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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 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 TER-119 antibody is named for the antigen to which it binds, a 52 kDa surface protein that is associated with glycophorin-A. TER-119 is considered to be a lineage marker for later stages of erythroid cell development, as its expression begins at the pro-erythroblast stage. TER-119 antigen is not expressed at either BFU-E or CFU-E stages, i.e. prior to the pro-erythroblast stage.

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The MOPC-21 immunoglobulin is useful as an isotype-matched control. The MOPC-21 immunolglobulin has an unknown binding specificity and is used as an isotype control for mouse IgG1 antibodies.

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The C17.8 antibody is specific for the 40 kDa (p40) protein subunit shared by the cytokines IL-12 and IL-23. To form IL-12, p40 assembles with a separate 35 kDa protein known as p35, resulting in a 70 kDa functional cytokine. IL-12 is secreted by activated monocytes, macrophages, and dendritic cells, and has been shown to target naïve, resting CD4+ T cells to promote their proliferation and secretion of cytokines. IL-23 contains the p40 subunit in combination with a 19 kDa protein chain, p19; its primary source being activated dendritic cells and other antigen-presenting cells. IL-23 appears to target different cell types than IL-12, acting on memory CD4+ T cells to induce a strong proliferative response and contributing to the generation and expansion of Th17 cells. Like the cytokines themselves, the receptors for IL-12 and IL-23 share one subunit, as well as containing distinct cytokine-specific subunits.

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The GARP5 antibody reacts with human GARP, also known as LRRC32 or Garpin, an 80 kDa transmembrane protein which acts as a receptor for the latent form of TGF-beta 1 (pro-TGF-beta), preventing its secretion. Specifically, GARP is reported to associate with the pro-domain of TGF-beta 1, known as latency-associated peptide (LAP), which must be cleaved to release the biologically active cytokine. The putative role of GARP in sequestering the TGF-beta is important for regulating its activity, as TGF-beta signaling is involved in development and function of Th17, Treg and many other immune cell types. GARP expression has been shown on platelets and at high levels on Foxp3+ Treg cells, where it is proposed to be a phenotypic identifier for activated human Treg cells.

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The PO3.1 antibody reacts with mouse CD86, also known as B7-2, an 80 kDa cell surface protein which is a ligand for CD28, a co-stimulatory receptor for the T cell receptor (TCR). CD28 can also bind a second B7 ligand known as CD80 (B7-1). 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 provides crucial communication between T cells and B cells or APCs to coordinate the adaptive immune response.

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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 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 SK1 antibody is specific for the 32 to 34 kDa alpha chain of human 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 for 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 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 SK7 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 OKT3 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 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 HI100 antibody reacts with the human CD45 isoform known as CD45RA, 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. With their broad cell distribution, CD45 isoforms are 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), CD45RB, CD45RO and others.

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The ACK2 antibody is specific for CD117, also called c-Kit, a 145 kDa cytokine receptor important in the development of hematopoietic stem cells, in oogenesis, and for functional activity of immune cells such as NK and mast cells. c-Kit binds to a ligand known as stem cell factor (SCF), or alternatively as mast cell growth factor. Ligand binding promotes the activation (dimerisation) and subsequent tyrosine kinase activity of the c-Kit receptor and triggers key survival, expansion and maturation signals during hematopoietic progenitor cell development. Conversely, shedding of extracellular domain of c-Kit receptor is reported to induce inactivation or apoptosis within these cells. The survival signaling activity of c-Kit confers a proto-oncogenic attribute to the receptor, as overexpression or mutations in this protein are associated with tumor development.

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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 BM8.1 antibody is specific for mouse F4/80 antigen, a 125 kDa transmembrane protein widely expressed by members of the mononuclear phagocyte system and considered to be a key marker for mature macrophage cells. F4/80 is differentially expressed during myeloid cell development, and may be regulated by certain cytokines within the tissue microenvironment. Other cell types shown to express this antigen include Langerhans cells, Kupffer cells and dendritic cell subsets. BM8.1 is widely used together with antibodies to CD115 (c-fms), CD11b and CD11c to identify myeloid / macrophage cells by flow cytometry.

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The DTA-1 antibody reacts with mouse CD357, also known as GITR or AITR (in humans), a 66-70 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 RPA-T4 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.

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The RPA-T4 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.

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The A20 antibody reacts with mouse CD 45.1, 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 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 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.

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The MPC-11 immunoglobulin is useful as an isotype-matched control. The MPC-11 immunolglobulin has an unknown binding specificity and is used as an isotype control for mouse IgG2b antibodies.

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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 J43.1 antibody is specific for mouse CD279, also known as programmed death-1 (PD-1), a 55 kDa glycoprotein which can co-regulate T cell antigen receptor signaling and therefore modulate T cell activation. PD-1 exists in a monomeric form that is expressed by CD4- CD8- thymocytes, where it participates in the processes of clonal selection, elimination of autoreactive lymphocytes, and development of tolerance. PD-1 expression is also inducible upon activation of mature T cells, where it has been proposed to interact with the co-stimulatory receptor CD80 to limit T cell activation. Two ligands for PD-1, known as PD-L1 (B7-H1) and PD-L2 (B7-DC) are differentially expressed on T and B cells, monocytes, macrophages, NK cells or dendritic cells. PD-1 is a member of a family of receptors including CD28 and CTLA-4 (CD152), which interact with 'B7' ligands to provide a balance of co-stimulatory /co-inhibitory signaling important in T cell activation, tolerance, and autoimmunity.

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The TER-119 antibody is named for the antigen to which it binds, a 52 kDa surface protein that is associated with glycophorin-A. TER-119 is considered to be a lineage marker for later stages of erythroid cell development, as its expression begins at the pro-erythroblast stage. TER-119 antigen is not expressed at either BFU-E or CFU-E stages, i.e. prior to the pro-erythroblast stage.

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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.

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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 PIP immunoglobulin is useful as an isotype-matched control. The PIP immunolglobulin is specific for Glutathione S-transferase and can be used as an isotype control for Armenian Hamster IgG antibodies.