Description
HLA-A Antibody | 18-549 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 35-285 of human HLA-A (NP_001229687.1) .
Research Area: Immunology
Tested Application: WB, IHC
Application: WB: 1:500 - 1:2000
IHC: 1:50 - 1:200
Specificiy: N/A
Positive Control 1: THP-1
Positive Control 2: DU145
Positive Control 3: SW480
Positive Control 4: HepG2
Positive Control 5: Mouse liver
Positive Control 6: N/A
Molecular Weight: Observed: 43kDa
Validation: N/A
Isoform: N/A
Purification: Affinity purification
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration: N/A
Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.
Alternate Name: HLAA, HLA class I histocompatibility antigen, A-1 alpha chain, MHC class I antigen HLA-A heavy chain, leukocyte antigen class I-A
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: HLA-A belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin) . The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-A alleles have been described.