Anti-Human HLA A2,B7 (MHC Class I) - Purified in vivo PLATINUM™ Functional Grade
Referencia H2685-1
embalaje : 1.0mg
Marca : Leinco Technologies
AntiHuman HLA A2,B7 (MHC Class I) – Purified in vivo PLATINUM™ Functional Grade
AntiHuman HLA A2,B7 (MHC Class I) – Purified in vivo PLATINUM™ Functional Grade
Product No.: H2685
Clone BB7.6 Target HLAA2,B7 MHC Class I Formats AvailableView All Product Type Monoclonal Antibody Alternate Names HLAA, HLAA2,B7, B.C.HLAA2 Isotype Mouse IgG1 Applications FC |
Antibody DetailsProduct DetailsReactive Species Human Host Species Mouse Recommended Isotype Controls Recommended Isotype Controls Recommended Dilution Buffer Immunogen Solubilized HLAB7 antigen Product Concentration ≥ 5.0 mg/ml Endotoxin Level <0.5 EU/mg as determined by the LAL method Purity ≥98% monomer by analytical SEC ⋅ >95% by SDS Page Formulation This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration. Product Preparation Functional grade preclinical antibodies are manufactured in an animal free facility using in vitro cell culture techniques and are purified by a multistep process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates. Pathogen Testing To protect mouse colonies from infection by pathogens and to assure that experimental preclinical data is not affected by such pathogens, all of Leinco’s Purified Functional PLATINUM™ antibodies are tested and guaranteed to be negative for all pathogens in the IDEXX IMPACT I Mouse Profile. Storage and Handling Functional grade preclinical antibodies may be stored sterile as received at 28°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at ≤ 70°C. Avoid Repeated Freeze Thaw Cycles. Country of Origin USA Shipping Next Day 28°C RRIDAB_2893763 Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. DescriptionDescriptionSpecificity Clone BB7.6 recognizes an epitope shared by the human MHC class I molecule HLAB. Background HLAB antibody, clone BB7.6, recognizes a shared epitope (Bw6) of the major histocompatibility complex (MHC) class I molecule human leukocyte antigen (HLA)B1. MHC class I is ubiquitously expressed on the cell surface of nucleated cells and consists of a 45kDa type I transmembrane glycoprotein (αchain or heavy chain) and a 12kDa soluble protein (β2microglobulin, β2M)2,3. The αchain consists of three domains (α1, α2, and α3)4. α1 and α2 form the closed antigenbinding groove and bind to 810 aa peptides derived from cytosolic antigens57. β2M noncovalently associates with α3, which is essential for MHC stability. MHC class I plays a critical role in the adaptive immune response by presenting endogenous antigens to cytotoxic CD8 T cells. MHC class I molecules can also present exogenous antigens to CD8 T cells via a process known as crosspresentation8. The T cell receptor (TCR)/CD3 complex of CD8 T cells interacts with peptideMHC class I, which induces CD8 T cell activation and subsequent cellkilling. CD8 molecules also bind to MHC class I, which helps augment TCR signaling9. In contrast to CD8 T cells, MHC class I is an inhibitory ligand for natural killer (NK) cells, promoting self tolerance10. MHC class I also contributes to the positive selection of CD8 T cells and NK cell specificity11,12. Antigen Distribution HLAB is ubiquitously expressed on nucleated cells. Research Area Immunology Leinco Antibody AdvisorPowered by AI: AI is experimental and still learning how to provide the best assistance. It may occasionally generate incorrect or incomplete responses. Please do not rely solely on its recommendations when making purchasing decisions or designing experiments. Clone BB7.6 is most commonly used in vivo in mice to specifically target human HLAA2 and HLAB7 molecules, particularly in models where human cells expressing these MHC class I proteins are introduced, such as xenograft and humanized mouse models. Key in vivo applications include:
