1056 Results for: "Tonbo Biosciences"

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The PK136 antibody is specific for mouse NK1.1, a type II transmembrane lectin-like receptor and member of the killer cell lectin-like receptor (KLR) family. NK1.1 is prominently expressed on natural killer (NK) cells, and is correlated with NK cytotoxic effects toward virus-infected cells and tumor cells. NK1.1 is expressed on subsets of NKT cells in certain mouse strains (C57BL/6, FVB/N, and NZB), yet absent from others (AKR, BALB/c, CBA/J, C3H, DBA/1, DBA/2, NOD, SJL, and 129). Putative subsets of NK cells and their expression of NK1.1 antigen are of continuing interest, including NK1.1+/CD117+ (c-Kit) cells reported to be immunosuppressive for CD8+ T cells in a mechanism involving PD-1 and PD-L1 (Ehlers et al. 2012. Endocrinology. 10: 1247).

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The RPA-T8 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 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 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 2H7 antibody reacts with human CD20, expressed by pre-B cells, resting and activated B cells, follicular dendritic cells and a small subset of T cells, but not on plasma cells. CD20 is a 33-37 kDa transmembrane protein which is differentially phosphorylated in resting and active B cells. The CD20 molecule plays a role in regulating B-cell activation.

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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 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 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 (dimerization) 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. The ACK2 antibody is widely utilized as a marker to identify hematopoietic progenitors, and to neutralize receptor-ligand binding in vitro and in vivo. Please choose the appropriate format for each application. In addition, the antibody is reported to be cross-reactive with rat c-Kit and is extensively published for use in this species.

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Lymphocyte Separation Medium (LSM) is a sterile-filtered iso-osmotic solution designed for the in vitro isolation of lymphocytes from diluted whole blood

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Ghost Dye™ UV 450 is an amine reactive viability dye that can be used to discriminate viable from non-viable mammalian cells in flow cytometry applications

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The 2H7 antibody reacts with human CD20, expressed by pre-B cells, resting and activated B cells, follicular dendritic cells and a small subset of T cells, but not on plasma cells. CD20 is a 33-37 kDa transmembrane protein which is differentially phosphorylated in resting and active B cells. The CD20 molecule plays a role in regulating B-cell activation.

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The SK3 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. The SK3 antibody is widely used as a phenotypic marker for human CD4 expression, and has been reported to be cross-reactive with Rhesus and Cynomolgus CD4. This antibody does not block binding of alternative clone RPA-T4, suggesting that they recognize different epitopes.

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The RM2-5 antibody reacts with mouse CD2, an approximately 50 kDa glycoprotein, and a member of the Ig superfamily. CD2, also known as LFA-2, is a receptor for CD48 in the mouse and is expressed on the cell surface of all mouse lymphocytes. CD2 mediates adhesion between cells and is involved in T cell activation.

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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 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 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 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 H57-597 antibody is specific for the beta chain of the mouse T cell Receptor (TCR). This cell surface protein combines with a second protein chain (alpha chain) to form the alpha-beta TCR that is expressed by NK1.1+ thymocytes, NKT cells, and the majority of peripheral T cells. A small number of T cells may express an alternative heteromer of gamma/delta protein chains, known as the g/d TCR. These receptors participate in a complex with CD3, and with the co-receptors CD4 or CD8, to recognize and respond to 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.

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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 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 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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RBC Lysis Buffer (10X) is a concentrated ammonium chloride-based lysing reagent

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Propidium Iodide (PI) is a membrane-impermeant DNA binding dye that cannot penetrate viable cells. PI rapidly enters cells with compromised membranes and intercalates between base pairs allowing exclusion of non-viable cells from analysis of flow cytometry data. PI has a broad emission spectrum from 535-617 nm and can be detected in either FL2 or FL3 detectors. When used with Annexin V FITC, it is recommended to analyze PI in FL2.

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The H57-597 antibody is specific for the beta chain of the mouse T cell Receptor (TCR). This cell surface protein combines with a second protein chain (alpha chain) to form the alpha-beta TCR that is expressed by NK1.1+ thymocytes, NKT cells, and the majority of peripheral T cells. A small number of T cells may express an alternative heteromer of gamma/delta protein chains, known as the g/d TCR. These receptors participate in a complex with CD3, and with the co-receptors CD4 or CD8, to recognize and respond to 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.

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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 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 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 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 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.