Rekombinanter HBA1 Antikörper (AA 1-100)

Produktnummer ABIN7867857

Der Maus Monoklonal anti-HBA1 Antikörper wird verwendet zum Nachweis von HBA1 in Proben von Human. Er wurde validiert für IHC (p).

Kurzübersicht für Rekombinanter HBA1 Antikörper (AA 1-100) (ABIN7867857)

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

Antikörpertyp: Recombinant Antibody

Reaktivität: Human

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Dieser HBA1 Antikörper ist unkonjugiert

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

Güteklasse: Carrier-free

Klon: RHBA-9167

Produktdetails anti-HBA1 Antikörper

Bindungsspezifität: AA 1-100

Verwendungszweck: Recombinant HBA Antibody / Hemoglobin alpha (azide and preservative free)

Aufreinigung: 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.

Isotyp: IgG2b, kappa

Anwendungsinformationen

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

Details zu HBA1

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

Andere Bezeichnung: HBA

Hintergrund: 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