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The RPA-2.10 antibody reacts with human CD2, an approximately 50 kDa glycoprotein, and a member of the Ig superfamily. CD2, also known as LFA-2, is a receptor for CD58 in the human and is expressed on the cell surface of 80-90% of human peripheral blood lymphocytes, a subset of NK cells, and all mature T cells. CD2 mediates lymphocyte adhesion and is involved in T cell activation.

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Goat anti-Human IgE (epsilon chain) - Affinity Pure, min x w/bovine, mouse or rabbit serum proteins

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Goat anti-Human IgA (alpha chain) - Affinity Pure, Biotin Conjugate

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The 3.9 antibody reacts with human CD11c, also known as integrin alpha X. This 150 kDa cell surface glycoprotein is part of a family of integrin receptors that mediate adhesion between cells (cell-cell) and components of the extracellular matrix, e.g. fibrinogen (cell-matrix). In addition, integrins are active signaling receptors which recruit leukocytes to inflammatory sites and promote cell activation. Complete, functional integrin receptors consist of distinct combinations of integrin chains which are differentially expressed. Integrin alpha X (CD11c) assembles with Integrin beta-2 (CD18) into a receptor known as CR4 which can bind and induce signaling through ICAMs and VCAM-1 on endothelial cells and can also facilitate removal of iC3b bearing foreign cells.

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The 17A2 antibody reacts with the mouse CD3 complex, comprised of CD3 epsilon, CD3 gamma and CD3 delta. These integral membrane protein chains assemble with additional chains of the T cell receptor (TCR), as well as CD3 zeta chain, to form the T cell receptor – CD3 complex. Together with co-receptors CD4 or CD8, the complex serves to recognize antigens bound to MHC molecules on antigen-presenting cells. Such interactions promote T cell receptor signaling (T cell activation) and can result in a number of cellular responses including proliferation, differentiation, production of cytokines or activation-induced cell death. CD3 is differentially expressed during thymocyte-to-T cell development and on all mature T cells.

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The UCHT1 antibody is specific for human CD3e, also known as CD3 epsilon, a 20 kDa subunit of the T cell receptor complex, along with CD3 gamma and CD3 delta. These integral membrane protein chains assemble with additional chains of the T cell receptor (TCR), as well as CD3 zeta chain, to form the T cell receptor – CD3 complex. Together with co-receptors CD4 or CD8, the complex serves to recognize antigens bound to MHC molecules on antigen-presenting cells. These interactions promote T cell receptor signaling (T cell activation), inducing cell proliferation, differentiation, production of cytokines or activation-induced cell death. CD3 is differentially expressed during thymocyte-to-T cell development and on all mature T cells.

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The HP-3G10 antibody is specific for human CD161, also known as NKR-P1A, a type II transmembrane lectin-like receptor and member of the killer cell lectin-like receptor (KLR) family. CD161 exists as a homodimer which is prominently expressed on natural killer (NK) and NKT cells, where it is proposed to regulate the function of both cell types. CD161 is also found on T cell subsets, including T regulatory cells (Tregs), memory/effector CD4+ T cells, and CD8+ T cells. Th17 cells have been demonstrated to co-express CD161, as surface IL-17A+ cells are contained within the CD161+ fraction of CD4 T cells, so that CD161 (in combination with CCR6) is often used as a marker for enrichment of Th17 cells.

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The RB6-8C5 antibody binds to mouse Ly-6G, commonly known as Gr-1, a member of the Ly-6 superfamily of GPI-anchored cell surface proteins with roles in cell signaling and cell adhesion. Gr-1 is differentially expressed during development and maturation of cells in the myeloid lineage and is expression at varying stages and levels on monocytes, macrophages, granulocytes, and peripheral neutrophils.

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The 30-H12 antibody reacts with mouse CD90.2 (Thy1.2). CD90.2 is a strain-specific allelic form of the GPI-linked membrane associated protein CD90 and is involved in adhesion and signal transduction. CD90.2 is expressed on thymocytes, mature T cells and neurons in mouse strains that express the CD90.2 allele (BALB/c, CBA, C3H, C57BL/6, SJL and others). 30-H12 does not react with the CD90.1 allele expressed in mouse strains such as PL and AKR.

