Sequencing grade trypsin (freeze-dried powder)
Product specification: 100 μg | 1mg
Storage temperature: 2-8 ℃
Nickname: Recombinant modified trypsin; Recombinant methylated modified trypsin; Recombinant Methylation Modified Mutant Trypsin
Source: Recombinant trypsin, genetically engineered production, expressed in Escherichia coli
Protein sequence: The amino acid sequence is completely consistent with the cationic trypsin derived from pig pancreas.
1. Product Introduction
Recombinant trypsin is expressed and produced by recombinant Escherichia coli, with an amino acid sequence that is completely consistent with cationic trypsin derived from pig pancreas. It is free from contamination by chymotrypsin and other miscellaneous enzymes, and does not contain or require TPCK to inhibit other enzyme activities. It has high activity and high cleavage specificity. Trypsin is prone to self cleaving and producing its own self cleaving fragments, which affect the results of mass spectrometry analysis. Methylation modification and mutation ensure that it does not self cleave, thereby removing the activity of pseudochymotrypsin produced by self cleaving.
2. Product characteristics
Source: Recombinant Escherichia coli
Appearance: White, almost white powder
Specific activity (units/mg protein) ≥ 4500 USP units/mg pro
Protein electrophoresis: single main band
Electrophoresis (molecular weight) 24.0 ± 2.4 kDa
Purity (HPLC) ≥ 95%
3. Recommended usage method
It is recommended to dissolve or dilute with 50mMHAc or 1mM HCl. When using, dilute in a buffer solution of 50mM NH4HCO3 or pH 7.0-8.0. It is recommended to use 1mM CaCl2 in the enzyme digestion buffer, recombinant trypsin: target protein=1:20-1:100, and the optimal pH is 7.0-8.0.
4. Storage and transportation stability
Storage stability: Recombinant trypsin freeze-dried powder is stable at 2-8 ℃ for 24 months; Dissolve in 50mMHAc or 1mM HCl and store at -20 ℃, repeatedly freeze thaw 5 times, without any loss of activity.
Transportation stability: Blue ice insulation transportation, stable activity.
5. Product Advantages
Sequence analysis of pure protease: high specificity and good stability.
No animal origin: Recombinant production, no exogenous virus pollution, and the production process does not use any animal origin raw materials.
Stable quality: Batch production can ensure stable and continuous batch production; There is no difference between product batches and the quality is stable.
High purity: high specific activity; The residual host protein is less than the limit requirement for biological products.
Freeze dried powder: Easy to store and transport.
Compliance with regulatory requirements: The production equipment and environment comply with relevant regulatory requirements, and the production process fully follows the NSF ISO 9001:2008 quality system and GMP guidelines.
Complete quality documents: According to customer requirements, relevant regulatory support documents can be provided.
6. Product Usage
Recombinant trypsin has the same enzymatic properties as animal derived trypsin. It can be used as a substitute for trypsin and has many advantages, such as no mixed enzyme activity, high stability, non self cleavage, and high activity; In use, there are no non-specific enzyme cleaved fragments or self cleaved fragments present. Used for specific protein enzymatic hydrolysis, protein sequencing, peptide mapping, proteomics research, pancreatic enzyme digestion of peptide segments on Z-D gel, etc.
