Pepsin from porcine gastric mucosa
SIGMA/P6887 - lyophilized powder, ≥3,200 units/mg protein
Synonym: Pepsin A; Pepsin from hog stomach
CAS Number: 9001-75-6
EC Number: 232-629-3
MDL Number: MFCD00081840
Product Type: Chemical
application(s) | diagnostic assay manufacturing |
biological source | Porcine gastric mucosa |
color | white to off-white |
form | lyophilized powder |
impurities | salt, essentially free |
mol wt | 35 kDa |
Quality Level | 300 |
shipped in | wet ice |
solubility | 10 mM HCl: soluble 4.0 mg/mL (Cold) |
deionized water: soluble 10 mg/mL | |
specific activity | ≥3,200 units/mg protein |
storage temp. | −20°C |
UniProt accession no. | P00791 |
Analysis Note: | Optimum pH is 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH 8.0 - 8.5. |
Analysis Note: | Protein determined by E |
Application: | Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at www.sigma-aldrich.com/enz |
Application: | Pepsin from Sigma has been used along with other enzymes for the determination of enzyme-resistant starch (RS) in bread. It has also been used to simulate in vitro gastrointestinal digestion of pea or whey protein isolates. |
Application: | Pepsin is a peptidase used to digest proteins and is commonly used in the preparation of Fab fragments from antibodies. Pepsin, from porcine gastric mucosa, has been used to hydrolyze dry cervical samples in mice. Product P6887 is provided as a lyophilized powder and has been used to digest protein during dietary fiber analysis. |
Biochem/physiol Actions: | Preferential cleavage: hydrophobic and aromatic residues in P1 and P1′ postitions. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the β chain of insulin |
Biochem/physiol Actions: | Unlike many other peptidases, pepsin hydrolyzes only peptide bonds, not amide or ester linkages. The cleavage specificity includes peptides with an aromatic acid on either side of the peptide bond, especially if the other residue is also an aromatic or a dicarboxylic amino acid. Increased susceptibility to hydrolysis occurs if there is a sulfur-containing amino acid close to the peptide bond, which has an aromatic amino acid. Pepsin will also preferentially cleave at the carboxyl side of phenylalanine and leucine, and to a lesser extent at the carboxyl side of glutamic acid residues. It does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalani |
Other Notes: | View more information on pepsin at www.sigma-aldrich.com/enz |
Packaging: | 1, 5, 10 g in glass bottle |
Packaging: | 250 mg in glass bottle |
Unit Definition: | One unit will produce a ΔA280 of 0.001 per min at pH 2.0 at 37°C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16 ml. Light path = 1 cm.) |
Symbol | GHS07,GHS08 |
Signal word | Danger |
Hazard statements | H315 - H319 - H334 - H335 |
Precautionary statements | P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338 |
Hazard Codes | Xn |
Risk Statements | 36/37/38-42 |
Safety Statements | 22-24-26-36/37 |
RIDADR | NONH for all modes of transport |
WGK Germany | WGK 1 |
Flash Point(F) | Not applicable |
Flash Point(C) | Not applicable |
activity | specific activity: ≥3,200 units/mg protein |
Storage Temp. | −20°C |
Enzyme Commission (EC) Number | 3.4.23.1 ( BRENDA | IUBMB ) |
UNSPSC | 12352204 |