1043 Results for: "Tonbo Biosciences"

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The CD28.6 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. The CD28.6 antibody is reported to have neutralizing activity and is also useful for western blotting.

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Goat anti-Human IgA (alpha chain) - Affinity Pure, FITC Conjugate, min x w/bovine, mouse, and rabbit serum proteins

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The HIT2 antibody is specific for human CD38, a 45 kD type II transmembrane glycoprotein expressed on thymocytes, activated T and B cells, and monocytes as well as other non-hematopoietic cells. CD38 is an ectoenzyme that functions to catalyze the synthesis and hydrolysis of cyclic ADP-ribose and is involved in cell signaling, regulating cell adhesion, and activation. Additionally, CD38 has been shown to be a prognostic marker for some leukemias and other diseases.

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The PIP immunoglobulin is useful as an isotype-matched control. The PIP immunolglobulin is specific for Glutathione S-transferase and can be used as an isotype control for Armenian Hamster IgG antibodies.

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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. The 3.9 antibody is widely used as a marker for CD11c expression on dendritic cells (DC), often in parallel with markers for CD11b, for identification of developmental stages and mature subsets of this cell type. CD11c is prominently expressed on tissue macrophages, and is also detected on activated neutrophils, granulocytes, some types of activated T cells and intestinal intraepithelial lymphocytes (IEL). The antibody is reported to be cross-reactive with Baboon, Chimpanzee, Cynomolgus and Rhesus CD11c.

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The PIP immunoglobulin is useful as an isotype-matched control. The PIP immunolglobulin is specific for Glutathione S-transferase and can be used as an isotype control for Armenian Hamster IgG antibodies.

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The L243 antibody reacts with a member of the human MHC Class II antigens, HLA-DR. The HLA-DR antigen is expressed on B lymphocytes, activated T lymphocytes, activated NK cells, monocytes, macrophages, other antigen presenting cells and progenitor cells. The L243 antibody is specific to an epitope on the alpha subunit of the heterodimeric HLA-DR protein and binds a different epitope than the LN3 antibody clone. It does not cross-react with HLA-DP or HLA-DQ. This antibody is reported to be cross-reactive with non-human primates including Chimpanzee, Cynomolgus, Rhesus and Baboon. Please choose the appropriate format for each application.

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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 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. It is important to review the literature in choosing an antibody for the Foxp3 antigen in flow cytometry, as the potential for high background or non-specific staining may be observed. The 3G3 antibody may be used for intracellular detection of Foxp3 in cells from mouse and Rhesus macaque.

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The EBVCS-5 antibody is specific for human CD23, also known as the low affinity IgE receptor (FceRII), a 45 kDa type II transmembrane protein and member of the immunoglobulin superfamily. It is expressed on most B cells and is upregulated upon activation. It is also present on mantle zone B cells, eosinophils, monocytes and a subset of T cells and platelets. CD23 plays a role in B cell development and differentiation, and also functions to regulate IgE production. Soluble secreted forms of CD23 have been reported to bind IgE, stimulate release of pro-inflammatory cytokines from monocytes, and play a role in B cell differentiation.

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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 61D3 antibody is specific for human CD14, a 53-55 kDa GPI-anchored glycoprotein. CD14 is highly expressed on monocytes and to a lesser extent on interfollicular macrophages, and some dendritic cells. Together with LPS-Binding Protein (LBP), CD14 binds to and mediates the innate immune response to bacterial lipopolysaccharide (LPS).

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Goat anti-Rabbit IgG (H&L) - Affinity Pure, FITC Conjugate, min x w/bovine, human, or mouse IgG

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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). These receptors are expressed by B cells, monocytes, macrophages, NK cells, dendritic cells, and neutrophils.

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The XMG1.2 antibody is specific for mouse Interferon-gamma (IFN-g), a 20 kDa type II cytokine known for its central roles in protection against bacterial or viral pathogens and for its anti-tumor properties. IFN-g is secreted by several types of immune cells, which allow the cytokine to modulate innate immunity, when secreted by NK and NKT cells, and to function in supporting adaptive immunity when secreted by Th1 and CD8+ T cells (CTLs).

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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 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 17A2 antibody reacts with the mouse CD3 complex, comprised of CD3 epsilon, 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 1D3 antibody reacts with mouse CD19, a 95 kDa glycoprotein which acts as a co-receptor, along with CD21 and CD81, 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 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 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 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 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 HP-3G10 antibody is specific for human CD161, also known as NKR-P1A, a type II transmembrane lectin-like receptor and member of the killer cell lectin-like receptor (KLR) family. CD161 exists as a homodimer which is prominently expressed on natural killer (NK) and NKT cells, where it is proposed to regulate the function of both cell types. CD161 is also found on T cell subsets, including T regulatory cells (Tregs), memory/effector CD4+ T cells, and CD8+ T cells. Th17 cells have been demonstrated to co-express CD161, as surface IL-17A+ cells are contained within the CD161+ fraction of CD4 T cells, so that CD161 (in combination with CCR6) is often used as a marker for enrichment of Th17 cells.

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The XMG1.2 antibody is specific for mouse Interferon-gamma (IFN-g), a 20 kDa type II cytokine known for its central roles in protection against bacterial or viral pathogens and for its anti-tumor properties. IFN-g is secreted by several types of immune cells, which allow the cytokine to modulate innate immunity, when secreted by NK and NKT cells, and to function in supporting adaptive immunity when secreted by Th1 and CD8+ T cells (CTLs).

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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 C17.8 antibody is specific for the 40 kDa (p40) protein subunit shared by the cytokines IL-12 and IL-23. To form IL-12, p40 assembles with a separate 35 kDa protein known as p35, resulting in a 70 kDa functional cytokine. IL-12 is secreted by activated monocytes, macrophages, and dendritic cells, and has been shown to target naïve, resting CD4+ T cells to promote their proliferation and secretion of cytokines. IL-23 contains the p40 subunit in combination with a 19 kDa protein chain, p19; its primary source being activated dendritic cells and other antigen-presenting cells. IL-23 appears to target different cell types than IL-12, acting on memory CD4+ T cells to induce a strong proliferative response and contributing to the generation and expansion of Th17 cells. Like the cytokines themselves, the receptors for IL-12 and IL-23 share one subunit, as well as containing distinct cytokine-specific subunits.

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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 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 61D3 antibody is specific for human CD14, a 53-55 kDa GPI-anchored glycoprotein. CD14 is highly expressed on monocytes and to a lesser extent on interfollicular macrophages, and some dendritic cells. Together with LPS-Binding Protein (LBP), CD14 binds to and mediates the innate immune response to bacterial lipopolysaccharide (LPS).