1056 Results for: "Tonbo Biosciences"

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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 BC96 antibody is specific for human 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. Signaling via CD25 may modulate Th17 and Treg cell differentiation, and has been shown to play a role in the function of dendritic cells.

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The Hit3a 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 ICRF44 antibody reacts with human 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, ICAM-2, ICAM-3 and ICAM-4 on endothelial cells and can also facilitate removal of iC3b bearing foreign cells.

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The NOK-1 antibody reacts with human CD178 (Fas ligand) in both membrane bound and soluble forms. Fas ligand is a 40 kDa transmembrane glycoprotein, a member of the TNF family, and is expressed by activated T and NK cells, neutrophils, and monocytes. Interactions between CD178 (Fas ligand) and CD95 (Fas) induce a program of apoptosis and play a key role in immune regulation and homeostasis. The extracellular domain of human CD178 can be cleaved from the surface by matrix metalloproteinases (MMPs) resulting in a 26 kDa soluble protein.

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The OKT4 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 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 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 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 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 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 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 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 104 antibody reacts with mouse CD45.2, also known as Ly5.2, 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 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 104 antibody reacts with mouse CD45.2, also known as Ly5.2, 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 SK1 antibody is specific for the 32-34 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 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 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 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 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 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 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 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 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 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 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 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 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 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 DATK32 antibody is specific for a combinatorial epitope of the mouse integrin alpha 4/beta 7 (LPAM-1) heterodimer. LPAM-1 is expressed on most mature lymphocytes and sub-populations of thymocytes and bone marrow cells. It is involved in lymphocyte adhesion and migration and is a receptor for several extracellular matrix proteins including VCAM-1, fibronectin, and MAdCAM-1.