2860 Results for: "Tonbo Biosciences"

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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 BNI3 antibody is specific for human CD152, commonly known as CTLA-4, a 33-37 kDa protein expressed as a homodimer on the surface of activated T and B cells, and on thymocytes. CTLA-4 is structurally similar, yet functionally disparate, to the T cell co-stimulatory molecule CD28. Both CTLA-4 and CD28 interact with the co-stimulatory molecules CD80 (B7-1) and CD86 (B7-2) on antigen-presenting cells, with CTLA-4 displaying a higher avidity than CD28. While CD28 typically delivers a potent co-stimulatory signal in support of T cell activation, CTLA-4 appears to act as a negative regulator of T cell activation and may contribute to the suppressor function of Treg 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 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 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 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 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 IM7 antibody recognises CD44, a ubiquitously expressed cell surface receptor which is important for extracellular matrix organisation, 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 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 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 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 TER-119 antibody is named for the antigen to which it binds, a 52 kDa surface protein that is associated with glycophorin-A. TER-119 is considered to be a lineage marker for later stages of erythroid cell development, as its expression begins at the pro-erythroblast stage. TER-119 antigen is not expressed at either BFU-E or CFU-E stages, i.e. prior to the pro-erythroblast stage.

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The 11B11 antibody binds to mouse Interleukin-4 (IL-4), a 14 kDa cytokine that is largely secreted by activated T cells of the Th2 subset, and to some degree by NKT and mast cells. This cytokine acts as a stimulatory factor for B cells, inducing their proliferation and differentiation, as well as playing a role in immunoglobulin class-switching. IL-4 may also provide autocrine stimulation for T cells, and affect the function of antigen presenting cells such as macrophages and dendritic cells. IL-4 can bind and signal via three cell surface receptor types: CD124 by itself, CD124 in combination with the common gamma chain (type I complex), or CD124 combined with CD213a1 (type II complex).

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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 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 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 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 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 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 30-H12 antibody reacts with mouse CD90.2 (Thy1.2). CD90.2 is a strain-specific allelic form of the GPI-linked membrane associated protein CD90 and is involved in adhesion and signal transduction. CD90.2 is expressed on thymocytes, mature T cells and neurons in mouse strains that express the CD90.2 allele (BALB/c, CBA, C3H, C57BL/6, SJL and others). 30-H12 does not react with the CD90.1 allele expressed in mouse strains such as PL and AKR.

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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 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 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 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 UCHT2 antibody is specific for human CD5, a 67 kD transmembrane glycoprotein, that is expressed on most thymocytes, mature T cells, and a subset of B cells. CD5 is involved in modulating antigen receptor signalling in both T and B cells and binds to CD72, expressed on B 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. The PC61,5 antibody is used as a marker for T cells, B cells and dendritic cell subsets. Expression of CD25, CD4 and the transcription factor Foxp3 is regarded as a phenotypic signature for Treg cells. As such, this antibody is widely used to distinguish Treg cells from na�ve or conventional T cells which are CD25-. This clone has also been reported for depletion of Treg cells in vivo (use format suitable for functional assays).

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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 lymphocytes. CD2 mediates cell to cell adhesion and is involved in T cell activation.

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Goat anti-Mouse IgG (H&L), F(ab')2 Fragment - Affinity Pure, FITC Conjugate

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Goat anti-Mouse IgM (H&L) - Affinity Pure, FITC Conjugate