as in the production of biodiesel, food additives, and cosmetics. ≥15U /mg powder, ≥100 U/mg protein. Source: Porcine liver.Properties The molecular weight of esterase monomer is approximately 66kDa. It is a serine enzyme with two active sites on each molecule, which dissociates into active half molecules in the presence of dilute acid or concentrated saltStabilityEsterase acts on water-soluble carboxylic acid esters containing short chain fatty acids. Its function comes from the catalytic triad of Ser, His, and Asp/Glu, which is stable in the form of a triad under low temperature and low pH conditions.Application1、Used for kinetic resolution and asymmetric synthesis in organic chemistry.2、Used to reveal fluorescence in the UV visible spectrum.3、Used in pharmaceutical and industrial applications to catalyze the hydrolysis of pentaacetyl catechins and epicatechin.4、It is used to develop an alternative experimental scheme based on gel for screening bead binding catalytic activity in aqueous media.Attention1、 Avoid contact with skin and eyes.2、 For your safety and health, please wear Lab coat and disposable gloves... Read More | Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.974 at 1.0 mg/ml for pure C3bMolecular Weight185,000 Da (2 chains)General DescriptionCynomolgus monkey C3 (cyno C3) is purified from pooled normal cynomolgus monkey serum. C3 is central to the activation of all three pathways of Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.974 at 1.0 mg/ml for pure C3bMolecular Weight185,000 Da (2 chains)General DescriptionCynomolgus monkey C3 (cyno C3) is purified from pooled normal cynomolgus monkey serum. C3 is central to the activation of all three pathways of complement activation (Law, S.K.A. and Reid, K.B.M. (1995)). Initiation of each pathway generates proteolytic enzyme complexes (C3 convertases) which are bound to the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. For a brief time (~60 µs) this nascent C3b is capable of reacting with and covalently coupling to hydroxyl groups on the target surface. Carbohydrates are the favored target, but protein hydroxyls and amino groups also react. This process of tagging the target surface with C3b is called opsonization. The reactive site in nascent C3b is a thioester (Tack B.J., et al. (1980); Pangburn M.K. and MüllerEberhard H.J. (1980)) and C3b is linked to the target through a covalent ester bond (an amide bond is formed if C3b is attached to amino groups). Most of the C3 activated during complement activation never attaches to the surface because its thioester reacts with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all three pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane. Surface-bound C3b and its breakdown products iC3b and C3d are recognized by numerous receptors on lymphoid and phagocytic cells which use the C3b ligand to stimulate antigen presentation to cells of the adaptive immune system. The end result is an expansion of target-specific B-cell and T-cell populations.Physical Characteristics & StructureCynomolgus monkey C3 is an uncharacterized protein. The calculated molecular weight based on its amino acid sequence is 184,926 daltons similar to that of human C3 (185,000 daltons). Like human C3, cyno C3 is composed of two disulfide-linked chains. Analysis of purified cyno C3 by SDS/polyacrylamide gel electrophoresis under non-reduced conditions shows the mobility of cyno C3 to be similar to that of human C3. Under reduced conditions, the migration of the alpha chain of cyno C3 is comparable to that of human C3 alpha chain (110,000 daltons) while the beta chain migrates slightly ahead of the human C3 beta chain (75,000daltons).The extinction coefficient of cyno C3 is calculated from its amino acid sequence using ProtParam and assumes all pairs of Cys residues form cystines (i.e. a pair of cystine molecules are joined by a disulfide bond). The theoretical pI value for cyno monkey C3 is 6.03. Employing immunoturbidimetric method the serum concentration of cyno C3 has been reported to be 1.27 mg/ml in males and 1.1 mg/ml in female monkeys (Park H-K et al., (2016)). FunctionThe biological functions of C3 are described above in the General Description and Physical Characteristics sections.GeneticsCynomolgus monkey C3 chromosome location 19. The NCBI Gene ID number for Cynomolgus monkey C3 is 102131458 and UniProt accession number is A0A2K5VPN1.Precautions/Toxicity/HazardsThis protein is purified from animal serum and therefore precautions appropriate for handling any animal blood-derived product must be used.ReferencesLaw, S.K.A. and Reid, K.B.M. (1995) Complement 2nd Edition (ISBN 0199633568) Oxford University Press, Oxford.Tack BF, Harrison RA, Janatova J, Thomas ML, Prahl JW. (1980) Evidence for presence of an internal thiolester bond in third component of human complement. Proc Natl Acad Sci U S A. 77:5764-8.Pangburn M.K. and Müller-Eberhard H.J. (1980) Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement. J Exp Med. 152:1102-14.Park H-K, Cho J-W, Lee B-S, Park H, Han J-S, Yang M-J, Im W-J, Park D-Y, Kim W-J, Han SC, Kim Y-B. (2016) Reference values of clinical pathology parameters in cynomolgus monkeys (Macaca fascicularis) used in preclinical studies. Lab Anim Res. 32(2):79-86... Read More | Purity>97% SDS-PAGE.FunctionReceptor for interleukin-2 | VEGF permeability factor, also known as Vascular permeability factor (VPF), is a highly specific permeability factor for endothelial growth factor. It can promote the increase of vascular permeability, extracellular matrix degeneration, vascular endothelial cell migration, proliferation and VEGF permeability factor, also known as Vascular permeability factor (VPF), is a highly specific permeability factor for endothelial growth factor. It can promote the increase of vascular permeability, extracellular matrix degeneration, vascular endothelial cell migration, proliferation and angiogenesis. VEGF has also been shown to have chemotaxis on monocytes and osteoblasts.OsrhVEGF is expressed by oryza sativa and purified by protein purification technology... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidicPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence mechanism.A35R could block some stage of antigen processing or presentation in infected cells or interfere with regulation of apoptosis. In addition, the A35R function may be required for growth in certain cell types, e.g., macrophage, in vivo. It localizes to factories where viral DNA is located and it was shown to be a constitutive transcriptional activator in a large-scale yeast two-hybrid study... Read More |