This rabbit IgG polyclonal antibody was generated against the conserved sequence of the protein tyrosine phosphatase (PTP) active site with catalytic cysteine modified with dimedone (DMD) and is specific for dimedone-modified PTP cysteine sulfenic acid.
The oxidation of cysteine to the sulfenic acid is often transient and difficult to detect, thus making it problematic in understanding the role that this oxidative post-translational modification plays in redox-biology and pathogenesis. This antibody was designed to recognize the conserved sequence of the PTP active site (VHCDMDSAG) harboring the catalytic cysteine modified with dimedone (CDMD), a nucleophile that chemoselectively reacts with cysteine sulfenic acids to form a stable thioether adduct. Protein tyrosine phosphatases are crucial regulators of signal transduction and function as antagonists towards protein tyrosine kinases to control reversible tyrosine phosphorylation, thereby regulating fundamental physiological processes. Growing evidence has supported the notion that reversible oxidative inactivation of the catalytic cysteine residue in protein tyrosine phosphatases serves as an oxidative post-translational modification that regulates its activity to influence downstream signaling by promoting phosphorylation and induction of the signaling cascade.
From the laboratory of Kate Carroll, PhD, The Scripps Research Institute.
|Antigen:||VHCDMDSAG (CDMD= dimedone modified cysteine)|
|Immunogen:||Conserved sequence of the PTP active site with catalytic cysteine modified with dimedone (DMD)|
|Epitope:||VHCDMDSAG (CDMD= dimedone modified cysteine)|
|Purification Method:||Unpurified serum (EST023) or affinity purified at 2.3mg/mL (EST024)|
|Tested Applications:||WB (1:200-1:1000), IF|
|Storage:||Stable for 1 year at -80C from date of receipt. 1-month after dilution in in WB buffer (containing 3-5% BSA, 0.01% NaN3)|
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