Saltar al contenido
Merck

P7125

Pepsina from porcine gastric mucosa

powder, ≥400 units/mg protein

Sinónimos:

Pepsina A, Pepsina from hog stomach

Iniciar sesión para ver los precios por organización y contrato.

Seleccione un Tamaño

Cambiar Vistas

Acerca de este artículo

Número CAS:
UNSPSC Code:
12352204
eCl@ss:
42010127
EC Number:
232-629-3
NACRES:
NA.54
MDL number:
Número CE:
Specific activity:
≥400 units/mg protein
Biological source:
Porcine gastric mucosa
Servicio técnico
¿Necesita ayuda? Nuestro equipo de científicos experimentados está aquí para ayudarle.
Permítanos ayudarle


biological source

Porcine gastric mucosa

Quality Segment

form

powder

specific activity

≥400 units/mg protein

mol wt

35 kDa

solubility

10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless

UniProt accession no.

storage temp.

2-8°C

Gene Information

Application

Puede utilizarse hidrólisis con pepsina para producir los fragmentos F(ab′)2 de los anticuerpos. pepsina en 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 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).

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.
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.
Escisión preferente: residuos hidrófobos y aromáticos en las posiciones P1 y P1′. Rompe los enlaces Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe y Phe-Tyr en la cadena β de la insulina

Analysis Note

pH óptimo es 2-4. Activa en urea 4 M y HCl de guanidina 3 M. Estable a 60 ºC. La pepsina se desactiva de manera irreversible a pH 8,0 - 8,5.
Protein determined by E1%/280

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


Still not finding the right product?


pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves



Elija entre una de las versiones más recientes:

Certificados de análisis (COA)

Lot/Batch Number

It looks like we've run into a problem, but you can still download Certificates of Analysis from our Documentos section.

Si necesita más asistencia, póngase en contacto con Atención al cliente

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos