ELISA, Immunohistochemistry, Western Blot. Histone H2AvD pS137 Antibody has been tested for use in ELISA, Immunohistochemistry, and by western blot. Specific conditions for reactivity should be optimized by the end user. Expect a band approximately 14 kDa in size corresponding to phosphorylated H2AvD protein by western blotting in the appropriate Drosophila tissue or cell lysate or extract. Minimal reactivity is observed against the non-phosphorylated form of the immunizing peptide. This antibody is phospho specific for pS137 of H2AvD protein.
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Description
This antibody is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI) and is suitable for Cancer, Immunology and Nuclear Signaling research. Variant histones H2A are synthesized throughout the cell cycle and are very different from classical S-phase regulated H2A. H2AvD is vital for viability, but the exact function of variant histones H2A is not known. H2A is a core component of the nucleosome, an octamer containing two molecules each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 bp of DNA. HsAvD is expressed both maternally and zygotically and is found in embryos through to adults (female only). The human homologue, H2AX, is phosphorylated by ATM protein kinase when double strand DNA breaks occur. In mouse, H2AX ''knock out'' mice have an increased incidence of cancer.
Immunogen
Histone H2AvD pS137 Antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to amino acids 132-141 of Drosophila melanogaster (fruit fly) H2AvD protein.
Bosveld, F., Rana, A., van der Wouden, P. E., Lemstra, W., Ritsema, M., Kampinga, H. H., & Sibon, O. C. (2008). De novo CoA biosynthesis is required to maintain DNA integrity during development of the Drosophila nervous system. Human molecular genetics, 17(13), 2058-2069.Ryu T, Spatola B, Delabaere L, Bowlin K, Hopp H, Kunitake R, Karpen GH, Chiolo I. (2015) Heterochromatic breaks move to the nuclear periphery to continue recombinational repair. Nat Cell Biol. 2015 Nov;17(11):1401-11. doi: 10.1038/ncb3258. Epub 2015 Oct 26.Vujatovic O, Zaragoza K, Vaquero A, Reina O, Bernues J, Azorin F. (2012) Drosophila melanogaster linker histone dH1 is required for transposon silencing and to preserve genome integrity. Nucleic Acids Res. 2012 Jul;40(12):5402-14. doi: 10.1093/nar/gks224. Epub 2012 Mar 9.