PathScan® RP BRD9 Sandwich ELISA Kit #27106
Important Ordering Details
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Supporting Data
| REACTIVITY | H |
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Description
The rapid protocol (RP) PathScan® RP BRD9 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of BRD9 protein in a reduced assay time of 1.5 hours. Incubation of cell lysates and detection antibody on the coated microwell plate forms a sandwich with BRD9 in a single step. The plate is then extensively washed and TMB reagent is added for signal development. The magnitude of absorbance for the developed color is proportional to the quantity of BRD9. Learn more about your ELISA kit options here.
*Antibodies in this kit are custom formulations specific to kit.
Protocol
Specificity / Sensitivity
The PathScan® RP BRD9 Sandwich ELISA Kit detects endogenous levels of BRD9 protein. The kit sensitivity is shown in Figure 1. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
Species Reactivity:
Human
Background
ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1, to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9).
GLTSCR1 and its paralog GLTSCR1L along with BRD9 have been identified as unique subunits of the non-canonical BAF (ncBAF) or GBAF complex. This complex contains either GLTSCR1 or GLTSCR1L instead of an ARID subunit, while also lacking the BAF45, BAF47, and BAF57 subunits. GBAF maps to regions distinct from the PBAF and canonical BAF complexes and has also been shown to be a synthetic lethal target for BAF driven cancers such as synovial sarcomas and rhabdoid tumors (10-12).
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- Alpsoy, A. and Dykhuizen, E.C. (2018) J Biol Chem 293, 3892-3903.
- Mashtalir, N. et al. (2018) Cell 175, 1272-1288.e20.
- Michel, B.C. et al. (2018) Nat Cell Biol 20, 1410-1420.
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