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Human B7-2/CD86 Alexa Fluor 594 MAb (Clone 37301)  100 TESTS图1

Human B7-2/CD86 Alexa Fluor 594 MAb (Clone 37301) 100 TESTS

2024-11-24 16:56IP属地 广东省东莞市 电信00留言

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Flow Cytometry      
     

Detection of B7‑2/CD86 in Human PBMCs by Flow Cytometry. Human peripheral blood mononuclear cells (PBMCs) were stained with Mouse Anti-Human CD14 APC‑conjugated Monoclonal Antibody (Catalog # ) and either (A) Mouse Anti-Human B7‑2/CD86 Alexa Fluor® 594‑conjugated Monoclonal Antibody (Catalog # FAB141T) or (B) Mouse IgG1 Alexa Fluor 594 Isotype Control (Catalog # ). View our protocol for .

Preparation and Storage

Background: B7-2/CD86

B7-1 and B7-2, together with their receptors CD28 and CTLA-4, constitute one of the dominant costimulatory pathways that regulate T- and B-cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells, and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through Interferon-gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. Human B7-2 is a 329 amino acid (aa) protein containing a putative 23 aa signal peptide, a 224 aa extracellular domain, a 21 aa transmembrane domain, and a 61 aa cytoplasmic domain. Human B7-2 and B7-1 share 26% amino acid identity. Human and mouse B7-2 share 50% amino acid identity. However, it has been observed that both human and mouse B7‑1 and B7‑2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.

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