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11418467001

Roche

Chymotrypsin Sequencing Grade

from bovine pancreas

Synonym(s):

chymotrypsin, protease

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About This Item

Enzyme Commission number:
3.4.21.1 (BRENDA, IUBMB)
UNSPSC Code:
12352204

biological source

bovine pancreas

Quality Level

100

Assay

≥90%

form

lyophilized (salt-free)

specific activity

≥70 units/mg protein (at 25 °C, with ATEE as a substrate)

mol wt

Mr 25 kDa

packaging

pkg of 4 × 25 μg

manufacturer/tradename

Roche

technique(s)

protein sequencing: suitable

optimum pH

7.0-9.0

shipped in

wet ice

storage temp.

2-8°C

Related Categories

General description

Chymotrypsin Sequencing Grade is isolated as a specific protease in pure form from bovine pancreas.

Specificity

Serine endopeptidase that specifically hydrolyzes peptide bonds at the C-terminial of Tyr, Phe, and Trp. Leu, Met, Ala, Asp, and Glu are cleaved at a lower rate. Acts also upon amides and esters of susceptible amino acids. The specificity of Chymotrypsin Sequencing Grade is tested with melittin as a substrate.

Application

Use Chymotrypsin Sequencing Grade for the hydrolysis of proteins by chymotrypsin alone or in combination with other proteases. It is suitable for peptide mapping, fingerprinting, and sequence analysis.

Quality

Purity: Free of impurities that may interfere with the specific cleavage or separation of peptides in reversed-phase HPLC.

Preparation Note

Working concentration: The recommended amount of enzyme is 1/200 to 1/20 of the quantity of protein by weight.
Storage conditions (working solution): 2 to 8 °C
A solution in 1 mM HCl can be stored for up to one week at 2 to 8 °C.
Inhibitors: Aprotinin, DFP, PMSF, phenothiazine-N-carbonyl chloride, TPCK, ZPCK, α2-macroglobulin, α1-antitrypsin, soybean trypsin inhibitor, and chymostatin. No inhibition by APMSF.

Reconstitution

Dissolve lyophilized chymotrypsin sequencing grade in 1mM HCl. The proteins to be sequenced are dissolved in digestion buffer (100mM Tris-HCl, 10mM CaCl2, pH 7.8).

Other Notes

For life science research only. Not for use in diagnostic procedures.

Pictograms

Exclamation markHealth hazard
GHS07,GHS08

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Virus-encoded proteinases and proteolytic processing in the Nidovirales.
J Ziebuhr et al.
The Journal of general virology, 81(Pt 4), 853-879 (2000-03-22)
A method for selective 19 F-labeling absent of probe sequestration (SLAPS).
Dixon, et al.
Protein Science, 31, e4454-e4454 (2023)
Wei-Qiang Chen et al.
Amino acids, 44(5), 1381-1389 (2013-03-21)
The protocol consists of running a native gel with in-gel digestion by proteases, subsequent mass spectrometrical determination of protein sequence and modifications, followed by electro-elution and conformational analysis using melting point and circular dichroism. Finally, the eluted protein is tested
Coagulation factor IX analysis in bioreactor cell culture supernatant predicts quality of the purified product.
Zacchi, et al.
Communications biology, 4, 390-390 (2021)
The kidney releases a nonpolymerizing form of uromodulin in the urine and circulation that retains the external hydrophobic patch domain.
Micanovic, et al.
American Journal of Physiology: Renal Physiology, 322, F403-F418 (2023)
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