Type of antibody:
Releasable antibodies, Primary antibodies, Recombinant antibodies
Alternative names:
MHC class I HLA-A2

Specifications for HLA-A2 Antibody, anti-human,


Clone REAL314 is an antibody fragment derived from the full HLA-A2 antibody molecule. It displays no binding to Fc receptors. The recombinantly engineered antibody fragments are multimerized to form the REAlease Complex to bind markers with high avidity.
Clone REAL314 recognizes the class I human leukocyte antigen A2 (HLA-A2). Expressed on the surface of most nucleated cells, class I molecules are heterodimeric molecules and consist of a type I integral membrane α heavy chain and a soluble β2 microglobulin protein. The extracellular region of the heavy chain further consists of three domains, one of which comprises the peptide binding groove. Antigens binding to class I molecules are 8–10 amino acids long and play an important role in recognition of virus infected and malignant cells by cytotoxic T lymphocytes (CTLs). In addition, class I molecules interact with natural killer (NK) cell receptors to modulate the activity of NK cells.
The REAlease Kits consist of the respective fluorochrome-conjugated REAlease Complexes and the REAlease Support Kit for removal of the REAlease Complexes and optional relabeling with different fluorochrome-conjugated REAlease Complexes.

Alternative names

MHC class I HLA-A2

Detailed product information

Technical specifications

Isotype controlControl Antibody
Hosthuman cell line
Type of antibodyReleasable antibodies, Primary antibodies, Recombinant antibodies
Alternative names of antigenMHC class I HLA-A2
RRIDAB_2811701, AB_2801704

Resources for HLA-A2 Antibody, anti-human,


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References for HLA-A2 Antibody, anti-human,


  1. Bjorkman, P. J. et al. (1987) Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329(6139): 506-512
  2. Hewitt, E. W. et al. (2003) The MHC class I antigen presentation pathway: strategies for viral immune evasion. Immunology 110(2): 163-169
  3. Smith, S. N. et al. (2013) Plasticity in the contribution of T cell receptor variable region residues to binding of peptide-HLA-A2 complexes. J. Mol. Biol. 425(22): 4496-4507

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