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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Product Name
Anti-CPA1 antibody produced in rabbit, affinity isolated antibody
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
47 kDa
species reactivity
horse, human
concentration
0.5 mg - 1 mg/mL
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Quality Level
Gene Information
human ... CPA1(1357)
Related Categories
Application
Anti-CPA1 antibody produced in rabbit is suitable for western blot analysis.
Biochem/physiol Actions
CPA1 (Carboxypeptidase A1) is a zinc metalloenzyme belonging to the tetragonal space group P4(3)2(1)2. It forms a multiprotein complex, Zn2+-poly(acrylic acid), by directly interacting with proteases in the gastrointestinal tract. It stimulates the hydrolytic separation of carboxyl-terminal aromatic or branched aliphatic side chain of amide bonds from peptides and proteins.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Immunogen
Synthetic peptide directed towards the N terminal region of human CPA1
Other Notes
Synthetic peptide located within the following region: QVLRISVADEAQVQKVKELEDLEHLQLDFWRGPAHPGSPIDVRVPFPSIQ
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
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Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Irantzu Pallarès et al.
Acta crystallographica. Section D, Biological crystallography, D64(Pt 7), 784-791 (2008-06-21)
Carboxypeptidase A1 has been the subject of extensive research in the last 30 y and is one of the most widely studied zinc metalloenzymes. However, the three-dimensional structure of the human form of the enzyme is not yet available. This
E Clauser et al.
The Journal of biological chemistry, 263(33), 17837-17845 (1988-11-25)
Nucleotide sequencing of a rat carboxypeptidase B (CPB) cDNA and direct sequencing of the CPB mRNA via primer extension on pancreatic polyadenylated RNA has yielded the complete amino acid sequence of rat CPB. The rat enzyme is synthesized as a
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