Recombinant antibody

Clone REA299 recognizes the mouse CD150 antigen, a 75-95 kD single-pass type I membrane protein also known as signaling lymphocyte activation molecule (SLAM). CD150 belongs to the immunoglobulin superfamily and acts as a self ligand. Expression of CD150 is found on B cells, dendritic cells and activated/memory T cells. It is involved in functions such as stimulation, proliferation and inhibition of apoptosis of B cells, stimulation and IFN-γ production in Th1 T-cell clones and recently it has been identified as the second receptor for measles virus. In combination with CD48 and CD244, CD150 is a useful marker for hematopoietic stem cell studies.

Additional information: Clone REA299 displays negligible binding to Fc receptors.

Clone REA309 recognizes the human CD156c antigen, a single-pass type I membrane protein which is also known as disintegrin or metalloproteinase domain-containing protein 10 (ADAM10). CD156c belongs to the family of disintegrin and metalloproteinases (ADAMs) and is expressed ubiquitously on hematopoietic and non-hematopoietic cells. ADAMs have emerged as the major proteinase family that mediates proteolytic ectodomain release, a process known as shedding. This shedding process has been recognised as a key mechanism for regulating the function of a diversity of cell surface proteins. Dysregulation of ectodomain shedding is associated with autoimmune and cardiovascular diseases, neurodegeneration, infection, inflammation, and cancer. CD156c has been studied in the context of ectodomain shedding and has been demonstrated as key molecule in most of the shedding events in cancer and neurodegenerative disorders.

Additional information: Clone REA309 displays negligible binding to Fc receptors.

 

Clone REA309 recognizes the human CD156c antigen, a single-pass type I membrane protein which is also known as disintegrin or metalloproteinase domain-containing protein 10 (ADAM10). CD156c belongs to the family of disintegrin and metalloproteinases (ADAMs) and is expressed ubiquitously on hematopoietic and non-hematopoietic cells. ADAMs have emerged as the major proteinase family that mediates proteolytic ectodomain release, a process known as shedding. This shedding process has been recognised as a key mechanism for regulating the function of a diversity of cell surface proteins. Dysregulation of ectodomain shedding is associated with autoimmune and cardiovascular diseases, neurodegeneration, infection, inflammation, and cancer. CD156c has been studied in the context of ectodomain shedding and has been demonstrated as key molecule in most of the shedding events in cancer and neurodegenerative disorders.

Additional information: Clone REA309 displays negligible binding to Fc receptors.

 

Clone REA309 recognizes the human CD156c antigen, a single-pass type I membrane protein which is also known as disintegrin or metalloproteinase domain-containing protein 10 (ADAM10). CD156c belongs to the family of disintegrin and metalloproteinases (ADAMs) and is expressed ubiquitously on hematopoietic and non-hematopoietic cells. ADAMs have emerged as the major proteinase family that mediates proteolytic ectodomain release, a process known as shedding. This shedding process has been recognised as a key mechanism for regulating the function of a diversity of cell surface proteins. Dysregulation of ectodomain shedding is associated with autoimmune and cardiovascular diseases, neurodegeneration, infection, inflammation, and cancer. CD156c has been studied in the context of ectodomain shedding and has been demonstrated as key molecule in most of the shedding events in cancer and neurodegenerative disorders.

Additional information: Clone REA309 displays negligible binding to Fc receptors.

 

Clone REA309 recognizes the human CD156c antigen, a single-pass type I membrane protein which is also known as disintegrin or metalloproteinase domain-containing protein 10 (ADAM10). CD156c belongs to the family of disintegrin and metalloproteinases (ADAMs) and is expressed ubiquitously on hematopoietic and non-hematopoietic cells. ADAMs have emerged as the major proteinase family that mediates proteolytic ectodomain release, a process known as shedding. This shedding process has been recognised as a key mechanism for regulating the function of a diversity of cell surface proteins. Dysregulation of ectodomain shedding is associated with autoimmune and cardiovascular diseases, neurodegeneration, infection, inflammation, and cancer. CD156c has been studied in the context of ectodomain shedding and has been demonstrated as key molecule in most of the shedding events in cancer and neurodegenerative disorders.

Additional information: Clone REA309 displays negligible binding to Fc receptors.

 

Clone REA309 recognizes the human CD156c antigen, a single-pass type I membrane protein which is also known as disintegrin or metalloproteinase domain-containing protein 10 (ADAM10). CD156c belongs to the family of disintegrin and metalloproteinases (ADAMs) and is expressed ubiquitously on hematopoietic and non-hematopoietic cells. ADAMs have emerged as the major proteinase family that mediates proteolytic ectodomain release, a process known as shedding. This shedding process has been recognised as a key mechanism for regulating the function of a diversity of cell surface proteins. Dysregulation of ectodomain shedding is associated with autoimmune and cardiovascular diseases, neurodegeneration, infection, inflammation, and cancer. CD156c has been studied in the context of ectodomain shedding and has been demonstrated as key molecule in most of the shedding events in cancer and neurodegenerative disorders.

Additional information: Clone REA309 displays negligible binding to Fc receptors.

 

Clone REA309 recognizes the human CD156c antigen, a single-pass type I membrane protein which is also known as disintegrin or metalloproteinase domain-containing protein 10 (ADAM10). CD156c belongs to the family of disintegrin and metalloproteinases (ADAMs) and is expressed ubiquitously on hematopoietic and non-hematopoietic cells. ADAMs have emerged as the major proteinase family that mediates proteolytic ectodomain release, a process known as shedding. This shedding process has been recognised as a key mechanism for regulating the function of a diversity of cell surface proteins. Dysregulation of ectodomain shedding is associated with autoimmune and cardiovascular diseases, neurodegeneration, infection, inflammation, and cancer. CD156c has been studied in the context of ectodomain shedding and has been demonstrated as key molecule in most of the shedding events in cancer and neurodegenerative disorders.

Additional information: Clone REA309 displays negligible binding to Fc receptors.

 

Clone REA319 recognizes the human CD162 antigen, a single-pass type I membrane protein which is also known as P-selectin glycoprotein ligand 1 (PSGL-1). CD162 is expressed on neutrophils, monocytes, and most lymphocytes. It is the high affinity receptor for CD62P (P-selectin) on myeloid cells and stimulated T lymphocytes and mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. CD162 is also involved in homeostasis including stem cell homing to the thymus and mature T cell homing to secondary lymphoid organs. It has been found to bind the homeostatic chemokines CCL19 and CCL21 and to support the chemotactic response to these chemokines. 

Additional information: Clone REA319 displays negligible binding to Fc receptors.