NTAN1 Antibodies, cDNA Clones Research Reagents

NTAN1 (N-Terminal Asparagine Amidase, also known as PNAA; PNAD), located on 16p13.11, is a Protein Coding gene. The protein encoded by this gene functions in a step-wise process of protein degradation through the N-end rule pathway. The gene produces a 34677 Da protein composed of 310 amino acids. The enzymatic deamidation of N-terminal L-Asn by NTAN1 is a feature of the ubiquitin-dependent N-end rule pathway of protein degradation, which relates the in vivo half-life of a protein to the identity of its N-terminal residue. Diseases such as Diabetes Mellitus and Insulin-Dependent, 21 are associated with NTAN1.

NTAN1 Antibody (2)

    NTAN1 cDNA Clone (15)

    BC017336

    クローニングベクター cDNA 製品

    In lentiviral vector

    NTAN1 qPCR Primer (1)

    NTAN1 の背景知識

    N-terminal asparagine amidohydrolase (NTAN1) is an essential component of a protein degradation signal, which is a destabilizing N-terminal residue of a protein, in the N-end rule. The enzymatic deamidation of N-terminal L-Asn by NTAN1 is a feature of the ubiquitin-dependent N-end rule pathway of protein degradation, which relates the in vivo half-life of a protein to the identity of its N-terminal residue. NTAN1 deamidates N-terminal asparagine to aspartate, which is conjugated to arginine by ATE1. An N-terminal arginine-bearing substrate protein is recognized, ubiquitylated by UBR1/E3alpha, and subsequently degraded by 26S proteasomes. The approximately 17-kilobase pair Ntan1 gene is located in the proximal region of mouse chromosome 16 and contains 10 exons ranging from 54 to 177 base pairs in length. Inactivation of the NTAN1 gene encoding the asparagine-specific N-terminal amidase in mice results in impaired spatial memory.

    NTAN1 の参考文献

    • Hirai T, et al. (2006) Stimulation of ubiquitin-proteasome pathway through the expression of amidohydrolase for n-terminal asparagine (ntan1) in cultured rat hippocampal neurons exposed to static magnetism. J Neurochem 96 (6): 1519-1530.
    • Grigoryev S, et al. (1996) A mouse amidase specific for n-terminal asparagine. The gene, the enzyme, and their function in the n-end rule pathway. J Biol Chem 271 (45): 28521-28532.
    • Cantor JR, et al. (2011) Expression and biochemical characterization of the human enzyme n-terminal asparagine amidohydrolase. Biochemistry 50 (14): 3025-3033.
    • Balogh SA, et al. (2000) Varying intertrial interval reveals temporally defined memory deficits and enhancements in ntan1-deficient mice. Learn Mem 7 (5): 279-286.

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