Rekombinanter Histone H1 Antikörper

Produktnummer ABIN7881065

Dieser Maus Monoklonal Antikörper detektiert spezifisch Histone H1 in IHC (p). Es zeigt Reaktivität gegenüber Proben von Human.

Kurzübersicht für Rekombinanter Histone H1 Antikörper (ABIN7881065)

Target: Histone H1

Antikörpertyp: Recombinant Antibody

Reaktivität: Human

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Dieser Histone H1 Antikörper ist unkonjugiert

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

Güteklasse: Carrier-free

Klon: RHH1-8702

Produktdetails anti-Histone H1 Antikörper

Verwendungszweck: Histone H1 Antibody (azide and preservative free)

Aufreinigung: Protein A/G affinity

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

Isotyp: IgG2b, kappa

Anwendungsinformationen

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

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Konzentration: 1 mg/mL

Buffer: 1 mg/mL in 1X PBS, BSA free, sodium azide free

Konservierungsmittel: Azide free

Lagerung: -20 °C

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

Details zu Histone H1

Target: Histone H1

Hintergrund: 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.