CPA3 Polyklonale Antilichaam, Cy5.5 Vermengd

Carboxypeptidase A (CPA) is a pancreatic exopeptidase which hydrolyses the peptide bond adjacent to the C-terminal end in polypeptide chains. Mast cell carboxypeptidase A (MC-CPA), a part of the peptidase M14 family, is a highly conserved metalloprotease localized to the secretory granules, along with trytases and chymases. MC-CPA is stored as an active enzyme in the granule and is released, along with other inflammatory mediators, upon mast cell degranulation. MC-CPA mirrors pancreatic carboxypeptidase A in cleaving COOH-terminal aromatic and aliphatic amino acid residues. The optimum pH of MC-CPA is between neutral and basic, depending upon the substrate. The MC-CPA gene, CPA3, resides on chromosome 3 and contains 11 exons.

Carboxypeptidase A; Carboxypeptidase A3; carboxypeptidase A3 mast cell; CBPA3_HUMAN; Cpa3; Mast cell carboxypeptidase A; mast cell carboxypeptidase A3; MC CPA; MC-CPA.

1359

Cytoplasm

Rat

101-200/417

CPA3

Cy5.5

KLH conjugated synthetic peptide derived from human CPA3/MC-CPA

WB, IF (IHC-P), IF (IHC-F), IF (ICC)

Purified by Protein A.

675nm/694nm

1µg/µl

WB (1:300-5000), IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)

Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Unmodified

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

1359

Human, Mouse