Recombinant Histone H1 antibody

Catalog No. ABIN7881066

The Mouse Monoclonal anti-Histone H1 antibody is suitable to detect Histone H1 in samples from Human. It has been validated for IHC (p).

Quick Overview for Recombinant Histone H1 antibody (ABIN7881066)

Target: Histone H1

Antibody Type: Recombinant Antibody

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This Histone H1 antibody is un-conjugated

Application: Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))

Clone: RHH1-8702

Product Details anti-Histone H1 Antibody

Purpose: Histone H1 Antibody

Purification: Protein A/G affinity

Immunogen: Nuclei of human leukemia biopsy cells were used as the immunogen for the Histone H1 antibody.

Isotype: IgG2b, kappa

Application Details

Application Notes: Optimal dilution of the Histone H1 antibody should be determined by the researcher.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 0.2 mg/mL

Buffer: 0.2 mg/mL in 1X PBS with 0.1 mg/mL BSA (US sourced), 0.05 % sodium azide

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: Aliquot the Histone H1 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.

Target Details for Histone H1

Target: Histone H1

Background: Eukaryotic histones are basic and water-soluble nuclear proteins that form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer, formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80 % of nucleosomes contain the linker Histone H1, derived from an intronless gene that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.