2860 Results for: "Tonbo Biosciences"

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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.

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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 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 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 2A3 immunoglobulin is useful as an isotype-matched control. The 2A3 immunolglobulin has an unknown binding specificity and is used as an isotype control for rat IgG2a antibodies.

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The 15.2 antibody reacts with human CD54, also known as ICAM-1 (Intercellular Adhesion Molecule 1), a 90 to 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 HIB19 antibody reacts with human CD19, a 95 kDa glycoprotein which acts as a co-receptor, along with CD21, CD81 and CD225, 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 LTF-2 immunoglobulin is useful as an isotype-matched control. The LTF-2 immunolglobulin has an unknown binding specificity and is used as an isotype control for rat IgG2b antibodies.

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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 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 10F.9G2 antibody is specific for mouse CD274, more commonly known as PD-L1 or B7-H1, which acts as a ligand for the T cell co-regulatory receptor PD-1 (CD279). This interaction modulates T cell antigen receptor (TCR) signaling and therefore T cell activation. PD-L1 binding to PD-1 expressed on CD4- CD8- thymocytes participates in the processes of clonal selection, elimination of autoreactive lymphocytes, and development of tolerance. PD-L1 may also bind PD-1 following the receptor’s inducible expression on activated, mature T cells, where it has been proposed to limit T cell activation. PD-L1 is one of a group of “B7” ligands whose interactions with the CD28 receptor family, also including CTLA-4 (CD152), provide a balance of co-stimulatory /co-inhibitory signaling important in T cell activation, tolerance, and autoimmunity.

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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 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 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 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.

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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 HIB19 antibody reacts with human CD19, a 95 kDa glycoprotein which acts as a co-receptor, along with CD21, CD81 and CD225, 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 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 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 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 OKT8 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 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 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 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 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 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 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 M1/69 antibody reacts with mouse CD24, a cell surface molecule also known as Heat Stable Antigen (HSA). CD24 is a GPI-linked glycoprotein involved in cell adhesion and is a ligand for CD62P (P-selectin). It is expressed on erthrocytes, thymocytes, peripheral lymphocytes and myeloid lineage cells. The expression of CD24 is used to delineate stages of of lymphocyte development in the bone marrow.

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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. The GK1.5 antibody is widely used as a phenotypic marker for CD4 expression. If used together, the GK1.5 antibody and an alternative antibody, Anti-Mouse CD4 clone RM4-5, will "compete" for binding, i.e. RM4-5 is able to block GK1.5 binding to cells. In contrast, the Anti-Mouse CD4 clone RM4-4 does not block binding of the GK1.5 antibody to cells (Arora S et al. 2006. Infect. Immun. 74: 4339-4348). The GK1.5 antibody is also reported to be cross-reactive with Syrian hamster CD4.

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The GL-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. The GL-1 antibody may be used as a marker for CD86 expression on B cells, macrophages, and dendritic cells.