|Application ||WB, E|
|Other Accession||AAH50719, 29792103|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||82016 Da|
|Application Notes||ZBTB2 antibody can be used for detection of ZBTB2 by Western blot at 1 µg/mL.|
|Target/Specificity||ZBTB1; This ZBTB2 antibody will not cross-react with ZBTB1.|
|Reconstitution & Storage||ZBTB2 antibody can be stored at 4℃ for three months and -20℃, 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.|
|Precautions||ZBTB2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Acts as a transcriptional repressor (PubMed:20797634). Represses cAMP-responsive element (CRE)-mediated transcriptional activation (PubMed:21706167). In addition, has a role in translesion DNA synthesis. Requires for UV-inducible RAD18 loading, PCNA monoubiquitination, POLH recruitment to replication factories and efficient translesion DNA synthesis (PubMed:24657165). Plays a key role in the transcriptional regulation of T lymphocyte development (By similarity).|
|Cellular Location||Nucleus. Nucleus, nucleoplasm. Note=Localized in dot-like structures in the nucleus (PubMed:21706167) Colocalized with SMRT in nuclear bodies (PubMed:20797634). The sumoylated form is preferentially located in the nucleoplasm outside the nuclear bodies(PubMed:20797634)|
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Provided below are standard protocols that you may find useful for product applications.
ZBTB2 Antibody: ZBTB2 is a zinc finger protein that also contains BTB (BR-C, ttk and bab) domain. While little is known about this protein or the related protein ZBTB1, ZBTB2 is thought to be phosphorylated in response to the DNA damage, probably by either ATM or ATR. At least two isoforms of ZBTB2 are known to exist.
Strausberg RL, Feingold EA, Grouse LH, et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. USA2002; 99:16899-903.
Matsuoka S, Ballif BA, Smogorzewska A, et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science2007; 1160-1166.
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