P7125
Pepsina from porcine gastric mucosa
powder, ≥400 units/mg protein
Sinónimos:
Pepsina A, Pepsina from hog stomach
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About This Item
Productos recomendados
origen biológico
Porcine gastric mucosa
Nivel de calidad
formulario
powder
actividad específica
≥400 units/mg protein
mol peso
35 kDa
solubilidad
10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless
Nº de acceso UniProt
temp. de almacenamiento
2-8°C
Información sobre el gen
pig ... LOC396892(396892)
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Categorías relacionadas
Aplicación
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).
Puede utilizarse hidrólisis con pepsina para producir los fragmentos F(ab′)2 de los anticuerpos. pepsina en www.sigma-aldrich.com/enzymeexplorer
Acciones bioquímicas o fisiológicas
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.
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
Definición de unidad
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.)
Nota de análisis
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
Otras notas
View more information on pepsin at www.sigma-aldrich.com/enzymeexplorer.
inhibidor
Referencia del producto
Descripción
Precios
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Órganos de actuación
Respiratory system
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Protocolos
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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