| Description | Is it sterile: YesMetallozyme is a water-soluble protein using recombinant genes, lyophilized and irradiated with cobalt-60, and aseptic packaging of celine bottles. A recombinant gene protein constructed according to the chemical structure of cephalosporins and penan. The active center of its gene Is it sterile: YesMetallozyme is a water-soluble protein using recombinant genes, lyophilized and irradiated with cobalt-60, and aseptic packaging of celine bottles. A recombinant gene protein constructed according to the chemical structure of cephalosporins and penan. The active center of its gene fragment can destroy the chemical structural formula of cephalosporins and penan antibiotics, so that the antibacterial properties of the two drugs are lost after ring opening/chain breaking.When doing sterility check of antibiotics, use a manual syringe to absorb sterile water and inject it into the drug vial, shake well, dissolve, and then suck it out. Add to 500ml solution of 0.9% sodium chloride, shake well, do not dissolve with the needle on the incubator, input, avoid high concentration of solution through the filter membrane, resulting in difficult to rinse thoroughly.Here, it is emphasized again: when doing sterile examination of antibiotics, it is necessary to inject sterile water into the manual syringe to dissolve the sample, and then transfer the dissolved sample to 500ml solution of 0.9% sodium chloride, so that the sample will not cause local concentration too high, difficult to wash thoroughly through the filter membrane.During sterility test, take 1 bottle of freeze-dried metal enzyme powder and add 5ml of sterile water to dissolve, shake well to make a metal enzyme solution, take 2ml of enzyme solution and put 1500ml of washing solution and shake well. After the rinse solution has washed the filter membrane of the incubator, the pump is exhausted. A manual syringe was used to Pierce the respiratory mouth of the three incubators, and 1ml of enzyme solution was added to each of them, and the enzymes were spread on the entire surface of the filter membrane as far as possible. Then, the high concentration of enzymes was fully in contact with the filter membrane of the incubator, so as to destroy (neutralize and inactivate) the residual cephalosporins and penem drugs on the filter membrane, and then pumped into the corresponding medium and shook well. Positive pairs were treated with 1ml of E. coli (100CFU/ml).Adding 1ml of the metal enzyme solution to the three incubators can remove the residual cephalosporins and penem on the inner wall of the incubators and the surface of the filter membrane.Shake the positive pair gently once a day in the morning and afternoon.Customers can do methodological verification according to the above, but also according to the actual operation of the verification... 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 | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 5.68 | Inquire | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems... Read More |