CD38 / PerCP / HB7
Product Details
Description | This antibody binds to an epitope between amino acids 273-285 of human CD38, an approximately 45 kDa type II transmembrane protein, expressed on essentially all pre-B lymphocytes, plasma cells, and thymocytes. Also present on activated T lymphocytes, natural killer (NK) lymphocytes, myeloblasts, and erythroblasts. Bimodally expressed during B cell development, modulating from high in immature cells to low in intermediate ones and back to high on mature B cells. This antibody competes with clone AT13/5 (Ab00289) (Ellis 1995). | |
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Conjugate | PerCP | |
Clone | HB7 | |
Target Species | Human | |
Applications | FC | |
Supplier | Novus Biologicals | |
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About CD38
The protein encoded by this gene is a non-lineage-restricted, type II transmembrane glycoprotein that synthesizes and hydrolyzes cyclic adenosine 5'-diphosphate-ribose, an intracellular calcium ion mobilizing messenger. The release of soluble protein and the ability of membrane-bound protein to become internalized indicate both extracellular and intracellular functions for the protein. This protein has an N-terminal cytoplasmic tail, a single membrane-spanning domain, and a C-terminal extracellular region with four N-glycosylation sites. Crystal structure analysis demonstrates that the functional molecule is a dimer, with the central portion containing the catalytic site. It is used as a prognostic marker for patients with chronic lymphocytic leukemia. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]
The protein encoded by this gene is a non-lineage-restricted, type II transmembrane glycoprotein that synthesizes and hydrolyzes cyclic adenosine 5'-diphosphate-ribose, an intracellular calcium ion mobilizing messenger. The release of soluble protein and the ability of membrane-bound protein to become internalized indicate both extracellular and intracellular functions for the protein. This protein has an N-terminal cytoplasmic tail, a single membrane-spanning domain, and a C-terminal extracellular region with four N-glycosylation sites. Crystal structure analysis demonstrates that the functional molecule is a dimer, with the central portion containing the catalytic site. It is used as a prognostic marker for patients with chronic lymphocytic leukemia. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]
About PerCP
Peridinin-Chlorophyll-Protein (PerCP) is a red-emitting fluorescent protein isolated from algae that can be excited by the 488 nm blue laser and captured with a 670/30 nm bandpass filter. PerCP exhibits a large Stokes' Shift, with an excitation peak at 482 nm and an emission peak at 675 nm. PerCP is was historically used in flow cytometry, however it is highly susceptible to photobleaching and has poor stability. Alternatives like BB700, NovaFluor Blue 690 or PerCP-eFluorâ„¢ 710 are preferred. PerCP is a generic dye that has no sole manufacturer.
Peridinin-Chlorophyll-Protein (PerCP) is a red-emitting fluorescent protein isolated from algae that can be excited by the 488 nm blue laser and captured with a 670/30 nm bandpass filter. PerCP exhibits a large Stokes' Shift, with an excitation peak at 482 nm and an emission peak at 675 nm. PerCP is was historically used in flow cytometry, however it is highly susceptible to photobleaching and has poor stability. Alternatives like BB700, NovaFluor Blue 690 or PerCP-eFluorâ„¢ 710 are preferred. PerCP is a generic dye that has no sole manufacturer.
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