Recombinant HBA1 antibody (AA 1-100)

Catalog No. ABIN7867858

The Mouse Monoclonal anti-HBA1 antibody (Clone rHBA-9167) (ABIN7867858) specifically detects HBA1 in IHC (p). The antibody is reactive with Human samples.

Quick Overview for Recombinant HBA1 antibody (AA 1-100) (ABIN7867858)

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

Antibody Type: Recombinant Antibody

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This HBA1 antibody is un-conjugated

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

Clone: RHBA-9167

Product Details anti-HBA1 Antibody

Binding Specificity: AA 1-100

Purpose: Recombinant HBA Antibody / Hemoglobin alpha

Purification: Protein A/G affinity

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

Isotype: IgG2b, kappa

Application Details

Application Notes: Optimal dilution of the recombinant HBA 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 recombinant HBA antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.

Target Details for HBA1

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

Alternative Name: HBA

Background: 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