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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 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 MF23 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 a member of the forkhead box or winged helix family of transcription factors and is expressed at constitutively high levels in Treg cells. Forced expression of Foxp3 in conventional T cells results in the upregulation of Treg associated molecules such as CD25, CTLA-4, and GITR and is sufficient to impart suppressive functional activity to these cells.

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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 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 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 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 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 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 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 SK7 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 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.

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The C1.18.4 immunoglobulin is useful as an isotype-matched control. The C.1.18.4 immunolglobulin has an unknown binding specificity and is used as an isotype control for mouse IgG2a antibodies.

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The 145-2C11 antibody is specific for mouse 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. 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 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 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 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 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 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 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-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 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 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 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 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 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 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.