Recombinant Histone H3 (Di Methyl Lys122) Monoclonal Antibody (AN302120L)
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For research use only.
| Verified Samples |
Verified Samples in IF: HeLa Verified Samples in ChIP: HeLa Verified Samples in WB: HeLa cytosol, HeLa nuclear, Mouse brain, Rat brain Verified Samples in IP: HeLa nuclear extracts |
| Dilution | WB 1:1000, IF 1:50, IP 1:25-1:100, ChIP 6 μg/5×106 cells |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | IF, ChIP, WB, IP |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Dimethylated human histone H3 (Lys122) peptide |
| Abbre | Histone H3 (Di Methyl Lys122) |
| 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 | 15 kDa |
| Observed MW |
15 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. | A844 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Post translational modifications on histones include acetylation, methylation, phosphorylation and some new acylation modifications found in recent years. These histone modifications directly affect the binding of chromatin to transcription factors or other epigenetic regulators, and change genome stability and gene transcription. Histone methylation usually occurs in lysine and arginine residues of core histones. Histone methylation can promote or inhibit gene transcription, depending on whether histone methylation occurs on lysine or arginine and the number of methylation groups (lysine can be monomethyl, dimethyl and trimethylated, arginine can be monomethyl, symmetric and asymmetric dimethyl). Histone lysine methylation usually occurs on lysine 4, 9, 27, 36, 79 of histone H3 and lysine 20 of histone H4; Arginine methylation usually occurs on arginine 2, 8, 17, 26 of histone H3 and arginine 3 of histone H4. Protein methylase (HMT) and histone demethylase (HDM) are the main regulators of methylation modification. H3K122me2 is a newly discovered modification site. |
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