BB7.6 is not reactive to mouse MHC, so its applications are restricted to models where human HLAA2/B7 is present, and it is predominantly used for research rather than direct clinical or diagnostic procedures. Applications in mice include functional assays, cell depletion, and cell tracking via flow cytometry and related techniques. Other antibodies and proteins frequently used with BB7.6 in the literature include:
Additional experimental contexts may include:
Commonly, these antibodies are applied in:
In summary, the most referenced antibodies and proteins used with BB7.6 are antiBw4 mAbs, antiBw6 mAbs such as SFR8B6, and other HLAspecific monoclonal antibodies (BB7.1, BB7.2, PA2.1, MA2.1), frequently in combination to analyze the specificity and structural characteristics of HLA class I molecules. Clone BB7.6 is a monoclonal antibody that has yielded important insights into HLA class I epitope recognition and immune system function through its extensive use in scientific research. Epitope Specificity and RecognitionClone BB7.6 recognizes the Bw6 public epitope on HLA class I molecules. More specifically, it binds to a shared epitope of the major histocompatibility complex (MHC) class I molecule human leukocyte antigen (HLA)B. This recognition is critical for understanding how antibodies distinguish between different HLA variants. Molecular Basis of BindingSitedirected mutagenesis studies have revealed the precise molecular determinants of BB7.6 binding. Research demonstrated that substitution of residue 83 (G83R) abrogates binding by the BB7.6 antiBw6 monoclonal antibody, likely due to steric hindrance. This finding highlights the importance of specific amino acid residues in the 7783 region for antibody recognition. The studies indicate that even though antibodyantigen contact sites are large, a few amino acid side chains often provide most of the binding energy. Epitope HeterogeneityA major conclusion from research using BB7.6 is that the Bw6 epitope is heterogeneous, and antiBw6 antibodies form energetic contacts with particular amino acids in the 7783 region. This heterogeneity means that Bw6 epitopes are best regarded as families of related structures rather than a single uniform target. Functional ContextThe antibody recognizes epitopes on HLAB molecules, which are type I transmembrane glycoproteins that form part of the MHC class I complex. These molecules play a critical role in the adaptive immune response by presenting endogenous antigens to cytotoxic CD8 T cells. Understanding how BB7.6 recognizes these molecules helps elucidate the broader mechanisms of immune recognition and HLAmediated immune responses. There is insufficient published data directly detailing how the dosing regimens of clone BB7.6 (an antiHLAA2 antibody) vary across different mouse models. Most available information related to BB7.6 focuses on its specificity, applications in flow cytometry, and use in identifying or depleting human HLAA2 or A2/B7expressing cells in mice engrafted with human tissues or cells. Essential context and supporting details:
Additional relevant information:
In summary, there are no standardized or published clone BB7.6 dosing regimens across mouse models. Empirical titration based on the scientific objective, similar antibody precedents, and mouse model specifics remains the recommended approach. References & Citations1. Lutz CT, et al. (1994) J Immunol. 153(9):4099110. 2. Mitaksov V & Fremont DH. (2006) J Biol Chem. 281(15):1061825. 3. Wieczorek M, et al. (2017) Front Immunol. 8:292. 4. Jones EY. (1997) Curr Opin Immunol. 9(1):759. 5. Matsumura M, et al (1992) Science. 257:927–34.10.1126/science.1323878 6. Bouvier M & Wiley DC. (1994) Science. 398–402.10.1126/science.8023162 7. Zacharias M & Springer S. (2004) Biophys J. 87:2203–14.10.1529/biophysj.104.044743 8. Cruz FM, et al. (2017) Annu Rev Immunol. 35:149176. 9. Artyomov MN, et al. (2010) Proc Natl Acad Sci USA. 107(39):1691616921. 10. Orr MT & Lanier LL. (2010) Cell. 142(6):847856. 11. Raulet DH. (1994) Adv Immunol. 55:381421. 12. Salcedo M & Ljunggren HG. (1996) Chem Immunol. 64:4458. |

