P7125
Pepsina
powder, ≥400 units/mg protein
Sinonimo/i:
Pepsina, Pepsina A
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About This Item
Prodotti consigliati
Origine biologica
Porcine gastric mucosa
Livello qualitativo
Forma fisica
powder
Attività specifica
≥400 units/mg protein
PM
35 kDa
Solubilità
10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless
N° accesso UniProt
Temperatura di conservazione
2-8°C
Informazioni sul gene
pig ... LOC396892(396892)
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Categorie correlate
Applicazioni
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.
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).
La scissione con pepsina può essere utilizzata per produrre frammenti F(ab′)2 di anticorpi. pepsina su www.sigma-aldrich.com/enzymeexplorer.
Azioni biochim/fisiol
It does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, or Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion. Pepsin is inhibited by several phenylalanine-containing peptides.
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.
Pepsin is the major proteolytic enzyme produced in the stomach. It digests proteins through the cleavage of interior peptide linkages.
Scissione preferenziale: residui idrofobi e aromatici nelle posizioni P1 e P1′. Scinde i legami Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe e Phe-Tyr nella catena β dell′insulina.
Definizione di unità
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.)
Risultati analitici
Il PH ottimale è compreso tra 2 e 4. Attivo in 4 M di urea e 3 M di guanidina HCl. Stabile a 60 °C. La pepsina viene inattivata irreversibilmente in presenza di pH 8,0 - 8,5.
Protein determined by E1%/280
Altre note
View more information on pepsin at www.sigma-aldrich.com/enzymeexplorer.
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organi bersaglio
Respiratory system
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Certificati d'analisi (COA)
Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.
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Protocolli
This procedure may be used for determination of Pepsin activity using hemoglobin as the substrate. It is a spectrophotometric stop rate determination.
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