The Calcium concentration in most classical medium formulations, including RPMI, is sufficient to activate and/or stabilize α-Chymotrypsin.
α-Chymotrypsin calcium requirements:
Significant occupancy of Ca2+ site - approximately 0.1 mM
Saturating level - approximately 1 mM
Concentration for stock solution storage - 5–10 mM
Please see the link below to review additional information available in the TLCK-treated version of this product, C3142:
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/349/963/c3142pis.pdf
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C4129
α-Chymotrypsin from bovine pancreas
Type II, lyophilized powder, ≥40 units/mg protein
Synonim(y):
α-chymotrypsin A and B, alpha-chymotrypsin
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Informacje o tej pozycji
Numer CAS:
UNSPSC Code:
12352204
eCl@ss:
42010112
EC Number:
232-671-2
NACRES:
NA.54
MDL number:
Numer WE:
Specific activity:
≥40 units/mg protein
Assay:
≥85% (UV)
Informacje o cenach i dostępności nie są obecnie dostępne.
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Type II
Quality Segment
assay
≥85% (UV)
form
lyophilized powder
specific activity
≥40 units/mg protein
mol wt
25 kDa
composition
protein, ≥85%
color
white to off-white
UniProt accession no.
application(s)
diagnostic assay manufacturing
storage temp.
−20°C
Gene Information
cow ... CTRB1(618826)
General description
Substrate Specificity
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa
Application
Biochem/physiol Actions
α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. The pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10 mM Cu2+ and Hg2+.
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.
Preparation Note
Produced from 3× crystallized chymotrypsinogen
Analysis Note
Protein determined by E1%/280
Other Notes
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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Ta pozycja | |||
|---|---|---|---|
| description Type II, lyophilized powder, ≥40 units/mg protein | 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 protein | specific activity ≥40 units/mg protein | specific activity ≥40 units/mg protein | specific activity - |
| assay ≥85% (UV) | assay - | assay ≥90% (UV) | assay - |
| Gene Information cow ... CTRB1(618826) | Gene Information cow ... CTRB1(618826) | Gene Information cow ... CTRB1(618826) | Gene Information cow ... CTRB1(618826) |
| application(s) diagnostic assay manufacturing | application(s) - | application(s) - | application(s) - |
| form lyophilized powder | form essentially salt-free, lyophilized powder | form essentially salt-free, lyophilized powder | form salt-free, lyophilized powder |
| UniProt accession no. | UniProt accession no. | UniProt accession no. - | UniProt accession no. - |
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Słowo ostrzegawcze
Danger
Kody zagrożeń
Hazard Classifications
Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Narządy docelowe
Respiratory system
Klasa składowania
11 - Combustible Solids
PPE (środki ochrony indywidualnej)
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Wykazy regulacyjne
Wykazy regulacyjne dotyczą głównie produktów chemicznych. Można w nich podawać ograniczoną liczbę informacji na temat produktów niechemicznych. Brak wpisu oznacza, że żaden ze składników nie znajduje się w wykazie. Użytkownik odpowiada za zagwarantowanie bezpiecznego i zgodnego z prawem stosowania produktu.
9004-07-3
CAS No.
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I intend to use it in RPMI cell conditioned media which I read contains at least ~0.5 mM Ca. Is this sufficient?
1 answer-
Helpful?
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What is the pH optimum for the enzyme, Product No. C4129?
1 answer-
The pH optimum for alpha-chymotrypsin is between pH 7.5-8.5. Please see the following reference: Wilcox, P.E., Chymotrypsingogens-chymotrypsins, Methods in Enzymology, 19, 64-80 (1970).
Helpful?
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What is the molecular weight of alpha-chymotrypsin from bovine pancreas, product C4129?
1 answer-
The molecular weight of alpha chymotrypsin, reported in the literature, is approximately 25 kDa.
Helpful?
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How can solutions of alpha chymotrypsin (Product No. C4129) be stored?
1 answer-
Stock solutions prepared in 1 mM HCl, containing 2 mM calcium chloride, can be stored at -20 ° for about one week.
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What is the Department of Transportation shipping information for this product?
1 answer-
Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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How do you recommend preparing a solution of Product No. C4129?
1 answer-
It is recommended to reconstitute Product No. C4129 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as a stabilizer, and possibly an activator, of the enzyme.
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