BAZ1B / WSTF Antibody (clone 5E9)
Mouse Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, E |
---|---|
Primary Accession | Q9UIG0 |
Reactivity | Human |
Host | Mouse |
Clonality | Monoclonal |
Clone Names | 5E9 |
Calculated MW | 171kDa |
Dilution | IHC-P (3-5 µg/ml) |
Gene ID | 9031 |
---|---|
Other Names | Tyrosine-protein kinase BAZ1B, 2.7.10.2, Bromodomain adjacent to zinc finger domain protein 1B, Williams syndrome transcription factor, Williams-Beuren syndrome chromosomal region 10 protein, Williams-Beuren syndrome chromosomal region 9 protein, hWALp2, BAZ1B, WBSC10, WBSCR10, WBSCR9, WSTF |
Target/Specificity | Human BAZ1B |
Reconstitution & Storage | Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. |
Precautions | BAZ1B / WSTF Antibody (clone 5E9) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | BAZ1B |
---|---|
Synonyms | WBSC10, WBSCR10, WBSCR9, WSTF |
Function | Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator (PubMed:19092802). Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph) (PubMed:19092802, PubMed:19234442). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress (PubMed:19092802, PubMed:19234442). Regulatory subunit of the ATP-dependent WICH-1 and WICH-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:11980720, PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). The WICH-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the WICH-5 ISWI chromatin remodeling complex (PubMed:28801535). The WICH-5 ISWI chromatin-remodeling complex regulates the transcription of various genes, has a role in RNA polymerase I transcription (By similarity). Within the B-WICH complex has a role in RNA polymerase III transcription (PubMed:16603771). Mediates the recruitment of the WICH-5 ISWI chromatin remodeling complex to replication foci during DNA replication (PubMed:15543136). |
Cellular Location | Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063, ECO:0000255|PROSITE-ProRule:PRU00475, ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:25593309}. Note=Accumulates in pericentromeric heterochromatin during replication (PubMed:15543136). Co-localizes with PCNA at replication foci during S phase (PubMed:15543136). Co-localizes with SMARCA5/SNF2H at replication foci during late-S phase (PubMed:15543136). Also localizes to replication foci independently of SMARCA5/SNF2H and PCNA (PubMed:15543136). Localizes to sites of DNA damage (PubMed:25593309). |
Tissue Location | Ubiquitously expressed with high levels of expression in heart, brain, placenta, skeletal muscle and ovary |
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Background
Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR- mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association.
References
Peoples R.J.,et al.Cytogenet. Cell Genet. 82:238-246(1998).
Lu X.,et al.Genomics 54:241-249(1998).
Jones M.H.,et al.Genomics 63:40-45(2000).
Hillier L.W.,et al.Nature 424:157-164(2003).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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