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Clone REAL1069 is an antibody fragment derived from the full CD20 N-terminal antibody molecule. It displays no binding to Fc receptors. The recombinantly engineered antibody fragments are multimerized to form the REAdye_lease Complex to bind markers with high avidity.
Clone REAL1069 recognizes the N-terminal region of the CD20 antigen. CD20 is a non-glycosylated transmembrane protein of 33–37 kDa that consists of four conserved transmembrane domains flanked by N- and C-terminal cytoplasmic domains. CD20 is expressed on B lineage cells from the pre–B cell stage to the B cell lymphoblast stage. The antigen is further expressed on most malignant B cells (B-cell lymphomas). CD20 is not found on early B cell progenitors or plasma cells. Oligomers of CD20 form a
Ca2+ channel and might function in the regulation of local responses during B cell activation. In vitro effects of CD20-specific antibodies on resting B cells indicate that CD20 is able to transduce an extracellular signal affecting the G0/G1 cell cycle transition. Studies have demonstrated that CD20-initiated intracellular signals involve tyrosine kinase activation and that CD20 is tightly associated with both serine and tyrosine kinases.
For removal of REAdye_lease fluorochromes for optional relabeling with different fluorochrome-conjugated REAdye_lease antibodies use the REAlease Support Kit (130-120-675).
MS4A1, B1, Bp35, CVID5, LEU-16, MS4A2, S7, Ly-44
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