Recombinant Histone H3 (Acetyl Lys122) Monoclonal Antibody (AN301409L)

For research use only.
Verified Samples |
Verified Samples in WB: NIH/3T3, BRL, Rat liver, Mouse kidney, Recombinant Histone H3 (20 ng), HeLa Verified Samples in IHC: Human cerebrum, Human spleen, Human testis, Mouse cerebrum, Mouse kidney, Rat liver |
Dilution | WB 1:500-1:2000, IHC 1:200-1:1000 |
Isotype | IgG, κ |
Host | Rabbit |
Reactivity | Human, Rat, Mouse |
Applications | WB, IHC |
Clonality | Monoclonal;Recombinant |
Immunogen | Acetylated human histone H3 (Lys122) peptide |
Abbre | Histone H3 (Acetyl 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. | A104 |
Conjugation | Unconjugated |
Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
Shipping | Ice bag |
background | Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation and novel acylations directly affect the accessibility of chromatin to transcription factors and other epigenetic regulators, altering genome stability, gene transcription, etc. Histone acetylation occurs primarily at multiple lysine residues on the amino-terminal of core histones, in response to various stimuli and plays vital roles in the regulation of gene expression, DNA damage repair, chromatin dynamics, etc. Mostly, histone H2A is primarily acetylated at Lys5, 9, 15, and 36; H2B is primarily acetylated at Lys5, 12, 15, 16, and 20. Histone H3 is primarily acetylated at Lys4, 9, 14, 18, 23, 27, 56, and 79. Histone H4 is primarily acetylated at Lys5, 8, 12, 16, and 20. Histone acetyltransferases (HATs) and histone deacetylases (HDACs) are major regulating factors. |
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Unconjugated
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