CD38 / Janelia Fluor 549 / AT13/5
Product Details
| Description | Binds specifically to 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 HB7 (Ab00128) (Ellis 1995) which has been shon to bind to an epitope between amino acids 273-285). | |
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| Conjugate | Janelia Fluor 549 | |
| Clone | AT13/5 | |
| 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 Janelia Fluor 549
Janelia Fluor® 549 was developed at the Janelia Campus of the Howard Hughes Medical Institute but is commercialized by other vendors. The Janelia Fluor®s family is unique in that the fluorophores are cell-permeable and are available in photoactivatable forms. These fluorophores were developed for super-resolution microscopy (STED, PALM and STORM) and live-cell microscopy in the HaloTag and SNAP-tag versions. Janelia Fluor® 549 has an excitation peak at 549 nm and an emission peak at 571 nm.
Janelia Fluor® 549 was developed at the Janelia Campus of the Howard Hughes Medical Institute but is commercialized by other vendors. The Janelia Fluor®s family is unique in that the fluorophores are cell-permeable and are available in photoactivatable forms. These fluorophores were developed for super-resolution microscopy (STED, PALM and STORM) and live-cell microscopy in the HaloTag and SNAP-tag versions. Janelia Fluor® 549 has an excitation peak at 549 nm and an emission peak at 571 nm.
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