Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococcus, is an extremely potent antistaphylococcal agent. Its molecular weight is 27kDa and is comprised of 246 amino acids. The isoeletric point of it is 10.5-11.0. The key enzymatic reaction of lysostaphin is the specific cleavage of the Gly-Gly bond in the pentaglycine subunit of the cell wall peptidoglycan and lyses cells in all metabolic states. Lysostaphin also hydrolyzes glycine-rich proteins such as insoluble elastin. .Both activities have a pH optimum in the neutral range and are inhibited by agent that would chelate the endogenous zinc, suggesting that zinc interferes directly with the catalytic activity of the enzyme. Lysostaphin has been in animals and topically in man against certain infections. It is used as a research and diagnostic tool. Because it lyses staphylococcus efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in studies aimed at tracing source of infection or bacterial contamination.
Lysostaphin(CAS:9011-93-2)
A-lactamase, recombinant urate-oxidase for injection, recombinant enterokinase, lysostaphin, recombinant human keratinocyte growth factor-2, recombinant human bone morphogenetic protein-2, a-lactamase test kits.
Penicillinase is also called A-lactamase, which hydrolyze A-lactamse. More than 200 A-lactamase were found by far, and can be classified according to the molecular biology or the BUSH classification system, the two major classification systems for A-lactamase. Penicillinase can be used to eliminate A-lactams pollution, such as those in hospital, on medical apparatus and in foods. The enzyme we providing is TEM1, which belongs to molecular biology classification group A and BUSH classification Class II, with a M.W. of 29 kDa and PI of 5.4. We provide both natural and fusion form of this enzyme. Physical Appearance: Lyophilized powder Formulation: 20mM pB, pH7.0 Solubility: The product is soluble (1.0 mg/ml) in 20mM pB, pH7.0. The solution can be filtered through a 0.2 m, low protein-binding membrane. Stability: It is recommended to store the product desiccated at -18 C . The product as supplied is stable for 1 year when stored properly. The product is stable in solution for at least three weeks at 2 - 8 C . Purity: RP-HPLC 90% SEC-HPLC 90% reducing and non-reducing SDS-PAGE 90% Amino-Acid Sequence : The sequence of the first five N-terminal amino acids was determined and was found to be Met-His-Pro-Glu-Thr Specific Activity: 1200 IU/mg.
Description: Recombinant urate-oxidase (rUOX) produced in E.Coli is a tetrameric protein with identical subunits of a molecular mass of about 34 kDa. The cDNA coding for urate-oxidase was cloned from a strain of Aspergillus flavus . The monomer, made up of a single 302 amino acid polypeptide chain, has no intra- or inter-disulfide bridges. Urate oxidase (uricase EC 1.7.3.3) is an enzyme of the purine breakdown pathway that catalyses the oxidation of uric acid to allantoin. It is present in many different organisms, but not in higher primates including human. Hyperuricaemia is most commonly associated with gout and also occurs in patients with malignancy, especially those with lymphoid malignancies due to rapid cell turnover and an increased rate of purine metabolism. Physical Appearance : Sterile Filtered White lyophilized (freeze-dried) powder. Formulation & Packaging : The protein was lyophilized from a concentrated (1.5mg/ml) solution. Solubility : The lyophilized rUOX is very soluble in water and most aqueous buffers. Stability : Lyophilized rUOX although stable at room temperature, should be stored desiccated below 0C. Reconstituted rUOX is best stored refrigerated at 4C.
Description : Recombinant Enterokinase is a highly purified preparation of the light chain of bovine enterokinase with high specificity and recognizes the identical cleavage site as the native enzyme. The product cleaves fusion proteins with sequence (Asp-Asp-Asp-Asp-Lys ) at¡¡the C-terminal of Lysine. The enzyme is produced in recombinant E.coli and purified to high homogeneity with specificity of 30,000U/mg. It can work at various different conditions, such as 4-45 degree, pH4.5-9.5, even in some detergents or denature reagents. Activity : One unit is defined as the amount of enzyme that will cleave 95% of 50 g fusion protein in 16 hours at 23 in 1x reaction buffer. 10x Reaction Buffer 500 mM Tris-HCl, pH 8.0 10 mM CaCl 2 1% Tween-20 (v/v) 1. For 1 liter, dissolve 60.5 g Tris base in 950 ml deionized water. 2. Adjust pH to 8.0 with concentrated HCl. 3. Add 1.47 g CaCl2-2H2O and 10 ml Tween-20 and mix. 4. Adjust the volume to 1 liter. Store at room temperature. Storage : 20mmol/L Tris-HCl 200mmol/L NaCL 2mmol/L CaCl 2 50% Glycerol Stored at -20 Stability : Stable at -20, can be used up to one year.
Description: Human Keratinocyte growth factor-2 (KGF-2 or FGF-10) is a novel human protein that stimulates the repair of injured mucosal tissues. KGF-2 directly promotes wound-healing by stimulating the proliferation, migration and differentiation of epithelial cells, and has direct chemotactic effects on tissue remodeling. KGF-2 also appears to result in less scarring. Recombinant Human KGF-2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids with molecular weight of about 19.3kD. Recombinant human KGF-2 is highly related to KGF-1(FGF-7) and binds to the same receptor as KGF-1 and shares 57% sequence homology. Recombinant KGF-2 is purified by proprietary chromatographic techniques. Source : Escherichia Coli. Physical Appearance : Sterile Filtered White lyophilized (freeze-dried) powder. Formulation : Lyophilized from a concentrated (1mg/ml) solution in water containing 40mM Sodium Phosphate buffer, pH 7.4 , 20 mM NaCl. Solubility : It is recommended to reconstitute the lyophilized KGF -2 in sterile 18M-cmH2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions. Stability : Lyophilized KGF-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18 . Upon reconstitution KGF-2 should be stored at 4 between 2-7 days and for future use below -18 . For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles. Amino-Acid Sequence :The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Leu-Gly-Asp. Dimers and aggregates :Less than 1% as determined by silver-stained SDS-PAGE gel analysis. Biological Activity :Recombinant human KGF-2 is fully biologically active when compared to standards. The specific activity is about 1.0 x 10 6 Units/mg.
