CD38 (NAD+ glycohydrolase) is a 45 kDa type II transmembrane glycoprotein able to induce activation, proliferation and differentiation of mature lymphocytes and mediate apoptosis of myeloid and lymphoid progenitor cells. Another role of CD38 is provided by enzymatic activity of its extracellular part. CD38 acts as NAD+ glycohydrolase converting NAD+ into ADP-ribose, as ADP-ribosyl cyclase producing cADPR and as cADPR hydrolase, thus affecting levels of calcium-mobilizing metabolites. ADPR produced by CD38 serves as an important second messenger of neutrophil and dendritic cell migration. It is strongly expressed mainly on plasma cells and activated T and B lymphocytes; it is an antigenic marker of lymphoid cells. Its binding is blocked by daratumumab. The mouse monoclonal antibody HB7 recognizes an extracellular epitope within amino acids 273-285 of human CD38, and can be used for flow cytometry, Western blotting, immunocytochemistry and immunoprecipitation. Currently availavle formats: purified 11-915-C100 FITC 1F-915-T100 Fig. 1: Separation of human monocytes (red-filled) from CD19 negative CD38 negative lymphocytes (black-dashed) in flow cytometry analysis (surface staining) of human peripheral whole blood stained using anti-human CD38 (HB7) purified antibody / GAM APC. Fig. 2: Staining pattern of Anti-human CD38 FITC antibody (clone HB7) in dot-plot fluorescence visualization (B cell gate) on blood leukocytes isolated from buffy coats. CD27 detected with anti-human CD27 Pacific Blue™ antibody (clone LT27). Fig. 3: Reactivity of anti-human CD38 FITC antibody (clone HB7) with human peripheral leukocytes (isolated from buffy coats).
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Today we bring an extension to the Notch topics presented in previous blog.
Notch signaling represents one of the cornerstones of the immune system.
Anti-human CD38 clones HB7 and HIT2 were compared regarding their reactivity with particular blood cell populations.