1056 Results for: "Tonbo Biosciences"

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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 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 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. 

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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 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 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 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 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 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 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 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 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 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 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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Anti-FASLG Mouse Antibody (Biotin) [clone: NOK-1]

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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 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 CD28.2 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 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 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 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 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 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 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 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 2.43 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 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 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 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 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 MP4-25D2 antibody is specific for human IL-4, a pleiotropic cytokine that Th2 cell differentiation, B cell proliferation and differentiation, and B cell class switching to IgE. MP4-25D2 is a neutralizing antibody and is reported to cross react with rhesus monkey IL-4.