| CatalogCode: | NB110-57045 |
| ProductName: | Acetyl-Histone H3 (K9) Antibody |
| Product Description: | Rabbit Monoclonal anti-Acetyl-Histone H3 (K9) (Y28) |
| Clone: | Y28 |
| Clonality: | Monoclonal |
| Specificity: | A synthetic acetylated peptide corresponding to residues surrounding Lys9 of Histone H3 was used as immunogen. The antibody only detects Histone H3 acetylated on Lysine 9. |
| CrossReactivity: | Reacts in human and mouse. Does not react in rat. Not tested in other species. |
| Packaging: | 0.1 ml |
| Uses: | WB: 1:500IHC: 1:50 - 100 ICC: 1:250IP: 1:40 |
| Background: | Changes in chromatin structure play a large role in the regulation of transcription in eukaryotes (1). The nucleosome is the primary building block of chromatin, and is made up of four core histone proteins (H2A, H2B, H3 and H4) (2). Acetylation of core histones regulates gene expression (2). Histone H3 is primarily acetylated at lysines 9, 14, 18, and 23 (3,4). Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (3,4). |
| Storage: | Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles. |
| Isotype: | IgG |
| Host_Name: | Rabbit |
| Buffer: | 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, and 0.05% BSA. |
| ListPrice: | 325 |
| AppSummary: | IHC, IP, WB, ICC |
| SpeciesSummary: | Hu, Mu, Rt(-) |
| ALTnames: | anti-H3 3A antibody, anti-H3 Histone antibody, anti-H3 Histone Family Member E Pseudogene antibody, anti-H3.4 antibody, anti-H3/g antibody, anti-H3F3 antibody, anti-H3FT antibody, anti-H3t antibody, anti-HIST3H3 antibody, anti-Histone H3 3 Pseudogene antibody |
| PackageSize: | 0.1 ml |
| GeneralRef: | 1. Braunstein, M., et al. Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern. Mol. Cell. Biol. 16: 4349-56 (1996). 2. Workman, J.L. and R.E. Kingston. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67: 545-579 (1998). 3. Hansen, J.C. et al. Structure and function of the core histone N-termini: more than meets the eye. Biochemistry 37, 17637-17641 (1998). 4. Strahl, B.D. and C.D. Allis. The language of covalent histone modifications. Nature 403, 41-45 (2000). |
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