P7125

Pepsin from porcine gastric mucosa

powder, ≥400 units/mg protein

• Synonim(y): Pepsin A, Pepsin from hog stomach
• Numer CAS: 9001-75-6
• Numer EC enzymu: 3.4.23.1 (BRENDA, IUBMB)
• Numer WE: 232-629-3
• Numer MDL: MFCD00081840
• Kod UNSPSC: 12352204
• eCl@ss: 42010127
• NACRES: NA.54

Właściwości

• pochodzenie biologiczne: Porcine gastric mucosa
• Poziom jakości: 200
• Formularz: powder
• aktywność właściwa: ≥400 units/mg protein
• masa cząsteczkowa: 35 kDa
• rozpuszczalność: 10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless
• numer dostępu UniProt: P00791
• temp. przechowywania: 2-8°C
• informacje o genach: pig ... LOC396892(396892)

Opis

Zastosowanie

Pepsin cleavage can be used to produce F(ab′)₂ fragments of antibodies. pepsin at www.sigma-aldrich.com/enzymeexplorer.

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[1] and to digest pathology samples from anal canal carcinomas (ACC) biopsies prior to EGFR staining[2].

The enzyme from Sigma has been used to obtain total vitamin B12 content in food products prior using immunoaffinity columns[3] It has also been used to digest minced soft tissue of snails prior to the isolation of the third stage larvae (L3).[4]

Działania biochem./fizjol.

It does not cleave at valine, alanine, or glycine linkages.[5] Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, or Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion.[5][6] Pepsin is inhibited by several phenylalanine-containing peptides.[7]

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.[8]

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

Definicja jednostki

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.)

Komentarz do analizy

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.

Protein determined by E1%/280

Inne uwagi

View more information on pepsin at www.sigma-aldrich.com/enzymeexplorer.

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Informacja o środkach bezpieczeństwa

• Piktogramy: GHS08,GHS07
• Hasło ostrzegawcze: Danger
• Zwroty wskazujące rodzaj zagrożenia: H315,H319,H334,H335
• Zwroty wskazujące środki ostrożności: P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338
• Klasyfikacja zagrożeń: Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
• Organy docelowe: Respiratory system
• Kod klasy składowania: 11 - Combustible Solids
• Klasa zagrożenia wodnego (WGK): WGK 1
• Temperatura zapłonu (°F): Not applicable
• Temperatura zapłonu (°C): Not applicable
• Środki ochrony indywidualnej: dust mask type N95 (US), Eyeshields, Faceshields, Gloves