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The C1.18.4 immunoglobulin is useful as an isotype-matched control. The C.1.18.4 immunolglobulin has an unknown binding specificity and is used as an isotype control for mouse IgG2a antibodies.

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The AFS98 antibody is specific for mouse CD115, also known as Colony-Stimulating Factor-1 Receptor (CSF-1R), a 145 kDa receptor from the PDGF receptor family. Receptor activation by the ligands IL-34 or CSF-1 (M-CSF) occurs via homodimerization of CD115 and subsequent tyrosine phosphorylation and ubiquitination of intracellular domains. CD115 signalling promotes differentiation of myeloid precursors, as well as the continued regulation of proliferation, survival and function of mononuclear phagocytes, dendritic cells and osteoclasts. While IL-34 and CSF-1 may induce similar cellular responses, they are differentially expressed and as such exert complimentary actions via CD115.

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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 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 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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Anti-PTPRC Rat Antibody (APC (Allophycocyanin)-Cy7®) [clone: LTF-2]

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The RM4-5 antibody reacts with mouse CD4, a 55 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 beta2-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 is typically expressed on thymocytes, certain mature T cell populations such as Th17 and T regulatory (Treg) cells, as well as on dendritic cells. The RM4-5 antibody is widely used as a phenotypic marker for CD4 expression. If used together, the RM4-5 antibody and an alternative antibody, Anti-Mouse CD4 clone GK1.5, will compete for binding, i.e. RM4-5 antibody is able to block GK1.5 antibody binding to cells. In contrast, RM4-5 antibody does not block the binding of Anti-Mouse CD4 clone RM4-4 to cells.

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Goat anti-Rabbit IgG (H&L) - Affinity Pure, Alkaline Phosphatase Conjugate

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Donkey anti-Mouse IgG (H&L) - Affinity Pure, HRP Conjugate

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Goat anti-Rat IgG (H&L) - Affinity Pure, HRP Conjugate

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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 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 N418 antibody reacts with mouse 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 complex 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 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 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 HRPN immunoglobulin is useful as an isotype-matched control. The HRPN immunolglobulin has an unknown binding specificity and is used as an isotype control for rat IgG1 antibodies.

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The DTA-1 antibody reacts with mouse CD357, also known as GITR or AITR (in humans), a 66 to 70 kDa member of the Tumor Necrosis Factor superfamily (TNFRSF18). GITR is primarily found on T cells, and its function may vary depending on the T cell type where it is expressed. GITR is upregulated on activated T cells where it provides co-stimulation, yet GITR may promote the inhibition of CD4+ CD25+ Treg cells, where it is expressed at high levels. GITR ligand (GITRL) is found on B cells, macrophages, dendritic and endothelial cells, and is implicated in regulating both innate and adaptive immune responses.

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The C1.18.4 immunoglobulin is useful as an isotype-matched control. The C.1.18.4 immunolglobulin has an unknown binding specificity and is used as an isotype control for mouse IgG2a antibodies.

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The 1A8 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 1D3 antibody reacts with mouse CD19, a 95 kDa glycoprotein which acts as a co-receptor, along with CD21 and CD81, in support of the functional B cell receptor (BCR). This complex provides antigen-specific recognition and subsequent activation of B cells to proliferate and differentiate into antibody-secreting cells (plasma cells) or memory B cells, which are crucial for secondary antigen encounter. CD19 is a lineage-differentiation marker, as its expression is detectable at the earliest B cell stages, through development, and is finally lost upon transition to mature plasma cells.

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The A7R34 antibody is specific for mouse CD127, a 60-90 kDa cell surface protein also known as the Interleukin-7 Receptor alpha chain, or IL-7R alpha. CD127 is typically expressed at the cell surface as a heterodimer with the common gamma chain (CD132). This complex acts as the functional receptor for IL-7, a cytokine important in T and B cell development, and in mature T cell homeostasis. A second cytokine known as Thymic Stromal Lymphopoietin (TSLP) also binds to a receptor complex of CD127 and the TSLPR chain to trigger activation of dendritic cells, and is involved in B cell development, allergy and autoimmunity.

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The A7R34 antibody is specific for mouse CD127, a 60-90 kDa cell surface protein also known as the Interleukin-7 Receptor alpha chain, or IL-7R alpha. CD127 is typically expressed at the cell surface as a heterodimer with the common gamma chain (CD132). This complex acts as the functional receptor for IL-7, a cytokine important in T and B cell development, and in mature T cell homeostasis. A second cytokine known as Thymic Stromal Lymphopoietin (TSLP) also binds to a receptor complex of CD127 and the TSLPR chain to trigger activation of dendritic cells, and is involved in B cell development, allergy and autoimmunity.

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The M1/70 antibody reacts with human and mouse CD11b, also known as integrin alpha M. This 165-170 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 M (CD11b) assembles with Integrin beta-2 (CD18) into a receptor known as Macrophage Antigen-1 (Mac-1) or complement receptor type 3 (CR3). This receptor binds and induces intracellular signaling through ICAM-1 on endothelial cells and can also facilitate removal of iC3b bearing foreign cells.

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The 2F1 antibody reacts with mouse KLRG1 (Killer cell Lectin-like Receptor G1). This 30-38 kDa homodimeric receptor may be expressed by activated, mature NK cells and by effector/memory T cells, with potentially different roles in each cell type. KLRG1 can regulate, in an inhibitory fashion, the development and effector functions of NK cells, and is often cited as a senescence or terminal differentiation marker for T cells. Ligands for KLRG1 include members of the cadherin family of adhesion molecules, specifically N-Cadherin, E-Cadherin, and R-Cadherin. These interactions may induce bidirectional, immunosuppressive signaling in both KLRG- and Cadherin-expressing cells. A more recently identified role for KLRG1-Cadherin signaling in tissue organization, e.g. in cardiac angiogenesis, expands the function of these interactions beyond immunosuppression of immune cells. (Bouchentouf et al. 2010. J. Immunol. 185: 7014-7025).

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The XMG1.2 antibody is specific for mouse Interferon-gamma (IFN-g), a 20 kDa type II cytokine known for its central roles in protection against bacterial or viral pathogens and for its anti-tumor properties. IFN-g is secreted by several types of immune cells, which allow the cytokine to modulate innate immunity, when secreted by NK and NKT cells, and to function in supporting adaptive immunity when secreted by Th1 and CD8+ T cells (CTLs).

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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 GK1.5 antibody reacts with mouse CD4, a 55 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 is typically expressed on thymocytes, certain mature T cell populations such as Th17 and T regulatory (Treg) cells, as well as on dendritic cells

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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 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 MAR-1 antibody reacts with the Fc epsilon Receptor I alpha chain (FceRIa), a transmembrane protein member of the Ig superfamily. This chain, together with a beta chain and two gamma chains form a tetrameric complex that supports IgE-mediated signaling and subsequent release of chemical mediators of allergy and immediate hypersensitivity. FceR1a is upregulated in the presence of IgE on those cell types which express it, such as Mast cells and Basophils.