|Reactivity||Human, Mouse, Rat|
|Calculated MW||52164 Da|
|Positive Control||Western blot: Jurkat, 3T3, rat kidney cell lysate|
|Application & Usage||Western blot: 1:200|
|Other Names||ATP-dependent DNA helicase VIII|
|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||G3BP Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium- dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.|
|Cellular Location||Cytoplasm. Cytoplasm, cytosol. Cytoplasmic granule. Cell membrane. Nucleus. Note=Cytoplasmic in proliferating cells, can be recruited to the plasma membrane in exponentially growing cells (By similarity). Cytosolic and partially nuclear in resting cells. Recruited to stress granules (SGs) upon either arsenite or high temperature treatment. Recruitment to SGs is influenced by HRAS.|
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G3BP1 (GTPase activating protein (SH3 domain) binding protein 1), also known as G3BP or HDH-VIII, is a ubiquitously expressed protein that localizes to the cytoplasm in proliferating cells and to the nucleus in non-proliferating cells. One of several DNA-unwinding enzymes, G3BP1 functions as a sequence-specific, phosphorylation-dependent helicase that unwinds partial RNA and DNA duplexes containing hanging 3’- or 5’- ends. G3BP1 uses magnesium as a cofactor and, in addition to its helicase activity, acts as an endoribonuclease that cleaves mRNA between adenine and cytosine residues at the 3’-UTR. An element of the Ras signaling pathway, G3BP1 binds to the SH3 domain of Ras GTPase-activating protein (Ras GAP) in proliferating cells, thereby regulating Ras signaling events in developing tissues. Due to its involvement in both DNA replication and signaling pathways within the cell, G3BP1 expression is implicated in the pathogenesis of several cancers, including esophageal squamous carcinoma.
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