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 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 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 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 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 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 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 OKT3 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 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 JES6-5H4 antibody binds to mouse Interleukin-2 (IL-2), a 17 kDa cytokine that is secreted by activated T cells. This cytokine acts as an autocrine stimulatory factor for T cell proliferation, differentiation and survival, as well as being an effective activator of B cells and inducer of NK cell cytotoxic functions. IL-2 plays a key modulatory role in the differentiation of T cells toward either Th17 or T regulatory (Treg) cell types and is important for Treg cell function. The IL-2 receptor (IL-2R) is a complex consisting of an IL-2R alpha chain (CD25), along with the IL-2R beta chain (CD122) and the common gamma chain (CD132). IL-2 may also bind with low affinity to the T cell surface protein CD25 alone, although this interaction does not induce cell signaling.

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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 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.

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The ICRF44 antibody reacts with human 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, ICAM-2, ICAM-3 and ICAM-4 on endothelial cells and can also facilitate removal of iC3b bearing foreign 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 UC10-4F10-11 antibody is specific for mouse 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 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 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 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 ICRF44 antibody reacts with human 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, ICAM-2, ICAM-3 and ICAM-4 on endothelial cells and can also facilitate removal of iC3b bearing foreign cells.

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The RM4-5 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 beta2-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 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 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 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.

Supplier: Tonbo Biosciences

The ICRF44 antibody reacts with human 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, ICAM-2, ICAM-3 and ICAM-4 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 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 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 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 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 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.