|Application ||WB, IHC-P|
|Dilution||IHC-P (10 µg/ml), WB (1:1000-1:10000),|
|Other Names||RuvB-like 2, 126.96.36.199, 48 kDa TATA box-binding protein-interacting protein, 48 kDa TBP-interacting protein, 51 kDa erythrocyte cytosolic protein, ECP-51, INO80 complex subunit J, Repressing pontin 52, Reptin 52, TIP49b, TIP60-associated protein 54-beta, TAP54-beta, RUVBL2, INO80J, TIP48, TIP49B|
|Target/Specificity||Human RUVBL2. Predicted cross-reactivity based on amino acid sequence homology: mouse (99%), rat (99%), bovine (98%), zebrafish (82%).|
|Reconstitution & Storage||Aliquot and store at -20°C. Minimize freezing and thawing.|
|Precautions||TIP48 / RUVBL2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||INO80J, TIP48, TIP49B|
|Function||Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes.|
|Cellular Location||Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm. Membrane. Note=Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol. Although it is also present in the cytoplasm and associated with the cell membranes|
|Tissue Location||Ubiquitously expressed. Highly expressed in testis and thymus|
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Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.
Salzer U.,et al.Biochim. Biophys. Acta 1446:365-370(1999).
Kanemaki M.,et al.J. Biol. Chem. 274:22437-22444(1999).
Parfait B.,et al.Ann. Genet. 43:69-74(2000).
Bauer A.,et al.EMBO J. 19:6121-6130(2000).
Wood M.A.,et al.Mol. Cell 5:321-330(2000).
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