Recombinant HBA1 anticorps (AA 1-100)

N° du produit ABIN7867860

L’anticorps anti-HBA1 Monoclonal Lapin est utilisé pour la détection de HBA1 dans des échantillons de Humain. Il a été validé pour IHC (p).

Aperçu rapide pour Recombinant HBA1 anticorps (AA 1-100) (ABIN7867860)

Antigène: HBA1 (Hemoglobin, alpha 1 (HBA1))

Type d'anticorp: Recombinant Antibody

Reactivité: Humain

Hôte: Lapin

Clonalité: Monoclonal

Conjugué: Cet anticorp HBA1 est non-conjugé

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

Clone: HBA-9193R

Détail du produit anti-HBA1 anticorps

Épitope: AA 1-100

Fonction: Recombinant Hemoglobin alpha Antibody / HBA

Purification: Protein A/G affinity

Immunogène: A recombinant fragment (within amino acids 1-100) of human HBA2 protein was used as the immunogen for the recombinant Hemoglobin alpha antibody.

Isotype: IgG, kappa

Information d'application

Indications d'application: Optimal dilution of the recombinant Hemoglobin alpha antibody should be determined by the researcher.

Restrictions: For Research Use only

Stockage

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

Agent conservateur: Sodium azide

Précaution d'utilisation: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Stock: -20 °C

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

Détails sur HBA1

Antigène: HBA1 (Hemoglobin, alpha 1 (HBA1))

Autre désignation: Hemoglobin alpha

Sujet: Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The alpha and beta globin loci determine the basic Hgb structure. The globin portion of Hgb consists of two alpha chains and two beta chains arranged in pairs forming a tetramer. Each of the four globin chains covalently associates with a heme group. The bonds between alpha and beta chains are weaker than between similar globin chains, thereby forming a cleavage plane that is important for oxygen binding and release. High affinity for oxygen occurs upon relaxation of the alpha1-beta2 cleavage plane. When the two alpha1-beta2 interfaces are closely bound, Hgb has a low affinity for oxygen. Hb A, which contains two alpha chains plus two beta chains, comprises 97 % of total circulating hemoglobin. The remaining 3 % of total circulating hemoglobin is comprised of Hb A-2, which consists of two alpha chains plus two delta chains, and fetal hemoglobin (Hb F), which consists of two alpha chains together with two gamma chains.

UniProt: P69905