Advanced Search



Carboxypeptidase A from bovine pancreas

SIGMA/SAE0046 - (Type II-PMSF treated), ≥20 units/mg protein

Synonym: Carboxypeptidase A; Carboxypolypeptidase; Peptidyl-L-amino-acid hydrolase

CAS Number: 11075-17-5
MDL Number: MFCD00130718
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-SAE0046-500UN 500 units
$51.70
1/EA
Add To Favorites
45-SAE0046-2.5KU 2500 units
$154.00
1/EA
Add To Favorites
45-SAE0046-5KU 5000 units
$259.00
1/EA
Add To Favorites
This image is provided for informative purposes only and does not represent an actual product label. It should not be used as a substitute for official product labeling.

 

biological source bovine pancreas
form aqueous suspension
impurities ≤0.05 BTEE units/mg protein chymotrpsin
  ≤10 BAEE units/mg protein trypsin
mol wt ~35 kDa
purified by 2× crystallization
quality (Type II-PMSF treated)
Quality Level 200 
specific activity ≥20 units/mg protein
storage temp. 2-8°C
Analysis Note: Protein determined by E1%/278
Application: Carboxypeptidase A from bovine pancreas has been used in in vitro simulated digestion.
Application: Carboxypeptidase A from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Carboxypeptidase A from bovine pancreas has also been used in a study to investigate the isolation and partial characterization of precursor forms of ostrich carboxypeptidase.
Biochem/physiol Actions: Carboxypeptidase as isolated from bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by β-phenylpropionate and indole acetate.†
General description: Carboxypeptidase A (CPA) is a secreted protease is liberated after the activation of mast cells to facilitate acute anaphylaxis. Carboxypeptidase A has a long half-life in vivo, when compared to other secreted proteases.
Other Notes: One unit will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C.
Packaging: 500, 2500, 5000 units in glass bottle
Preparation Note: Treated with phenylmethylsulfonyl fluoride to eliminate trypsin and chymotrypsin activity. Dialyzed and recrystallized: aqueous suspension with toluene added.
Symbol GHS08  GHS08
Signal word Danger
Hazard statements H334
RIDADR NONH for all modes of transport
WGK Germany WGK 1
Flash Point(F) Not applicable
Flash Point(C) Not applicable
activity specific activity: ≥20 units/mg protein
Storage Temp. 2-8°C
Enzyme Commission (EC) Number 3.4.17.1   ( BRENDA  | IUBMB  )
UNSPSC 12352204

The following items have been added to your cart:

Choose a favorite list for this item:

Catalog Number Description Price
$

Returns/Order support

Please fill out the form below if you want to request order support from Krackeler Scientific.


Quick Order

* Required


New Year Price Updates

We are currently working diligently to update our website pricing information for the New Year. If you place an order, you will be acknowledged with any corrected pricing. If you'd like the most current information sooner, please don't hesitate to drop us an email or give us a call and we'd be happy to assist. Thank you for your patience while we are updating.

800-334-7725
office@krackeler.com


Play Video

To Request a Quote

  1. Search or Browse for items and add to them to your Shopping Cart.
  2. Click the "Request Quote" button at the bottom of the Shopping Cart page.
  3. Fill out required fields.
  4. Optionally you can convert to standard checkout mode by choosing a payment type.
  5. Click "Request Quote" at the bottom of the page.

You will be contacted with a quote.

To Order From a Quote

  1. Register and login to the website.
  2. Receive a quote from your sales representative or customer service.
  3. Have your copy of the quote in hand.
  4. Visit our quote module to search for your quote.
Back to Top