1043 Résultats pour : « Tonbo Biosciences »

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Goat anti-Mouse IgG2b, secondary antibody, conjugated to SureLight® R-Phycoerythrin

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Goat anti-Rabbit IgG (H&L) - Affinity Pure, FITC Conjugate

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The 2D1 antibody reacts with human CD45, one of the most abundant hematopoietic markers and one that 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. The 2D1 antibody is widely used as a marker for human CD45 expression on peripheral blood T cells, B cells, monocytes, macrophages, and NK cells.

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The HRPN immunoglobulin is useful as an isotype-matched control. The HRPN immunolglobulin has an unknown binding specificity and is used as an isotype control for rat IgG1 antibodies.

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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 HIB19 antibody reacts with human CD19, a 95 kDa glycoprotein which acts as a co-receptor, along with CD21, CD81 and CD225, 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.

The HIB19 antibody is widely used as a phenotypic marker for CD19 expression on B cells, as well as on dendritic cell subsets.

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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 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 MY31 antibody reacts with human CD56, also known as the neural cell adhesion molecule (NCAM), a glycoprotein which is a member of the immunoglobulin superfamily. The 140 kDa isoform of CD56 is expressed on human NK cells and NK-T cells, with increased expression levels on activated NK lymphocytes. The CD56 antigen is also expressed by neurons and is reported to play a role in nervous system development and neural cell-to-cell adhesion.

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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 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 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 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 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 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.

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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 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.

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The HRPN immunoglobulin is useful as an isotype-matched control. The HRPN immunolglobulin has an unknown binding specificity and is used as an isotype control for rat IgG1 antibodies.

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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 HI30 antibody reacts with human CD45, one of the most abundant hematopoietic markers and one that 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, CD45RO and others.

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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 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 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 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 Mouse Dendritic Cell backbone panel is a six-color combination of anti-mouse antibodies. This panel can serve as a backbone for identifying major dendritic cell (DC) subsets. Hosts: Rat, Armenian Hamster

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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 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 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 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 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.