Recombinant Histone H1 anticorps

N° du produit ABIN7881065

Cet anticorps Souris Monoclonal détecte spécifiquement Histone H1 dans IHC (p). Il présente une réactivité avec des échantillons de Humain.

Aperçu rapide pour Recombinant Histone H1 anticorps (ABIN7881065)

Antigène: Histone H1

Type d'anticorp: Recombinant Antibody

Reactivité: Humain

Hôte: Souris

Clonalité: Monoclonal

Conjugué: Cet anticorp Histone H1 est non-conjugé

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

Classe de qualité: Carrier-free

Clone: RHH1-8702

Détail du produit anti-Histone H1 anticorps

Fonction: Histone H1 Antibody (azide and preservative free)

Purification: Protein A/G affinity

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

Isotype: IgG2b, kappa

Information d'application

Indications d'application: Optimal dilution of the Histone H1 antibody should be determined by the researcher.

Restrictions: For Research Use only

Stockage

Format: Liquid

Concentration: 1 mg/mL

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

Agent conservateur: Azide free

Stock: -20 °C

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

Détails sur Histone H1

Antigène: Histone H1

Sujet: 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.