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C4879

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

Synonym(s):

chymotrypsin A zymogen

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100 mg
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$69.10
250 mg
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$87.40
1 g
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$189.00
5 g
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$659.00

About This Item

CAS Number:
9035-75-0
UNSPSC Code:
12352204
EC Number:
232-905-3
NACRES:
NA.54
MDL number:
MFCD00130483
Specific activity:
≥40 units/mg solid
Biological source:
bovine pancreas

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biological source

bovine pancreas

Quality Level

200

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.

P00767

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.[1] It has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems.[2] 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.[3]
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.
View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer

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This Item
C3142C7762C4129
α-Chymotrypsinogen A from bovine pancreas essentially salt-free, lyophilized powder

Sigma-Aldrich

C4879

α-Chymotrypsinogen A from bovine pancreas

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

Sigma-Aldrich

C3142

α-Chymotrypsin from bovine pancreas

α-Chymotrypsin from bovine pancreas Type I-S, essentially salt-free, lyophilized powder

Sigma-Aldrich

C7762

α-Chymotrypsin from bovine pancreas

α-Chymotrypsin from bovine pancreas Type II, lyophilized powder, ≥40 units/mg protein

Sigma-Aldrich

C4129

α-Chymotrypsin from bovine pancreas

biological source

bovine pancreas

biological source

-

biological source

-

biological source

-

specific activity

≥40 units/mg solid

specific activity

≥40 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥40 units/mg protein

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

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

solubility

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

solubility

1 mM HCl: soluble 10 mg/mL, clear

solubility

1 mM HCl: soluble 2.0 mg/mL, clear

solubility

-

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000421773
0000421773
0000362307
0000362310
0000334512

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Articles

Chymotrypsin

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

Related Content

Product Information Sheet - C4879

Product Information Sheet

Simulation of the activation of alpha-chymotrypsin: Analysis of the pathway and role of the propeptide
Matrai J, et al.
Protein Science, 13(12), 3139-3150 (2004)
Rob Haselberg et al.
Analytica chimica acta, 678(1), 128-134 (2010-09-28)
A capillary electrophoresis-mass spectrometry (CE-MS) method using sheath liquid electrospray ionization interfacing was studied and optimized for the analysis of intact basic proteins. To prevent protein adsorption, capillaries with a noncovalent positively charged coating were utilized. Capillaries were coated by
Angelina Angelova et al.
International journal of pharmaceutics, 454(2), 625-632 (2013-06-25)
Defining appropriate delivery strategies of therapeutic proteins, based on lipid nanoparticulate carriers, requires knowledge of the nanoscale organization that determines the loading and release properties of the nanostructured particles. Nanoencapsulation of three cationic proteins (human brain-derived neurotrophic factor (BDNF), α-chymotrypsinogen
View All Related Papers

Global Trade Item Number

SKUGTIN
C4879-100MG04061833493229
C4879-5G04061833493359
C4879-1G04061833493298
C4879-250MG04061832700076

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