Pepsin from porcine gastric mucosa
SIGMA/P7125 - powder, ≥400 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
Pepsin, a member of the Peptidase A1 family . It exhibits preferential cleavage for hydrophobic, preferably aromatic.
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: P7125-100G
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: P7125-500G
| biological source | Porcine gastric mucosa |
| form | powder |
| mol wt | 35 kDa |
| Quality Level | 200  |
| solubility | 10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless |
| specific activity | ≥400 units/mg protein |
| storage temp. | 2-8°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 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 P7125 is provided in powder form. Product P7125 has been used to denature DNA from kidney cells and to digest pathology samples from anal canal carcinomas (ACC) biopsies prior to EGFR staining. |
| Application: | The enzyme from Sigma has been used to obtain total vitamin B12 content in food products prior using immunoaffinity columns It has also been used to digest minced soft tissue of snails prior to the isolation of the third stage larvae (L3). |
| Biochem/physiol Actions: | It does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalani |
| 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 |
| 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 = 16 mL. Light path = 1 cm.) |
| Other Notes: | View more information on pepsin at www.sigma-aldrich.com/enz. |
| Packaging: | 100, 500 g in poly bottle |
| Symbol |   GHS07,GHS08 |
| Signal word | Danger |
| Hazard statements | H315 - H319 - H334 - H335 |
| Precautionary statements | P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - 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: ≥400 units/mg protein |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 3.4.23.1 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |