Recombinant Phospho-Histone H3 (Ser10) Monoclonal Antibody (AN302105L)
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For research use only.
| Verified Samples |
Verified Samples in WB: HeLa, NIH-3T3 Verified Samples in ChIP: HeLa+Nocodazole(100ng/mL, 18h) Verified Samples in IP: HeLa+Nocodazole(100ng/mL, 18h) cells extracts |
| Dilution | WB 1:1000-1:5000, ChIP 6μg antibody/100μg chromatin, IP 1:50-1:100 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB, ChIP, IP |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab |
| Abbre | Phospho-Histone H3 (Ser10) |
| Synonyms | Histone H, H3C, H3/A, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3C10, H3C11, H3C12, HIST1H3A, H3C1, Histone H3.1, Histone H3/a, Histone H3/b, H3FL, HIST1H3B, H3FC, HIST1H3C, H3FB, HIST1H3D, H3FD, HIST1H3E, H3FI, HIST1H3F, H3FH, HIST1H3G, H3FK, HIST1H3H, H3FF, HIST1H3I, H3FJ, HIST1H3J, H3/A, H3FA, H3FB, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, Hist1h3a, HIST1H3B, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J, Histone H3.1, Histone H3/a, Histone H3/b, H3 histone family, H31, H3a, histone 1, Histone cluster 1, Histone H3/c, Histone H3/d, Histone H3/f, Histone H3/h, Histone H3/i, Histone H3/j, Histone H3/k, Histone H3/l, member A |
| Swissprot | |
| Calculated MW | 17 kDa |
| Observed MW |
17 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Nucleus |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Epigenetics and Nuclear Signaling, Isotype, Loading Controls |
| Clone No. | A829 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Crotonylation of lysine is a newly identified reversible modification controlling chromosome structure and gene transcription. The reversible lysine crotonylation has been well demonstrated in eukaryotic histones from worm to human. The unique structure and genomic localization of histone lysine crotonylation suggest that it is mechanistically and functionally different from histone lysine acetylation. Specifically, in both human somatic and mouse male germ cell genomes, histone crotonylation marks either active promoters or potential enhancers. Crotonylation of histone H4 at Lys5 may play a vital role in the epigenetic modulation, including chromatin remodeling and DNA transcriptional regulation. |
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