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APEH Rabbit anti-Human, Polyclonal, Invitrogen™

Rabbit Polyclonal Antibody

Manufacturer:  Invitrogen PA528251

Catalog No. PIPA528251


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Description

Description

PA5-28251 targets APEH in WB applications and shows reactivity with Human samples. The PA5-28251 immunogen is recombit protein fragment corresponding to a region within amino acids 290 and 658 of Human APEH. Store product as a concentrated solution. Centrifuge briefly prior to opening the vial. For short-term storage (1-2 weeks), product can be stored at 4°C. For long-term storage, aliquot and store product at -20° C or below, avioiding multiple freeze-thaw cycles.

This gene encodes the enzyme acylpeptide hydrolase, which catalyzes the hydrolysis of the terminal acetylated amino acid preferentially from small acetylated peptides. The acetyl amino acid formed by this hydrolase is further processed to acetate and a free amino acid by an aminoacylase. This gene is located within the same region of chromosome 3 (3p21) as the aminoacylase gene, and deletions at this locus are also associated with a decrease in aminoacylase activity. The acylpeptide hydrolase is a homotetrameric protein of 300 kDa with each subunit consisting of 732 amino acid residues. It can play an important role in destroying oxidatively damaged proteins in living cells. Deletions of this gene locus are found in various types of carcinomas, including small cell lung carcinoma and renal cell carcinoma.
Specifications

Specifications

APEH
Polyclonal
Unconjugated
APEH
Liquid
APEH
Recombit protein fragment corresponding to a region within amino acids 290 and 658 of Human APEH
Antigen affinity chromatography
RUO
Antibody
Polyclonal
Human
Western Blot
0.34 mg/mL
0.1M tris glycine with 10% glycerol and 0.01% thimerosal; pH 7
P13798
AARE, ACPH, APH, D3F15S2, D3S48E, DNF15S2, OPH, acyl-peptide hydrolase, acylamino-acid-releasing enzyme, acylaminoacyl-peptidase, oxidized protein hydrolase
Rabbit
IgG
100 μL
Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.
Primary
327
Documents
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