Product Pathways - Chromatin Regulation / Epigenetics
CENP-A (C51A7) Rabbit mAb (Mouse Specific; IF Preferred) #2048
|W IF-IC||M||Endogenous||17||Rabbit IgG|
Reactivity Key: M=Mouse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
CENP-A (C51A7) Rabbit mAb detects endogenous levels of total mouse CENP-A protein. This antibody does not cross-react with other histone proteins, including Histone H3.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the amino terminus of mouse CENP-A protein.
Western blot analysis of extracts from NIH/3T3 and C2C12 cells using CENP-A (C51A7) Rabbit mAb.
Modulation of chromatin structure plays a critical role in the regulation of transcription and replication of the eukaryotic genome. The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). CENP-A, also known as the chromatin-associated protein CSE4 (capping-enzyme suppressor 4-p), is an essential histone H3 variant that replaces canonical histone H3 in centromeric heterochromatin (2). The greatest divergence between CENP-A and canonical histone H3 occurs in the amino-terminal tail of the protein, which binds linker DNA between nucleosomes and facilitates proper folding of centromeric heterochromatin (3). The amino-terminal tail of CENP-A is also required for recruitment of other centromeric proteins (CENP-C, hSMC1, hZW10), proper kinetochore assembly and chromosome segregation during mitosis (4). Additional sequence divergence in the histone fold domain is responsible for correct targeting of CENP-A to the centromere (5). Many of the functions of CENP-A are regulated by phosphorylation (6,7). Aurora A-dependent phosphorylation of CENP-A on Ser7 during prophase is required for proper targeting of Aurora B to the inner centromere in prometaphase, proper kinetochore/microtubule attachment and proper alignment of chromosomes during mitosis (6).
- Jin, J. et al. (2005) Trends Biochem Sci 30, 680-7.
- Ausió, J. (2006) Brief Funct Genomic Proteomic 5, 228-43.
- Heit, R. et al. (2006) Biochem Cell Biol 84, 605-18.
- Van Hooser, A.A. et al. (2001) J Cell Sci 114, 3529-42.
- Black, B.E. et al. (2004) Nature 430, 578-82.
- Kunitoku, N. et al. (2003) Dev Cell 5, 853-64.
- Zeitlin, S.G. et al. (2001) J Cell Biol 155, 1147-57.
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For Research Use Only. Not For Use In Diagnostic Procedures.