Technical Data
MHC Class 1 (Biotin)
Human MHC Class I (HLA-A, B & C) molecules are expressed on nearly all nucleated cells. MHC Class I molecules consist of heterodimers of a highly polymorphic transmembrane a chain and an invariant b chain. MHC Class I molecules bind to endogenously synthesized peptides of about 8-10 amino acids which are presented to CD8+ T cells. Recent evidence now indicates exogenously derived peptides are also presented by MHC Class I molecules.

Suitable for use in Flow Cytometry, ELISA and Immunohistochemistry. Functional Application: Antibody (whole molecule) is cytotoxic in the presence of complement (1). Other applications not tested.

Recommended Dilution:
Optimal dilutions to be determined by the researcher.

Flow Cytometry Analysis:
5x10e5 Ficoll prepared peripheral blood mononuclear cells (PBMC) were washed and incubated 45 minutes on ice with 80ul of M3885-48E at 5ug/ml. Cells were washed twice and incubated with secondary reagent Streptavidin/R-Phycoerythrin, after which they were washed three times, fixed and analyzed by FACS. Cells stained positive with a mean shift of 2.28 log10 fluorescent units when compared to a mouse IgG2a/Biotin negative control at a similar concentration. Binding was blocked when cells were pre incubated 10 minutes with 20ul of 0.5 mg/ml anti-MHC Class I antibody M3885-48D (unconjugated clone 7H121).

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 6 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
MabIgG2a7H121Affinity Purified
100ug-20CBlue IceHumanMouse
Human HSB-2 T cell line
Purified by Protein A affinity chromatography
Supplied as a liquid in PBS containing 5% glycerol, 0.2% BSA, 0.04% sodium azide
Recognizes a monomorphic Class I epitope on the a chain
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. G.S. Eisenbarth, et al, (1980) J Immunol 124: 1237-1244. 2. P.J. Bjorkman & P. Parham, (1990) Annu Rev Biochem 59: 253-288. 3. L.D. Barber & P. Parham, (1994) J Exp Med 180: 1191-1194. 4. K.L. Rock, (1996) Immunol Today 17: 131-137. 5. J Immunol (1985) 135(3): 1752-1759. 6.. A. Kawana-Tachikawa, A. Iwamoto, et al (2002) J Virol 76(23):11982-11988. 7. J.E. Shaw, R.W. Lang, et al (2001) J Virol Meth 94: 137-146.