The H-2D[b]:Ig fusion protein consists of three extracellular major histocompatibility complex (MHC) class I H-2D[b] domains that are fused to the VH regions of mouse IgG1 (see Figure 1). In order for the MHC class I to be functional, ie, capable of binding peptides, ß2 Microglobulin (ß2M) must be present. For this reason, BD™ DimerX consists of recombinant H-2D[b]:Ig fusion protein, supplemented with recombinant ß2M. Recombinant MHC molecules, like the DimerX fusion protein, are useful for studying T-cell function by immunofluorescent staining and flow cytometric analysis of antigen-specific T cells. The MHC gene locus encodes a group of highly polymorphic, cell-surface proteins that play a broad role in the immune response to protein antigens. MHC molecules function by binding and presenting small antigenic protein fragments to antigen-specific receptors expressed by T cells (TCR). Human ( human leukocyte antigen /HLA) and mouse ( histocompatibility 2 /H-2) MHC molecules are structurally and functionally related proteins that comprise two major classes. Class I MHC molecules consist of two separate polypeptide chains. The class I α chain is an MHC encoded, transmembrane polypeptide containing three extracellular domains: α1, α2, and α3. The second chain consists of a non-MHC encoded polypeptide called ß2M. Since ß2M does not contain a transmembrane domain, it associates with the achain through noncovalent interaction. Functionally, class I MHC molecules can bind peptides derived from intracellular antigens (eg, viral and some bacterial antigens) that are specifically recognized by CD8+ T cells. Class II MHC molecules consist of two different transmembrane proteins that can bind peptide fragments derived from extracellular proteins (eg, bacteria and fungi) and are specifically recognized by CD4+ T cells. TCR recognize both processed peptides bound to MHC, as well as regions of the MHC molecule itself. CD4 and CD8 accessory molecules strengthen formation of the TCR-MHC complex through their interaction with non-polymorphic regions of the MHC molecule.

DimerX/H-2Db The H-2D[b]:Ig fusion protein consists of three extracellular major histocompatibility complex (MHC) class I H-2D[b] domains that are fused to the VH regions of mouse IgG1 (see Figure 1). In order for the MHC class I to be functional, ie, capable of binding peptides, ß2 Microglobulin (ß2M) must be present. For this reason, BD™ DimerX consists of recombinant H-2D[b]:Ig fusion protein, supplemented with recombinant ß2M. Recombinant MHC molecules, like the DimerX fusion protein, are useful for studying T-cell function by immunofluorescent staining and flow cytometric analysis of antigen-specific T cells. The MHC gene locus encodes a group of highly polymorphic, cell-surface proteins that play a broad role in the immune response to protein antigens. MHC molecules function by binding and presenting small antigenic protein fragments to antigen-specific receptors expressed by T cells (TCR). Human ( human leukocyte antigen /HLA) and mouse ( histocompatibility 2 /H-2) MHC molecules are structurally and functionally related proteins that comprise two major classes. Class I MHC molecules consist of two separate polypeptide chains. The class I α chain is an MHC encoded, transmembrane polypeptide containing three extracellular domains: α1, α2, and α3. The second chain consists of a non-MHC encoded polypeptide called ß2M. Since ß2M does not contain a transmembrane domain, it associates with the achain through noncovalent interaction. Functionally, class I MHC molecules can bind peptides derived from intracellular antigens (eg, viral and some bacterial antigens) that are specifically recognized by CD8+ T cells. Class II MHC molecules consist of two different transmembrane proteins that can bind peptide fragments derived from extracellular proteins (eg, bacteria and fungi) and are specifically recognized by CD4+ T cells. TCR recognize both processed peptides bound to MHC, as well as regions of the MHC molecule itself. CD4 and CD8 accessory molecules strengthen formation of the TCR-MHC complex through their interaction with non-polymorphic regions of the MHC molecule.

Mouse IgG1, λ

克隆 DimerX/H-2Db (RUO)

0.5 mg/ml

Flow cytometry (Routinely Tested)

H-2D[b]:Ig Fusion Protein

Aqueous buffered solution containing ≤0.09% sodium azide.

研发参考(7) 1. Dal Porto J, Johansen TE, Catipovic B, et al. A soluble divalent class I major histocompatibility complex molecule inhibits alloreactive T cells at nanomolar concentrations. Proc Natl Acad Sci U S A. 1993; 90(14):6671-6675. (Biology). 2. Mendel I, Kerlero de Rosbo N, Ben-Nun A. encephalomyelitis in H-2b mice: fine specificity and T cell receptor V beta expression of encephalitogenic T cells. Eur J Immunol. 1995; 25(7):1951-1959. (Biology). 3. Murali-Krishna K, Altman JD, Suresh M, et al. Counting antigen-specific CD8 T cells: a reevaluation of bystander activation during viral infection. Immunity. 1998; 8(2):177-187. (Biology). 4. Rammensee HG, Friede T, Stevanoviíc S. MHC ligands and peptide motifs: first listing. Immunogenetics. 1995; 41(4):178-228. (Biology). 5. Schneck JP, Slansky JE, O'Herrin SM, Greten TF . Monitoring antigen-specific T cells using MHC-Ig dimers. In: Coligan J, Kruisbeek D, Margulies EM, Shevach EM, Strober W, ed. Current Protocols in Immunology. New York: John Wiley & Sons, Inc; 2000:17.2.1-17.2.17. 6. Selin LK, Lin MY, Kraemer KA, et al. Attrition of T cell memory: selective loss of LCMV epitope-specific memory CD8 T cells following infections with heterologous viruses. Immunity. 1999; 11(6):733-742. (Biology). 7. Sun D, Zhang Y, Wei B, Peiper SC, Shao H, Kaplan HJ. Encephalitogenic activity of truncated myelin oligodendrocyte glycoprotein (MOG) peptides and their recognition by CD8+ MOG-speci®c T cells on oligomeric MHC class I molecules. Int Immunol. 2003; 26(10):2470-2479. (Biology: Flow cytometry).