2860 Results for: "Tonbo Biosciences"

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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 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 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 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 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.

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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 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 homodimerisation of CD115 and subsequent tyrosine phosphorylation and ubiquitination of intracellular domains. CD115 signaling 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 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 2.4G2 antibody is specific for a common epitope found in the extracellular regions of mouse Fc-receptors Fc-gamma II (CD32) and Fc-gamma III (CD16). As these are receptors for the Fc portion of mouse IgG, they may also bind laboratory antibody preparations and products used in a variety of cell analysis protocols such as flow cytometry, immunohistochemistry and functional cell assays. The 2.4G2 antibody is therefore widely used as a pre-treatment reagent to block binding of specific antibodies of interest, e.g. fluorescently conjugated antibodies, to Fc receptors via their Fc domains and contributing to “non-specific” staining.

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The M5/114.15.2 antibody reacts with mouse MHC Class II alloantigens I-Ab, I-Ad, I-Aq, I-Ed, and I-Ek, as well as being cross-reactive with mouse cells of H-2p and H-2r haplotype. MHC Class II is widely expressed by mouse immune cells bearing these alloantigens, including T and B cells, monocytes, macrophages and dendritic cells. The antibody does not react with the following alloantigens: I-Af, I-Ak, I-As, or NOD H-2g7.

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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 37.51 antibody reacts with mouse CD28, a 45 kDa glycoprotein which acts as a co-stimulatory receptor in support of the T cell receptor (TCR). CD28 exists as a homodimer with specificity for two known ligands, known as B7-1 (CD80) and B7-2 (CD86), 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. Other members of the CD28 family of co-stimulatory receptors include CTLA-4 (CD152), PD-1 (CD279), ICOS and BTLA.

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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 2.43 antibody reacts with the 32 to 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 induced by 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 and facilitate 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 in tumor cells, as well as in cells infected by virus, bacteria or parasites.

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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 CD 28,2 antibody reacts with human CD28, a 44 kDa type I surface glycoprotein which acts as a co-stimulatory receptor in support of the T cell receptor (TCR). CD28 exists as a homodimer with specificity for two known ligands, known as B7-1 (CD80) and B7-2 (CD86), which 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. Other members of the CD28 family of receptors include CTLA-4 (CD152), PD-1 (CD279), ICOS and BTLA.

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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 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 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 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 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 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 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.

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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 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 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 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.