The Dcbl Ex6 8C4 antibody, developed by the Developmental Studies Hybridoma Bank (DSHB), targets the Drosophila D-cbl protein, a member of the Cbl family involved in signal transduction and protein ubiquitination.
Host Species: Mouse (IgG1 isotype)
Applications: Immunofluorescence (IF), Western Blot (WB), Immunocytochemistry (ICC)
Immunogen: Recombinant 6X-His D-Cbl fusion protein
Reactivity: Specific to Drosophila melanogaster
Molecular Weight: 51.4 kDa
This antibody has been instrumental in studying the role of D-cbl in Drosophila development, particularly in cell signaling pathways and ubiquitin-mediated protein degradation .
Mouse-derived antibodies targeting Calcineurin B-like protein 6 (CBL6) in plants, such as Oryza sativa (rice) and Arabidopsis thaliana, are used to investigate calcium signaling and stress responses.
| Product ID | Host Species | Reactivity | Applications | Conjugates Available |
|---|---|---|---|---|
| CBMOAB-22055FYB | Mouse | Rice, A. thaliana | WB, ELISA | AP, APC, Biotin, FITC, HRP |
| MO-AB-27303W | Mouse | Cottonwood, A. thaliana | WB, ELISA | Cy3, Cy5, PE, PerCP |
Role of CBL6: Regulates calcium-dependent signaling pathways under abiotic stress (e.g., salinity, drought).
Experimental Use: These antibodies enable protein localization studies and quantification via Western blotting and ELISA .
| Parameter | Dcbl Ex6 8C4 (DSHB) | CBMOAB-22055FYB (Creative Biolabs) |
|---|---|---|
| Target Species | Drosophila melanogaster | Oryza sativa, A. thaliana |
| Primary Use | Developmental biology | Plant stress response mechanisms |
| Conjugate Options | None specified | Multiple (AP, APC, Biotin, etc.) |
| Binding Specificity | D-cbl protein | Calcineurin B-like protein 6 |
While existing CBL6 antibodies are critical for basic research, their utility is confined to model organisms (e.g., Drosophila and plants). No clinical or therapeutic applications have been reported for CBL6-targeting antibodies. Future studies could explore:
Cross-reactivity with mammalian CBL homologs.
Structural characterization of antibody-epitope interactions.