CD38 / PE-Cy7 / AT1
Product Details
Description | CD38 is a type II transmembrane glycoprotein that is present on early B- and T-cell lineages and activated B- and T-cells but is absent from most mature resting peripheral lymphocytes. CD38 is also found on thymocytes, pre-B cells, germinal center B-cells, mitogen-activated T-cells, monocytes and Ig-secreting plasma cells. CD38 is expressed on CD34+ cells. The CD34+CD38- population of hematopoietic stems cells defines the most pluripotent cells (e.g. blast colony forming cells). | |
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Conjugate | PE-Cy7 | |
Clone | AT1 | |
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 PE-Cy7
PE-Cyanine®7 (PE-Cy7, RPE-Cy7) is a far red-emitting tandem fluorophore that combines phycoerythrin (PE) and Cy7. The donor molecule, PE can be excited by the 488-nm blue, 532-nm green, or 561-nm yellow-green laser and and transfers energy to the acceptor molecule, Cy7, which emitts light that can be captured with a 780/60 nm bandpass filter. PE-CY7 has an excitation peak at 565 nm and an emission peak at 778 nm, and is a suitable alternative to PE-Vio®770 and PE-Fire™ 780.
PE-Cyanine®7 (PE-Cy7, RPE-Cy7) is a far red-emitting tandem fluorophore that combines phycoerythrin (PE) and Cy7. The donor molecule, PE can be excited by the 488-nm blue, 532-nm green, or 561-nm yellow-green laser and and transfers energy to the acceptor molecule, Cy7, which emitts light that can be captured with a 780/60 nm bandpass filter. PE-CY7 has an excitation peak at 565 nm and an emission peak at 778 nm, and is a suitable alternative to PE-Vio®770 and PE-Fire™ 780.
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