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The IM7 antibody recognizes CD44, a ubiquitously expressed cell surface receptor which is important for extracellular matrix organization, cell-cell and cell-matrix adhesion and migration. CD44 may be expressed in a number of different isoforms (splice variants) from the most typical or “standard” form, known as CD44s, to variants designated CD44v, e.g. CD44v1 or CD44v6. These receptors interact with several ligands, but most often associate with an extracellular matrix component hyaluronate, through which it mediates adhesion.

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The RA3-6B2 antibody reacts with the human and mouse CD45 isoform known as CD45R, or B220, a protein tyrosine phosphatase of 220 kDa. CD45 is one of the most abundant hematopoietic markers, and is expressed on all leukocytes (the Leukocyte Common Antigen, LCA). Various isoforms are generated and expressed in cell-specific patterns, all critical for leukocyte function. In mouse, the CD45R/B220 isoform is predominantly found on B cells, at varying levels on all stages from pro-B cells to activated B cells, and may also be detected on certain T cell and NK cell subsets. It is of note that B220 is not similarly expressed on human B cells, where it appears to be differentiation-specific and therefore expressed on only some B cell subsets. Other forms of CD45 with restricted cellular expression include CD45RA, CD45RB and CD45RO.

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The 15.2 antibody reacts with human CD54, also known as ICAM-1 (Intercellular Adhesion Molecule 1), a 90-110 kDa cell surface glycoprotein that is inducibly expressed on both immune and endothelial cells. As its name implies, ICAM-1 participates in cell-cell adhesion between leukocytes and endothelial cells, facilitating leukocyte recruitment and transmigration at sites of inflammation. The ligands for ICAM-1 are also expressed on leukocyte and endothelial cells, and include Mac-1, fibrinogen, and a member of the integrin protein family, LFA-1 (CD11a).

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The 53-6.7 antibody reacts with the 32-34 kDa alpha subunit of mouse CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor in antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

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The RB6-8C5 antibody binds to mouse Ly-6G, commonly known as Gr-1, a member of the Ly-6 superfamily of GPI-anchored cell surface proteins with roles in cell signaling and cell adhesion. Gr-1 is differentially expressed during development and maturation of cells in the myeloid lineage and is expression at varying stages and levels on monocytes, macrophages, granulocytes, and peripheral neutrophils.

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The PC61.5 antibody is specific for mouse CD25, a 55 kDa surface protein also known as the Interleukin-2 Receptor alpha chain, or IL-2R alpha. CD25 may bind IL-2 by itself, although with low affinity and without induction of cell signaling. CD25 is also expressed within a high-affinity complex, along with the IL-2R beta chain (CD122) and the common gamma chain (CD132), to form a signaling receptor complex. Expression of CD25 varies during developmental stages of T and B cells, is induced on activated mature T and B cells, and is present on subsets of dendritic cells. CD25 signaling as part of the IL-2 receptor complex triggers T cell activation and proliferation, as well as modulating the differentiation and function of Th17 cells, T regulatory (Treg) cells, and dendritic cells.

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The 16-10A1 antibody reacts with mouse CD80, also known as B7-1, a 55 kDa type I transmembrane protein ligand for CD152 (CTLA-4) and for CD28, a co-stimulatory receptor for the T cell receptor (TCR). CD28 also binds a second B7 ligand known as CD86 (B7-2). Both CD80 and CD86 are expressed on activated B cells and antigen-presenting cells. These ligands trigger CD28 signaling in concert with TCR activation to drive T cell proliferation, induce high-level expression of IL-2, impart resistance to apoptosis, and enhance T cell cytotoxicity. The interaction / co-stimulatory signaling between the B7 ligands and CD28 or CTLA-4 provides crucial communication between T cells and B cells or APCs to coordinate the adaptive immune response.

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The A20 antibody reacts with mouse CD45.1, also known as Ly5.1, which is a strain-specific allelic form of the CD45 Leukocyte Common Antigen (LCA). Functionally, CD45 is a protein tyrosine phosphatase whose broad cell distribution supports a critical role in many leukocyte functions, including regulation of signal transduction and cell activation associated with the T cell and B cell receptors.

