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C4879

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

Sinónimos:

chymotrypsin A zymogen

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Talla/SKUDisponibilidadPrecio
100 mg
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59,40 €
250 mg
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75,90 €
1 g
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287,00 €
5 g
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543,00 €

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Número CAS:
UNSPSC Code:
12352204
EC Number:
232-905-3
NACRES:
NA.54
MDL number:
Specific activity:
≥40 units/mg solid
Biological source:
bovine pancreas

59,40 €


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biological source

bovine pancreas

Quality Segment

type

Type II

form

essentially salt-free, lyophilized powder

specific activity

≥40 units/mg solid

mol wt

25,656 Da by calculation

purified by

6× crystallization

solubility

1 mM HCl: soluble 10 mg/mL, clear, colorless

UniProt accession no.

foreign activity

α-chymotrypsin ≤1 U/mg (prior to activation by trypsin)

storage temp.

−20°C

Gene Information

cow ... CTRB1(618826)

General description

Chymotrypsinogen from bovine pancreas is a zymogen containing 5 disulfide bridges. It has an isoelectric pH of 8.97.

Application

The enzyme from Sigma has been used in the non-invasive determination of solid-state protein conformation using near infrared (NIR) spectroscopy. It has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. The enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. In this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution.
α-Chymotrypsinogen A from bovine pancreas has been used as model protein crystallization reproducibility studies. It has also been used in the hydrolysis of α-gliadins prior to mass spectroscopy studies.

Biochem/physiol Actions

A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the peptide bond.
Chymotrypsinogen A requires limited proteolysis for its activation. Chymotrypsinogen A may be activated by trypsin and chymotrypsin (autolytic activation) to form m α, β, γ, δ and π chymotrypsin (depending upon the conditions of activation). Chymotrypsin is a protease that will preferentially cleave peptides on the carboxyl side of aromatic amino acids including tryptophan, tyrosine, and phenylalanine. It will also hydrolyze peptides on the carboxyl side of leucine, methionine, and alanine.

Other Notes

After activation to Chymotrypsin, one unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

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Este artículo
C7762C3142C6423
description

essentially salt-free, lyophilized powder

description

Type I-S, essentially salt-free, lyophilized powder

description

(TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein

description

suitable for protein sequencing, salt-free, lyophilized powder

specific activity

≥40 units/mg solid

specific activity

≥40 units/mg protein

specific activity

≥40 units/mg protein

specific activity

-

biological source

bovine pancreas

biological source

-

biological source

-

biological source

-

Gene Information

cow ... CTRB1(618826)

Gene Information

cow ... CTRB1(618826)

Gene Information

cow ... CTRB1(618826)

Gene Information

cow ... CTRB1(618826)

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

salt-free, lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

UniProt accession no.

P00767

UniProt accession no.

P00767

UniProt accession no.

P00767

UniProt accession no.

P00767


Clase de almacenamiento

11 - Combustible Solids

¿Qué está pasando?

WGK 3

Punto de inflamación (°F)

Not applicable

Punto de inflamación (°C)

Not applicable

EPI (equipos de protección individual)

Eyeshields, Gloves, type N95 (US)



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