Recombinant Histone H4 (CT) Monoclonal Antibody (AN301940L)
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For research use only.
| Verified Samples |
Verified Samples in WB: HeLa, C2C12, BRL, Saccharomyces cerevisiae, Pig brain, COS-7, Mouse liver, Rat kidney Verified Samples in IHC: Human colon, Human testis, Human cerebrum, Rat stomach, Mouse stomach |
| Dilution | WB 1:2000-1:10000, IHC 1:50-1:100 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse, Yeast, Pig |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Synthetic peptide corresponding to the C-terminus of human histone H4 protein |
| Abbre | Histone H4 |
| Synonyms | H4F, methyl histone H, methylated histone H, HIST2H, HIST1H, HISTH4H, histone H, HIST2H4B, H4/o, histone H4, HIST1H4A, FO108, H4/p, HIST1H4, Hist4h4, HISTH4H4, methyl histone H4, methylated histone H4, H4/A, H4FA, H4/I, H4FI, HIST1H4B, H4/G, H4FG, HIST1H4C, H4/B, H4FB, HIST1H4D, H4/J, H4FJ, HIST1H4E, H4/C, H4FC, HIST1H4F, H4/H, H4FH, HIST1H4H, H4/M, H4FM, HIST1H4I, H4/E, H4FE, H4/D, H4FD, HIST1H4K, H4/K, H4FK, HIST1H4L, H4/N, H4F2, H4FN, HIST2H4, HIST2H4A, H4, H4C1, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4C11, H4C12, H4C13, H4C14, H4C15, H4-16, A, I, H4B, H4J, H4H, H4M, H4E, HIST1H4J, H4D, H4C, H4/p, histone H4, HIST1H4B H4/I |
| Swissprot | |
| Calculated MW | 11 kDa |
| Observed MW |
11 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 |
| Clone No. | A656 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Histones are a family of basic proteins that form the core of the nucleosome – the fundamental structural unit of chromatin. In a single nucleosome, core histone proteins H2A, H2B, H3, and H4 form an octamer around which the DNA is tightly wrapped. Histone proteins not only serve to compact chromosomal DNA but also play vital roles in the dynamic and long-term regulation of genes by a wide variety of post-translational modifications (PTMs). These PTMs including acetylation, methylation, phosphorylation, and novel acylations directly affect the accessibility of chromatin to transcription factors and other epigenetic regulators, altering genome stability and gene transcription. Histone H4 is primarily acetylated at Lys5, 8, 12, and 16, and methylated at Lys20. |
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Unconjugated
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