Positive control:
Lane 1: human heart tissue lysate
Lane 2: human spleen tissue lysate
Lane 3: rat heart tissue lysate
Applications
-
WB
-
IHC-P
-
IP
REACTIVITY
-
Human
-
Mouse
-
Rat
SPECIFICATIONS
Product Type
Recombinant Rabbit monoclonal primary
Product Name
Recombinant Hemoglobin subunit alpha Monoclonal Antibody (ET1611-81)
Immunogen
Recombinant protein
Host
Rabbit
Positive Control
Human heart tissue lysate, human spleen tissue lysate, rat heart tissue lysate, human lung tissue, human spleen tissue, mouse embryo tissue.
Conjugation
Unconjugated
Clonality
Monoclonal
Clone Number
SN70-09
PROPERTIES
Form
Liquid
Storage Condition
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
Storage Buffer
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Concentration
1 ug/ul
PURIFICATION
Protein A affinity purified.
MOLECULAR WEIGHT
15 kDa
Isotype
IgG
APPLICATION DILUTION
-
WB
-
1:1,000
-
IHC-P
-
1:10-1:50
TARGET
UNIPROT #
PROTEIN NAME
Hemoglobin subunit alpha
SYNONYMS
Alpha 1 globin antibody; Alpha globin antibody; Alpha one globin antibody; Alpha-globin antibody; HBA_HUMAN antibody; HBA1 antibody; HBA2 antibody; Hemoglobin alpha 1 antibody; Hemoglobin alpha 1 chain antibody; Hemoglobin alpha 1 globin chain antibody; Hemoglobin alpha 2 antibody; Hemoglobin alpha chain antibody; Hemoglobin subunit alpha antibody; MGC126895 antibody; MGC126897 antibody
SEQUENCE SIMILARITIES
Belongs to the globin family.
TISSUE SPECIFICITY
Red blood cells.
POST-TRANSLATIONAL MODIFICATION
The initiator Met is not cleaved in variant Thionville and is acetylated.
SUBCELLULAR LOCATION
Cytosol, membrane, extracellular region
FUNCTION
Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The α (16p13.3; 5'-ζ-pseudoz-pseudo α2-pseudo α1-α2-α1-?1-3') and β (11p15.5) globin loci determine the basic hemoglobin structure. The globin portion of hemoglobin consists of two α chains and two β chains arranged in pairs forming a tetramer. Each of the four globin chains covalently associates with a heme group. The bonds between α and β 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 α1-β2 cleavage plane. When the two α1-β2 interfaces are closely bound, hemoglobin has a low affinity for oxygen. Hb A, which contains two α chains plus two β chains, comprises 97% of total circulating hemoglobin. The remaining 3% of total circulating hemoglobin is comprised of Hb A-2, which consists of two α chains plus two δ chains, and fetal hemoglobin (Hb F), which consists of two α chains together with two γ chains.