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Native Bovine Trypsin

Cat No.
NATE-0721
Description
Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, 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.
Abbr
Trypsin, Native (Bovine)
Alias
trypsin
Source
Bovine pancreas
Species
Bovine
Applications
For trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps. Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin has been used in a study to assess the effects of macromolecular crowding on the structural stability of human α-lactalbumin. Trypsin has also been used in a study to investigate BN-PAGE analysis of Trichoderma harzianum secretome.
Product Overview
Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys-lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys-Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family.
Form
lyophilized powder
Enzyme Commission Number
EC 3.4.21.4
Activity
~10 ,000 BAEE units/mg protein; TPCK Treated, essentially salt-free, lyophilized powder, > 10 ,000 BAEE units/mg protein; > 2,500 USP units/mg solid; > 6 ,000 BAEE units/mg protein; essentially salt-free, lyophilized powder, > 9 ,000 BAEE units/mg protein
CAS No.
9002-07-7
Molecular Weight
23.8 kDa
Unit Definition
One BAEE unit will produce a ΔA253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate. One BTEE unit = 320 ATEE units
Storage
Solutions in 1 mM HCl are stable for 1 year in aliquots and stored at-20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS.
Buffer
Solubilizing trypsin should be done with a buffered salt solution containing no Ca2+ or Mg2+. This product is from pancreas sourced from New Zealand. It is soluble in 1 mM HCl at 1 mg/mL.
Pathway
Cell surface interactions at the vascular wall, organism-specific biosystem (from REACTOME) Class A/1 (Rhodopsin-like receptors), organism-specific biosystem (from REACTOME) Common Pathway, organism-specific biosystem (from REACTOME) Complement and Coagulation Cascades, organism-specific biosystem (from WikiPathways) Complement and coagulation cascades, organism-specific biosystem (from KEGG) Complement and coagulation cascades, conserved biosystem (from KEGG)
Function
the weaker rapid interaction between prothrombin and membranes is the most important in vivo when considering the activation of prothrombin at the cell surface. novel pyranosic sulfated arabinan Ab1 exerts its anticoagulant activity on thrombin by a mechanism different from those found previously for other sulfated polysaccharides and glycosaminoglycans Exogenous delivery of thrombin enhances microvascular collateral development in response to ischemic insult, and accelerates tissue reperfusion.
Synonyms
α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin
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TRYPSIN-TPCKDITC-GLASS -Enzymatic Assay Protocol
protease -Enzymatic Assay Protocol
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