V8 Protease | Product Advantage |
Sequence analysis of pure trypsin: high specificity, good stability. Free of animal origin: recombinant production, no exogenous virus contamination, the production process does not use any animal source raw materials. Quality: Mass production can ensure stable and continuous batch production; there is no difference between product batches and the quality is stable. Purity: specific activity is high; the host protein residue is less than the limit requirement of biological products. Freeze dried powder: easy to store and transport. Compliance with regulatory requirements: The production equipment and production environment comply with relevant regulatory requirements, and the production process is fully followed. NSF ISO 9001: 2015 quality system and comply GMP guiding principles. Quality documents complete: According to customer needs, can provide relevant regulatory support documents. |
| Product Application | Can be used alone or in combination with other proteases when used in performing protein digestion sequencing, peptide mapping, and peptide mass fingerprinting. |
| Basic Characteristics | V8 protease was active at pH 4.0-10.0, and the optimum pH was 8.0-8.5. The inhibitors of V8 protease are diisopropyl fluorophosphate (DFP), α2-macroglobulin and Nα-P-tosyl-L-lysine chloromethyl ketone (TLCK). |
| Method of Use |
Note before use: can be divided according to the amount of use to minimize contamination or self-cutting. Objective Protein Dissolution: Dissolve the target protein with an enzyme cutting buffer, e.g. 25-50 mM NH4HCO3 pH7.8, if the solubility is not good to denature the target protein, add urea, SDS, DTT or heat. Enzyme cutting: V8 protease to target protein is 1/20-1/100 (W/W), and the enzyme is cut at 25°C or 37°C for 2-18h. |
| Dissolution |
Water or 50 mM Tris-HCl pH8.0 is dissolved, it is stored below -20°C (1 mg/ml) and stable for 6 months. Water or 50mM Tris-HCl pH8.0 is dissolved, it is stored at 4°C(1 mg/ml, sterile) and stable for 2 months. Use 50mM Tris-HCl pH8.0 is dissolved, it is stored at 25°C or 37°C (0.5 mg/ml) for 12h, and the activity can be maintained above 85%. After dissolution, the solution can be frozen and thawed repeatedly for 10 times without activity loss. |
| Sizes | 100ug; 1mg; 2mg |
| Cutting Sites | V8 protease belongs to the serine protease family, which can specifically hydrolyze glutamic acid (Glutamic acid, E) or aspartic acid (Aspartic acid, D) residue carboxyl side peptide bond. At pH7.8 and CH3COONH4 buffer of pH 4.0, and the carboxy-terminal peptide bond of Glu or Asp was recognized and cleaved in phosphate buffer of pH 7.8, and the hydrolysis rate of Glu was higher than that of Asp. |
| Appearance | White, almost white, like yellow powder |
| Specific Activity | ≥ 5.0 U/mg pro. |
| Protein Electrophoresis | Single Master Strip |
| Molecular Weight (Protein Electrophoresis) | 24.0±2.4 kDa |
| Remarks | The amount of enzyme required to catalyze the substrate (Z-Phe-Leu-Glu-4-nitranilide) to produce 1 μmol of p-nitroaniline (4-nitroaniline) per minute at 25°C, pH 7.8 is one enzymatic activity unit. |
| Storage | Storage stability: recombinant V8 protease lyophilized powder stored at 2-8°C, 24 months stability. |
| Transportation | Transport stability: blue ice insulation transport, stable activity. |
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