NTAN1 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q96AB6 |
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Clone Names | 110808201 |
Gene ID | 123803 |
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Other Names | Protein N-terminal asparagine amidohydrolase, 351-, Protein NH2-terminal asparagine amidohydrolase, PNAA, Protein NH2-terminal asparagine deamidase, PNAD, Protein N-terminal Asn amidase, Protein N-terminal asparagine amidase, Protein NTN-amidase, NTAN1 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | NTAN1 |
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Function | N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn. |
Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:Q28955}. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Side-chain deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position (By similarity).
References
Okada, Y., et al. Hum. Mol. Genet. 19(11):2303-2312(2010)Kamdem, L.K., et al. Pharmacogenet. Genomics 18(6):507-514(2008)Lamesch, P., et al. Genomics 89(3):307-315(2007)Grigoryev, S., et al. J. Biol. Chem. 271(45):28521-28532(1996)
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