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CUSABIO synthesized the recombinant gene by integrating the N-terminal 6xHis tag sequence into the targeted gene encoding the 1-732aa of the human APEH. The synthesized gene was subsequently cloned into an expression vector. After cloning, the expression vector was introduced into the E.coli for expression. The product was purified to obtain the recombinant human APEH protein carrying N-terminal 6xHis tag. The SDS-PAGE assayed the purity of this recombinant APEH protein greater than 85%. This APEH protein migrated along the gel to a band of about 90 kDa molecular weight.APEH is a gene providing instruction of making a protein called acylamino-acid-releasing enzyme in human and belongs to peptidase S9C family. This protein, also abbreviated APH or AARE, is a tetrameric serine protease which specifically removes acetyl amino acids from N-terminally acetylated peptides and play an important role in destroying oxidatively-damaged proteins in living cells. APH preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. Deletions of this gene locus are found in various types of carcinomas, including small-cell lung carcinoma and renal cell carcinoma.
CUSABIO synthesized the recombinant gene by integrating the N-terminal 6xHis tag sequence into the targeted gene encoding the 1-732aa of the human APEH. The synthesized gene was subsequently cloned into an expression vector. After cloning, the expression vector was introduced into the E.coli for expression. The product was purified to obtain the recombinant human APEH protein carrying N-terminal 6xHis tag. The SDS-PAGE assayed the purity of this recombinant APEH protein greater than 85%. This APEH protein migrated along the gel to a band of about 90 kDa molecular weight.APEH is a gene providing instruction of making a protein called acylamino-acid-releasing enzyme in human and belongs to peptidase S9C family. This protein, also abbreviated APH or AARE, is a tetrameric serine protease which specifically removes acetyl amino acids from N-terminally acetylated peptides and play an important role in destroying oxidatively-damaged proteins in living cells. APH preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. Deletions of this gene locus are found in various types of carcinomas, including small-cell lung carcinoma and renal cell carcinoma.
| Cat.No | ACP02351 | Target Name | APEH |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 1-732aa | Mol Weight | 85.2 kDa |
| Protein Length | Full length | Purity | Greater than 85% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P13798 |
|---|
Uniprot Id
P13798
Target Species
Human
Target Name
APEH
Target Full Name
Acylamino-acid-releasing enzyme
Target Function
This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser.
Target Subcellular Location
Cytoplasm.
Target Protein Families
Peptidase S9C family
Target Research Area
Others
Target Synonyms
AARE; ACPH; ACPH_HUMAN; Acyl peptide hydrolase; Acyl-peptide hydrolase; Acylamino acid releasing enzyme; Acylamino-acid-releasing enzyme; Acylaminoacyl peptidase; Acylaminoacyl-peptidase; APEH; APH; N acylaminoacyl peptide hydrolase; OPH; Oxidized protein hydrolase
Target Background
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.
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