Mouse anti Human CD86 antibody, clone Bu63 recognizes human CD86 also known as B7-2, a type I transmembrane protein expressed by monocytes and activated B cells (Engel et al. 1994). CD86 acts as a co-stimulaory molecule along with CD80 (Lanier et al. 1995) and is a ligand for CD28 and CTLA-4 (Azuma et al. 1993).CD86 is a member of the Immunoglobulin superfamily and carries an extracellular domain bearing both an Ig-v-like domain which contains the CTLA-4 binding site and an adjacent C2-like domain. CD86 plays an important role in co-stimulation of T cell proliferation (Freeman et al. 1993), IL-2 production (Ribot et al. 2012) and in the primary immune response (Schultze et al. 1996).Domain depletion epitope mapping studies indicate that the binding site of Mouse anti Human CD86, clone Bu63 is located within the Ig-v-like domain of human CD86 (Jeanin et al. 1997).CD86 along with CD80 may be exploited as receptors for adenovirus entry into cells (Short et al. 2004 2006).
Mouse anti Human CD86 antibody, clone Bu63 recognizes human CD86 also known as B7-2, a type I transmembrane protein expressed by monocytes and activated B cells (Engel et al. 1994). CD86 acts as a co-stimulaory molecule along with CD80 (Lanier et al. 1995) and is a ligand for CD28 and CTLA-4 (Azuma et al. 1993).CD86 is a member of the Immunoglobulin superfamily and carries an extracellular domain bearing both an Ig-v-like domain which contains the CTLA-4 binding site and an adjacent C2-like domain. CD86 plays an important role in co-stimulation of T cell proliferation (Freeman et al. 1993), IL-2 production (Ribot et al. 2012) and in the primary immune response (Schultze et al. 1996).Domain depletion epitope mapping studies indicate that the binding site of Mouse anti Human CD86, clone Bu63 is located within the Ig-v-like domain of human CD86 (Jeanin et al. 1997).CD86 along with CD80 may be exploited as receptors for adenovirus entry into cells (Short et al. 2004 2006).
Mouse anti Human CD86 antibody, clone Bu63 recognizes human CD86 also known as B7-2, a type I transmembrane protein expressed by monocytes and activated B cells (Engel et al. 1994). CD86 acts as a co-stimulaory molecule along with CD80 (Lanier et al. 1995) and is a ligand for CD28 and CTLA-4 (Azuma et al. 1993).CD86 is a member of the Immunoglobulin superfamily and carries an extracellular domain bearing both an Ig-v-like domain which contains the CTLA-4 binding site and an adjacent C2-like domain. CD86 plays an important role in co-stimulation of T cell proliferation (Freeman et al. 1993), IL-2 production (Ribot et al. 2012) and in the primary immune response (Schultze et al. 1996).Domain depletion epitope mapping studies indicate that the binding site of Mouse anti Human CD86, clone Bu63 is located within the Ig-v-like domain of human CD86 (Jeanin et al. 1997).CD86 along with CD80 may be exploited as receptors for adenovirus entry into cells (Short et al. 2004 2006).
The monoclonal antibody BV4 recognizes human beta3 integrin subunit present in Platelet glycoprotein GPIIb-IIIa (integrin alphaIIb/beta3, CD41/CD61) and in the vitronectin receptor (integrin alphaV/beta3, CD51/CD61). Intergins are a family of heterodimeric membrane glycoproteins expressed on diverse cell types which function as the major receptors for extracellular matrix and as cell-cell adhesion molecules. As adhesion molecules they play an important role in numerous biological processes such as platelet aggregation, inflammation, immune function, wound healing, tumour metastasis and tissue migration during embryogenesis. In addition integrins are involved in signaling pathways, transmitting signals both into an out from cells. All integrins consist of two non-covalently associated subunits, alpha and beta. At least 12 different alpha subunits and 8 beta subunits have been identified. The beta subunits all contain 56 conserved cysteines (except beta4 which has 48) which are arranged in four repeating units. The beta3 subunit is a 93kDa protein that contains a large loop in the N-terminus stabilized by intrachain disulphide bonding with the first cysteine-rich repeat.<br /> Platelet glycoprotein GPIIb-IIIa is expressed on platelets and megakaryoblasts. It is constitutively expressed and becomes activated on triggered platelets. Platelet glycoprotein GPIIb-IIIa binds to fibrinogen, fibronectin, vWF, vitronectin and thrombospondin. Next to this it is also a receptor for several soluble adhesive proteins.Vitronectin receptor is expressed on endothelial cells, some B cells, monocytes/macrophages, platelets and tumour cells. Vitronectin receptor binds next to vitronectin to fibrinogen, vWF, thrombospondin, fibronectin, osteopontin and collagen. Defects in human beta3 integrin are a cause of Glanzmann thrombasthenia, which is an autosomal recessive disorder characterized by mucocutaneous bleeding and the inability of this integrin to recognize macromolecular or synthetic peptide ligands.
The histochemical antibody for Vesicular Monoamine Trnasporter 2 (VMAT2) is generated in a rabbit from a synthetic peptide corresponding to rat VMAT2 496-515 coupled to carrier protein. The antiserum is provided as l00 µL of lyophilized whole serum.
Product Type:
Antibody - Antibodies
Antibody Type:
polyclonal
Format:
Lyophilised
Host Animal:
Rabbit
Species Reactivity:
Rat
Expected Species:
100% sequence homology with rat, 85% with mouse and 93% with human
Immunogen:
Synthetic peptide corresponding to rat VMAT2 496-515 coupled to carrier protein.
Applications:
Immunohistochemistry, Immunocytochemistry, Western Blot
The VMAT2 antiserum was quality control tested using standard immunohistochemical methods in rat brain and adrenal medulla using biotin/avidin-HRP techniques. Specificity of the antiserum was demonstrated by soluble pre-adsorption and Western blot. Tissue staining is completely eliminated by pretreatment of the diluted antibody with an excess of rat VMAT2 peptide residues 496-515. Western blot analysis of immunoprecipitated rat brain homogenates demonstrates a dense immunoreactive band of approximately 55 kD and a minor band of approximately 75 kD.
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