Recombinant Trypsin from E. coli

 Product Information

Cat #
MBS-1910
CAS No.
9002-0 7-7
Enzyme Commission Number
EC 3.4.21.4
Product Overview
Trypsin is a serine protease that specifically cleaves lysine and arginine C-terminal peptide bonds. The amino acid sequence of the recombinant trypsin is exactly the same as the trypsin derived from porcine pancreas, and has the same enzymatic properties as the porcine trypsin derived from animal. It can replace trypsin derived from porcine pancreas in various in a biotechnological process. The optimal pH of recombinant trypsin is 7.0-11.0.
Features
Ready-to-use product, accelerating research progress, enhancing application performance.
Method
Technology
Synonyms
Type
Function
Applications
Pharmaceutical Industry
Storage
-18°C
Storage Buffer
Shelf Life
Stored in lyophilized form at -18°C, it is stable for 24 months.
Strains
Escherichia coli
Source
E. coli
Appearance
Molecular Weight
23.5kD
Color / Form
freeze-dried white, off-white powder
Instruction
Avoid multiple freeze-thaw cycles.
Avoid inhalation during use, prevent contact with skin or mucous membranes, and rinse with water immediately after accidental contact.
Enzyme Class
Hydrolases
Production Methods
Recombinant trypsin, produced by genetic engineering, expressed in Escherichia coli
Activity
Specific Enzyme Activity
≥3800 USP units/mg pro
Purity
Unit Definition
Amino Acids Sequence
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPWVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN
WARNINGS
Shipping
Timely shipping by optional means
Formula
Reaction
Recommendation
Species Reactivity
Contents
Compatibility
Melting Point
Final Titre
Fermentation Time
Recovery Yield
Starting Material
Specification
On customer requests
Substrates
Concentration
Usage And Dosage

 Description

Trypsin is found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.

For Research Use Only.
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