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The 30-F11 antibody reacts with mouse CD45, which is one of the most abundant hematopoietic markers and is expressed on all leukocytes (the Leukocyte Common Antigen, LCA). CD45 is a protein tyrosine phosphatase existing in several isoforms, each being generated and expressed in cell-specific patterns. With its broad cell distribution, CD45 is critical for many leukocyte functions, regulating signal transduction and cell activation associated with the T cell receptor, B cell receptor, and IL-2 receptor. Other forms of CD45, with restricted cellular expression, include CD45R (B220), CD45RA, CD45RB and CD45RO.

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The PC61.5 antibody is specific for mouse CD25, a 55 kDa surface protein also known as the Interleukin-2 Receptor alpha chain, or IL-2R alpha. CD25 may bind IL-2 by itself, although with low affinity and without induction of cell signaling. CD25 is also expressed within a high-affinity complex, along with the IL-2R beta chain (CD122) and the common gamma chain (CD132), to form a signaling receptor complex. Expression of CD25 varies during developmental stages of T and B cells, is induced on activated mature T and B cells, and is present on subsets of dendritic cells. CD25 signaling as part of the IL-2 receptor complex triggers T cell activation and proliferation, as well as modulating the differentiation and function of Th17 cells, T regulatory (Treg) cells, and dendritic cells.

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The JES5-2A5 antibody is specific for mouse IL-10. IL-10 has numerous biological activities including the ability to inhibit both the synthesis of Th1 cytokines and proliferation of T cells. In the mouse, IL-10 is produced by phagocytic cells, conventional dendritic, cells, T cells, B cells, and NK cells. The JES5-2A5 antibody is a neutralizing antibody.

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The HI30 antibody reacts with human CD45, one of the most abundant hematopoietic markers and one that is expressed on all leukocytes (the Leukocyte Common Antigen, LCA). CD45 is a protein tyrosine phosphatase existing in several isoforms, each being generated and expressed in cell-specific patterns. With its broad cell distribution, CD45 is critical for many leukocyte functions, regulating signal transduction and cell activation associated with the T cell receptor, B cell receptor, and IL-2 receptor. Other forms of CD45, with restricted cellular expression, include CD45R (B220), CD45RA, CD45RB, CD45RO and others.

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The MR1 antibody is specific for mouse CD154, a 39 kD glycoprotein that is primarily expressed on activated T cells. CD154 (CD40 ligand, gp39) binds to CD40 expressed on antigen presenting cells and mediates important costimulatory functions between these cells. Signals generated via cognate interactions between CD154-CD40 on activated T and B cells are required for T-dependent B cell responses. The MR1 antibody is reported to block interaction of CD154 with CD40.

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The 2H7 antibody reacts with human CD20, expressed by pre-B cells, resting and activated B cells, follicular dendritic cells and a small subset of T cells, but not on plasma cells. CD20 is a 33-37 kDa transmembrane protein which is differentially phosphorylated in resting and active B cells. The CD20 molecule plays a role in regulating B-cell activation.

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The 2D1 antibody reacts with human CD45, one of the most abundant hematopoietic markers and one that is expressed on all leukocytes (the Leukocyte Common Antigen, LCA). CD45 is a protein tyrosine phosphatase existing in several isoforms, each being generated and expressed in cell-specific patterns. With its broad cell distribution, CD45 is critical for many leukocyte functions, regulating signal transduction and cell activation associated with the T cell receptor, B cell receptor, and IL-2 receptor. Other forms of CD45, with restricted cellular expression, include CD45R (B220), CD45RA, CD45RB, and CD45RO.

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The 2D1 antibody reacts with human CD45, one of the most abundant hematopoietic markers and one that is expressed on all leukocytes (the Leukocyte Common Antigen, LCA). CD45 is a protein tyrosine phosphatase existing in several isoforms, each being generated and expressed in cell-specific patterns. With its broad cell distribution, CD45 is critical for many leukocyte functions, regulating signal transduction and cell activation associated with the T cell receptor, B cell receptor, and IL-2 receptor. Other forms of CD45, with restricted cellular expression, include CD45R (B220), CD45RA, CD45RB, and CD45RO.

