Passa al contenuto
Merck
Tutte le immagini(4)

Key Documents

View All Documentation

C4879

Sigma-Aldrich

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

Sinonimo/i:

chymotrypsin A zymogen

Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
Tutte le immagini(4)

About This Item

Numero CAS:
9035-75-0
Numero CE:
232-905-3
Numero MDL:
MFCD00130483
Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

bovine pancreas

Livello qualitativo

200

Tipo

Type II

Forma fisica

essentially salt-free, lyophilized powder

Attività specifica

≥40 units/mg solid

PM

25,656 Da by calculation

Purificato mediante

6× crystallization

Solubilità

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

N° accesso UniProt

P00767

Attività estranea

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

Temperatura di conservazione

−20°C

Informazioni sul gene

cow ... CTRB1(618826)

Categorie correlate

Descrizione generale

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

Applicazioni

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.
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.

Azioni biochim/fisiol

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.
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.

Definizione di unità

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

Altre note

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

Applicazioni

N° Catalogo
Descrizione
Determinazione del prezzo

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

Possiedi già questo prodotto?

I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.

Visita l’Archivio dei documenti

I clienti hanno visto anche

Slide 1 of 10

1 of 10

Ribonucleasi A Type XII-A, ≥90% (SDS-PAGE), 75-125 Kunitz units/mg protein

Sigma-Aldrich

R5500

Ribonucleasi A

Citocromo c ≥95% based on Mol. Wt. 12,327 basis, powder, suitable for mammalian cell culture

Sigma-Aldrich

C3131

Citocromo c

Citocromo c ≥95% based on Mol. Wt. 12,327 basis

Sigma-Aldrich

C2037

Citocromo c

Myoglobin from equine skeletal muscle 95-100%, essentially salt-free, lyophilized powder

Sigma-Aldrich

M0630

Myoglobin from equine skeletal muscle

Lisozima powder or granules, ≥90 %, ≥39,000 units/mg protein

Sigma-Aldrich

L6876

Lisozima

Myoglobin from equine heart ≥90% (SDS-PAGE), essentially salt-free, lyophilized powder

Sigma-Aldrich

M1882

Myoglobin from equine heart

Ubiquitin from bovine erythrocytes BioUltra, ≥98% (SDS-PAGE), essentially salt-free, lyophilized powder

Sigma-Aldrich

U6253

Ubiquitin from bovine erythrocytes

vibrant-m

C2160000

Chymotrypsin

Met-Arg-Phe-Ala acetate salt ≥90% (HPLC)

Sigma-Aldrich

M1170

Met-Arg-Phe-Ala acetate salt

Albumina lyophilized powder, ≥98% (agarose gel electrophoresis)

Sigma-Aldrich

A5503

Albumina

Curtiss P Schneider et al.
The journal of physical chemistry. B, 115(22), 7447-7458 (2011-05-17)
L-Arginine hydrochloride is a very important aggregation suppressor for which there has been much attention given regarding elucidating its mechanism of action. Little consideration, however, has been given toward other salt forms besides chloride, even though the counterion likely imparts
Curtiss P Schneider et al.
The journal of physical chemistry. B, 113(7), 2050-2058 (2009-02-10)
The relatively new technique of vapor pressure osmometry was utilized to determine the preferential interaction of five common solution additives (arginine HCl, guanidine HCl, glycerol, glucose, and urea) using three different model proteins (BSA, lysozyme, and alpha-chymotrypsinogen). Results for guanidine
Effect of real-world sounds on protein crystallization
Zhang CY, et al.
International Journal of Biological Macromolecules, 112, 841-851 (2018)
Pedro P Madeira et al.
Journal of chromatography. A, 1190(1-2), 39-43 (2008-04-02)
Distribution coefficients of randomly selected proteins were measured in aqueous two-phase systems (ATPSs) formed by different combinations of Dextran-75 (Dex), Ficoll-70, polyethylene glycol-8000 (PEG), hydroxypropyl starch-100 (PES), and Ucon50HB5100 (Ucon, a random copolymer of ethylene glycol and propylene glycol) at
Shujun Bai et al.
Journal of pharmaceutical sciences, 94(9), 2030-2038 (2005-07-30)
Fourier transform infrared (FTIR) spectroscopy is a powerful tool for monitoring structural changes in lyophilized protein formulations. However, direct measurement of IR spectra requires significant handling time and effort. The possibility of using near infrared (NIR) spectroscopy as a rapid
Visualizza tutti i documenti correlati

Articoli

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX-NP5: Affect of pH

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX: Affect of Particle Size

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

Chymotrypsin

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

Chromatograms

application for HPLC

Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..

Contatta l'Assistenza Tecnica.