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Trypsin cryst dcc, 250 mg

Trypsin cryst dcc, 250 mg

$96.15

SKU: 0210492283

Synonyms
Parenzymol; Parenzyme; Tryptar; Trypure; U-4858
CAS Number:
9002-07-7
Molecular Weight:
mol wt 23.8 kDa(Lit.)
EC Number:
232-650-8
MDL Number:
MFCD00082094
Packaging size:
250 mg
Product Description

Crystallized and treated with diphenylcarbamyl chloride (DCC) to inhibit chymotrypsin. The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding. Trypsin consists of a single chain polypeptide of 223 amino acid residues. Trypsin is produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys- Ile peptide bond. The amino acid sequence of trypsin is crosslinked by 6 disulfide bridges. This native form of trypsin is referred to as β-trypsin. Autolysis of β-trypsin (which is cleaved at Lys- Ser) results in a-trypsin which is held together by disulfide bridges. Trypsin is a member of the serine protease family. The active site amino acid residues of trypsin include His and Ser.

Application Notes

Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin has been used in a study to assess the efficacy of polyethyleneglycol/sodium citrate aqueous two-phase extraction systems. Trypsin has also been used in a study to investigate peptide-ligand affinity chromatography adsorbents. Tyrpsin is a serine protease used to hydrolyze proteins. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins . Can be used in the isolation of intact, detergent-free phycobilisomes and in the hydrolysis/condensation of carboxylic ester bonds.

Usage Statement

Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.

Specifications
SKU 0210492283
Alternate Names Parenzymol; Parenzyme; Tryptar; Trypure; U-4858
Application Notes Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin has been used in a study to assess the efficacy of polyethyleneglycol/sodium citrate aqueous two-phase extraction systems. Trypsin has also been used in a study to investigate peptide-ligand affinity chromatography adsorbents. Tyrpsin is a serine protease used to hydrolyze proteins. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins . Can be used in the isolation of intact, detergent-free phycobilisomes and in the hydrolysis/condensation of carboxylic ester bonds.
Base Catalog Number 10492283
Biochemical Physiological Actions Tyrpsin cleaves peptide chains, amides and esters mainly at the carboxyl side of the amino acids lysine or arginine. Tyrpsin plays an important role in digestion and protein absorption. Tyrpsin originates in the pancreas in the form of the zymogen, trypsinogen.
CAS # 9002-07-7
EC Number 232-650-8
Extinction Coefficient Extinction coefficient: E1%280 = 14.3(Lit.)
Grade DCC treated
Hazard Statements H315-H319-H334-H335
Molecular Weight mol wt 23.8 kDa(Lit.)
Pack Size 250 mg
Personal Protective Equipment Dust mask, Eyeshields, Faceshields, Gloves
pH Optimum pH: Approximately 8.0(Lit.)
RTECS Number YN5075000
Safety Symbol GHS07, GHS08
Solubility Soluble in water; practically insoluble in alcohol and glycerol. Soluble in 1 mM HCl (1 mg/mL).
Usage Statement Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.
Citations
Documents

Material Safety Data Sheet

Material Safety Data Sheet
English (United States)

Certificates of Analysis

Certificates of Analysis
English (United States)