Pepsin from porcine gastric mucosa
SIGMA/P7012 - lyophilized powder, ≥2,500 units/mg protein (E1%/280 )
Synonym: Pepsin A; Pepsin from hog stomach
CAS Number: 9001-75-6
EC Number: 232-629-3
MDL Number: MFCD00081840
Product Type: Chemical
Pepsin, a member of the Peptidase A1 family . It exhibits preferential cleavage for hydrophobic, preferably aromatic.
| application(s) | diagnostic assay manufacturing |
| color | off-white to yellow |
| form | lyophilized powder |
| mol wt | 35 kDa |
| Quality Level | 300  |
| solubility | 10 mM HCl: soluble 4 mg/mL (Cold) |
| deionized water: soluble 10 mg/mL | |
| specific activity | ≥2,500 units/mg protein (E |
| storage temp. | −20°C |
| UniProt accession no. | P00791  |
| Analysis Note: | E |
| 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 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. |
| Application: | The enzyme from Sigma has been used in the digestion of crude wheat gliadin. It has been used along with other enzymes to demonstrate the effects of fixation and enzymatic digestion in immunohistochemical assays, using paraffin embedded tissue. It has been used for digestion (before using immunoperoxidase techniques) to reduce non-specific background staining in sections of bronchial tissues. The enzyme has also been used in the preparation of F(ab)2 fragment from IgG. |
| Biochem/physiol Actions: | Pepsin hydrolyzes peptide bonds, not amide or ester linkages. Pepsin cleaves peptides with an aromatic acid on either side of the peptide bond. Sulfur-containing amino acids increase susceptibility to hydrolysis when they are close to the peptide bond. Pepsin preferentially cleaves at the carboxyl side of phenylalanine and leucine and at the carboxyl side of glutamic acid residues. 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 Pepsin is the major proteolytic enzyme produced in the stomach. It digests proteins through the cleavage of interior peptide linkages. |
| 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: | The enzyme does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalani |
| Other Notes: | 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 = 16mL. Light path = 1cm.) |
| Other Notes: | View more information on pepsin at www.sigma-aldrich.com/enz. |
| Packaging: | 1, 5, 10, 25, 100 g in poly bottle |
| Packaging: | 250 mg in poly bottle |
| 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: ≥2,500 units/mg protein (E |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 3.4.23.1 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |