Description
NTAN1 Antibody | 59-421 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human
Homology: N/A
Immunogen: This NTAN1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 203-230 amino acids from the C-terminal region of human NTAN1.
Research Area: Cell Cycle
Tested Application: WB
Application: For WB starting dilution is: 1:1000
Specificiy: N/A
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 35 kDa
Validation: N/A
Isoform: N/A
Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.
Clonality: Polyclonal
Clone: N/A
Isotype: Rabbit Ig
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: batch dependent
Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Alternate Name: 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
User Note: Optimal dilutions for each application to be determined by the researcher.
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) .