癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
Phospho-Histone H3(S10) Antibody
Purified Mouse Monoclonal Antibody (Mab)
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, E |
|---|---|
| Primary Accession | P84243 |
| Other Accession | P61830, P02299, P08898, P02302, P02301, Q6NXT2, A5PK61, Q6PI79, P84245, P84246, Q71LE2, P84244, P84249, Q6PI20, P84247, Q5E9F8, Q27532, Q9U281, Q10453, P84233, P84228, Q71DI3, Q4QRF4, P84229, P84227, Q6LED0, P68433, P68431, P68432, Q16695 |
| Reactivity | Human, Mouse |
| Predicted | Rat, Rabbit, Zebrafish, Pig, Chicken, Yeast, Xenopus, Bovine, C.Elegans, Drosophila |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | Mouse IgG1 |
| Clone Names | 44AT1232.94 |
| Calculated MW | 15328 Da |
| Gene ID | 3020;3021 |
|---|---|
| Other Names | Histone H33, H3F3A, H33A, H3F3 |
| Target/Specificity | This Histone H3 Antibody is generated from mice immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S10 of human Histone H3. |
| Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
| Format | Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Phospho-Histone H3(S10) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | H3-3A (HGNC:4764) |
|---|---|
| Synonyms | H3.3A, H3F3, H3F3A |
| Function | Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. |
| Cellular Location | Nucleus. Chromosome |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene contains introns and its mRNA is polyadenylated, unlike most histone genes. The protein encoded is a replication-independent member of the histone H3 family.
REFERENCES
Distinct factors control histone variant H3.3 localization at specific genomic regions. Goldberg AD, et al. Cell, 2010 Mar 5. PMID 20211137.
New functions for an old variant: no substitute for histone H3.3. Elsaesser SJ, et al. Curr Opin Genet Dev, 2010 Apr. PMID 20153629.
ATRX interacts with H3.3 in maintaining telomere structural integrity in pluripotent embryonic stem cells. Wong LH, et al. Genome Res, 2010 Mar. PMID 20110566.
Phosphorylation of histone H3 by protein kinase C signaling plays a critical role in the regulation of the developmentally important TBX2 gene. Teng H, et al. J Biol Chem, 2009 Sep 25. PMID 19633291.
Organismal differences in post-translational modifications in histones H3 and H4. Garcia BA, et al. J Biol Chem, 2007 Mar 9. PMID 17194708.
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