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Carboxypeptidase A2 Protein (His tag)

CPA2 Origin: Human Host: Human Cells Recombinant > 95 % as determined by reducing SDS-PAGE.
Catalog No. ABIN7318243
  • Target See all Carboxypeptidase A2 (CPA2) Proteins
    Carboxypeptidase A2 (CPA2) (Carboxypeptidase A2 (Pancreatic) (CPA2))
    Protein Type
    Recombinant
    Origin
    • 5
    • 4
    • 3
    Human
    Source
    • 4
    • 3
    • 3
    • 1
    • 1
    Human Cells
    Purification tag / Conjugate
    This Carboxypeptidase A2 protein is labelled with His tag.
    Purpose
    Recombinant Human Carboxypeptidase A2/CPA2 Protein (His Tag)
    Sequence
    Leu17-Tyr417
    Characteristics
    Recombinant Human Carboxypeptidase A2 is produced by our Mammalian expression system and the target gene encoding Leu17-Tyr417 is expressed with a 6His tag at the C-terminus.
    Purity
    > 95 % as determined by reducing SDS-PAGE.
    Endotoxin Level
    < 1.0 EU per μg as determined by the LAL method.
    Top Product
    Discover our top product CPA2 Protein
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Reconstitution
    Please refer to the printed manual for detailed information.
    Buffer
    Lyophilized from a 0.2 μm filtered solution of 20 mM TrisHCl, 150mm NaCl, pH 7.5.
    Storage
    4 °C,-20 °C,-80 °C
    Storage Comment
    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
  • Target
    Carboxypeptidase A2 (CPA2) (Carboxypeptidase A2 (Pancreatic) (CPA2))
    Alternative Name
    Carboxypeptidase A2/CPA2 (CPA2 Products)
    Synonyms
    CPA2 Protein, zgc:92530 Protein, carboxypeptidase A2 Protein, carboxypeptidase A2 (pancreatic) Protein, Carboxypeptidase A2 Protein, carboxypeptidase A2, pancreatic Protein, CPA2 Protein, cpa2 Protein, CpipJ_CPIJ001743 Protein, cbpa2 Protein, Cpa2 Protein
    Background

    Background: Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition.

    Synonym: Carboxypeptidase A2, CPA2

    Molecular Weight
    45.9 kDa
    UniProt
    P48052
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