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Human Carboxypeptidase A4 Recombinant


accession:  Q9UI42
   Size A     10ug   $ 160
   Size B      50ug  $680
   Size C      200ug  $ 1950
Domain  : 
Gene  :  CPA4
Catalog no. :  RKQ9UI42



Optimized DNA sequence encoding Human Carboxypeptidase A4(GLY17 - TYR421) preprotein including a C-terminal His tag was expressed in HEK293 cells.

Molecular weight:

Recombinant Human Carboxypeptidase A4 (CPA3) is a protein consisting of 410 amino acid residue subunits,due to glycosylation migrates as an approximately as 50kDa band protein on reduced SDS-PAGE.

>95%, as determined by SDS-PAGE and HPLC

Biological Activity:
The activity was tested by the ability to cleave a fluorogenic substrate Ac-Phe-Thiaphe-OH in the presence of 5,5’Dithio-bis. The specific activity was measured to be 3 nmole/ug/min
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

Recombinant Carboxypeptidase A4 (A3) is lyophilized  from 0.2 μm filtered PBS solution,  pH7.2 ,  5% Trehalose.

A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.

Recombinant Carboxypeptidase A4 (CPA4) can be stored in working aliquots at 2° - 8° C for one month, or at -20°C to -70°C for twelve months.

Avoid repeated freeze/thaw cycles.

This product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.


Carboxypeptidase A4

Carboxypeptidases (CPs)3 hydrolyze a single amino acid from the C terminus of peptides and proteins. Metallo-CPs use a catalytic mechanism in which nucleophilic attack on a peptide bond is mediated by a Zn2+-activated water molecule. CPA4 (carboxypeptidase A4) belongs to the M14A subfamily of carboxypeptidases.CPA4 was originally referred to as CPA3 (9) but was renamed CPA4 to reflect the order in which the CPAs were discovered.he human CPA4 gene is located on chromosome 7q32, which is a region in the genome that might contain genes for prostate cancer aggressiveness.

Related Publications:
crystal structure of novel metallocarboxypeptidase inhibitor from marine mollusk nerita versicolor in complex with human Carboxypeptidase A4
J. Biol. Chem., Mar 2012; 287: 9250 - 9258.
characterization of the substrate specificity of human Carboxypeptidase A4 and implications for a role in extracellular peptide processing
J. Biol. Chem., Jun 2010; 285: 18385 - 18396.

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