2860 Results for: "Tonbo Biosciences"

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The J43.1 antibody is specific for mouse CD279, also known as programmed death-1 (PD-1), a 55 kDa glycoprotein which can co-regulate T cell antigen receptor signaling and therefore modulate T cell activation. PD-1 exists in a monomeric form that is expressed by CD4- CD8- thymocytes, where it participates in the processes of clonal selection, elimination of autoreactive lymphocytes, and development of tolerance. PD-1 expression is also inducible upon activation of mature T cells, where it has been proposed to interact with the co-stimulatory receptor CD80 to limit T cell activation. Two ligands for PD-1, known as PD-L1 (B7-H1) and PD-L2 (B7-DC) are differentially expressed on T and B cells, monocytes, macrophages, NK cells or dendritic cells. PD-1 is a member of a family of receptors including CD28 and CTLA-4 (CD152), which interact with 'B7' ligands to provide a balance of co-stimulatory/co-inhibitory signaling important in T cell activation, tolerance, and autoimmunity.

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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 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 MEL-14 antibody is specific for mouse CD62L, also known as L-Selectin, a cell adhesion molecule which facilitates lymphocyte “rolling” on activated vascular endothelium and homing to high endothelial venules (HEV) as immune cells transmigrate from blood into peripheral tissues. L-Selectin is a member of a family of Selectin molecules which act together with the integrin family of adhesion molecules to mediate leukocyte-endothelial interactions. L-Selectin is characteristically expressed by neutrophils, and is also found on B cells, monocytes, granulocytes, and at varying levels on naive, effector and memory T cells. It is rapidly shed upon cell activation, releasing into the circulation a soluble form whose biological role is of particular interest in cancer biology research.

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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 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 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 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 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 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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Anti-Ly-6G Rat Monoclonal Antibody (PE (Phycoerythrin)/Cy7®) [clone: RB6-8C5]

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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 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 and CD45RO.

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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 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 UCHL1 antibody reacts with the human CD45 isoform known as CD45RO, 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), CD45RA and CD45RB.

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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 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 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 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 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 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 3G3 antibody reacts with mouse Foxp3, a 50-55 kDa transcription factor which is a central regulator of T cell activity and is critical for the development and function of regulatory T cells (Tregs). Foxp3 is expressed at constitutively high levels in Treg cells, which are further identified as being CD4+ CD25+. In resting conventional T cells (CD4+ CD25-) Foxp3 expression is restricted, and upon TCR activation is expressed only transiently and in a small proportion of cells. However, the growth factor TGF-beta has been shown to induce expression of Foxp3 in naïve T cells, driving their development into Foxp3+ Tregs, which are called “induced” or “adaptive” Tregs. These cells are phenotypically similar to so-called “natural” Tregs (CD4+ CD25high Foxp3+) which originate in the thymus and comprise the majority of Treg cells. Tregs are critical for maintaining peripheral tolerance and are implicated in the development of autoimmunity.

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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 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 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 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 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 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.