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The SK3 antibody reacts with human CD4, a 59 kDa protein which acts as a co-receptor for the T cell receptor (TCR) in its interaction with MHC Class II molecules on antigen-presenting cells. The extracellular domain of CD4 binds to the beta-2 domain of MHC Class II, while its cytoplasmic tail provides a binding site for the tyrosine kinase lck, facilitating the signaling cascade that initiates T cell activation. CD4, and co-receptors CCR5 and CXCR4, may also be utilized by HIV-1 to enter T cells. Human CD4 is typically expressed on thymocytes, some mature T cell populations such as Th17 and T regulatory (Treg) cells, as well as on dendritic cells. The SK3 antibody is widely used as a phenotypic marker for human CD4 expression, and has been reported to be cross-reactive with Rhesus and Cynomolgus CD4. This antibody does not block binding of alternative clone RPA-T4, suggesting that they recognize different epitopes.

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The MEL-14 antibody is specific for mouse CD62L, also known as L-Selectin, a cell adhesion molecule which facilitates lymphocyte "rolling" on activated vascular endothelium and homing to high endothelial venules (HEV) as immune cells transmigrate from blood into peripheral tissues. L-Selectin is a member of a family of Selectin molecules which act together with the integrin family of adhesion molecules to mediate leukocyte-endothelial interactions. L-Selectin is characteristically expressed by neutrophils, and is also found on B cells, monocytes, granulocytes, and at varying levels on naive, effector and memory T cells. It is rapidly shed upon cell activation, releasing into the circulation a soluble form whose biological role is of particular interest in cancer biology research. The MEL-14 antibody may be used as a phenotypic marker for CD62L expression on a variety of immune cell types. Please note that CD62L (L-Selectin) itself is also referred to as MEL-14 in the literature.

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The MY31 antibody reacts with human CD56, also known as the neural cell adhesion molecule (NCAM), a glycoprotein which is a member of the immunoglobulin superfamily. The 140 kDa isoform of CD56 is expressed on human NK cells and NK-T cells, with increased expression levels on activated NK lymphocytes. The CD56 antigen is also expressed by neurons and is reported to play a role in nervous system development and neural cell-to-cell adhesion. Clone MY31 also reacts with a subset of CD14+ monocytes in non-human primates, and is reported to be cross-reactive with Chimpanzee, Cynomolgus and Rhesus.

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The O323 antibody reacts with human CD27 (TNFRSF7), a cell surface homodimer of 55 kDa subunits, which provides co-stimulatory signaling in support of the T cell (TCR) and B cell (BCR) receptors. By comparison with CD28, whose TCR co-stimulatory signal can trigger cell proliferation, CD27 signaling appears to promote cell survival and differentiation to effector / memory stages. Also in contrast with CD28, the CD27 receptor may be shed following interaction with its ligand CD70, which is typically expressed on activated dendritic cells, T cells and B cells. With respect to B cells, CD27 is considered to be a phenotypic marker for memory B cells. CD27 has been included within a group of phenotypic markers for identifying human B regulatory cells (Bregs), a cell type proposed to regulate CD4+ T cell proliferation and Foxp3 / CTLA-4 expression in Treg cells.

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The 145-2C11 antibody is specific for mouse CD3e, also known as CD3 epsilon, a 20 kDa subunit of the T cell receptor complex, along with CD3 gamma and CD3 delta. These integral membrane protein chains assemble with additional chains of the T cell receptor (TCR), as well as CD3 zeta chain, to form the T cell receptor CD3 complex. Together with co-receptors CD4 or CD8, the complex serves to recognize antigens bound to MHC molecules on antigen-presenting cells. Such interactions promote T cell receptor signaling (T cell activation) and can result in a number of cellular responses including proliferation, differentiation, production of cytokines or activation-induced cell death. CD3 is differentially expressed during thymocyte-to-T cell development and on all mature T cells. The 145-2C11 antibody is a widely used phenotypic marker for mouse T cells. In addition, binding of 145-2C11 antibody to CD3e can induce cell activation. A recent publication of the crystal structure of a murine CD3e-mitogenic antibody complex provides further insight into the action of commonly used agonist antibodies (Fernandes, R.A. et al. 2012. J. Biol. Chem. 287: 13324-13335).