|Reactivity||Human, Mouse, Rat|
|Calculated MW||34003 Da|
|Positive Control||Western blot: Jurkat cell lysate|
|Application & Usage||Western blot: 1:200|
|Other Names||G0/G1 switch regulatory protein 24, Growth factor-inducible, nuclear protein NUP475, Protein TIS11A, Zinc finger protein 36 homolog|
|Formulation||100 µg (0.5 mg/ml) of antibody in PBS, 0.01 % BSA, 0.01 % thimerosal, and 50 % glycerol, pH 7.2|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||TTP Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||G0S24, RNF162A, TIS11A, TTP|
|Function||mRNA-binding protein involved in post-transcriptional regulation of AU-rich element (ARE)-containing mRNAs. Acts by specifically binding ARE-containing mRNAs and promoting their degradation. Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1. Plays a key role in the post- transcriptional regulation of tumor necrosis factor (TNF). Plays a key role in the post-transcriptional regulation of tumor necrosis factor (TNF).|
|Cellular Location||Nucleus. Cytoplasm. Note=Localizes to stress granules upon energy starvation. phosphorylation by MAPKAPK2 promotes exclusion from stress granules|
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Tristetraprolin (TTP), also known as Nup475 and TIS11, is a zinc-binding protein encoded by the immediate-early response gene, Zfp-36. Stimulation of quiescent fibroblasts by mitogens, including platelet derived growth factor and fibroblast growth factor, results in the serine phosphorylation of TTP and the rapid redistribution of the protein from the nucleus to the cytoplasm. in vitro studies have demonstrated that TTP is phosphorylated by p42 MAP kinase, indicating that the activity of TTP may be regulated by the MAP kinase pathway in vivo. Knockout mice deficient in TTP develop autoimmunity, inflammatory arthritis and dermatitis. These conditions can be reversed by blocking the activity of the inflammatory mediator, tumor necrosis factor-alpha (TNF-α), suggesting that TTP may function to negatively regulate the expression of TNF-α.
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