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Description:
The 2.43 monoclonal antibody specifically reacts with mouse CD8 antigen. CD8a (the alpha chains) form heterodimers with CD8b (the beta chains) or homodimers (alpha-alpha), which occur as receptors on the surface of the majority of thymocytes. A subpopulation of mature T lymphocytes expresses the CD8 alpha beta (alpha beta TCR T cells), and a subpopulation of intestinal intraepithelial lymphocytes and dendritic cells express CD8a without CD8b. CD8 interacts with the mouse major histocompatibility complex class I (MHC class I) molecules on antigen-presenting cells or epithelial cells.
Description:
The 17B7 monoclonal antibody specifically binds to mouse and rat IL-17A, a pro-inflammatory cytokine. It is produced by T helper 17 (Th17) cells, a unique subset of IL-23 dependent CD4+ T cells. Interleukin-17A is highly expressed in transplant rejection, asthma, psoriasis, and multiple sclerosis, and enhances the expression of ICAM-1 in human fibroblasts. The homodimer is expressed by activated peripheral CD4+ T lymphocytes. The Interleukin-17A binds to the IL-17 receptors (IL-17R) expressed by mast cells, monocytes and macrophages, fibroblasts, and endothelial and epithelial cells.
Description:
The 1A8 monoclonal antibody specifically reacts with the 21-25 kDa glycophosphatidylinositol-anchored protein known as Ly-6G, expressed by the granulocytes from the bone marrow and periphery neutrophils. Ly-6G and Ly-6C form the Granulocyte Receptor-1 antigen (GR-1). The binding of the 1A8 antibody to the Ly-6G can be blocked by another antibody, RB6-8C5, which also recognizes Ly-6C. While 1A8 is specific for only Ly-6G, RB6-8C5 also binds to Ly-6C.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
The ACK2 monoclonal antibody specifically reacts with mouse CD117 (c-Kit receptor), a 145 kDa transmembrane tyrosine-kinase receptor encoded by the Kit gene. The c-Kit receptor, also known as stem cell factor receptor, is expressed on hematopoietic progenitor cells in adult bone marrow, in progenitors of erythroid and myeloid lineages, and precursors of B and T cells. CD117 enhances the proliferation and the differentiation of the hematopoietic progenitor cells and seems to enhance the development of T cells, as the c-Kit receptor and its ligand are expressed by the thymus.
Description:
The 30-H12 monoclonal antibody specifically binds to MouseCD90.2, an alloantigen known as Thy-1.2, expressed on thymocytes, mature T cells, epithelial cells, neurons, hematopoietic stem cells, and fibroblasts. CD90 is a membrane glycoprotein that regulates the adhesion and signal transduction in T lymphocytes, and the adhesion of thymocytes to thymic stroma.The interaction between 30-H12 and the antibody to the CD3/TCR complex upregulates thymocytes signal transduction and apoptosis and downregulates mature T cell proliferation. The 30-H12 antibody seems to be unable to cross-link with CD90.1.
Description:
The 1A8 monoclonal antibody specifically reacts with the 21-25 kDa glycophosphatidylinositol-anchored protein known as Ly-6G, expressed by the granulocytes from the bone marrow and periphery neutrophils. Ly-6G and Ly-6C form the Granulocyte Receptor-1 antigen (GR-1). The binding of the 1A8 antibody to the Ly-6G can be blocked by another antibody, RB6-8C5, which also recognizes Ly-6C. While 1A8 is specific for only Ly-6G, RB6-8C5 also binds to Ly-6C.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
Description:
Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.
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