DYNLL2 Antibody (1G7): sc-293315

DYNLL2 Antibody (1G7) is a mouse monoclonal IgG2b kappa light chain antibody that detects DYNLL2 protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-DYNLL2 antibody (1G7) is available as the non-conjugated format. DYNLL2 plays a crucial role in cellular transport mechanisms, functioning as a light chain of the dynein motor complex, which is essential for the movement of cellular cargo along microtubules. DYNLL2 is primarily located in the cytoplasm, where DYNLL2 interacts with various components of the dynein complex to facilitate the transport of organelles, vesicles, and other cellular materials toward the minus end of microtubules, which is vital for maintaining cellular organization and function. DYNLL2 is particularly important in neurons, where DYNLL2 contributes to the transport of signaling molecules and organelles necessary for synaptic function and neuronal health. Dysregulation of dynein-mediated transport has been implicated in several neurodegenerative diseases, highlighting the significance of DYNLL2 in both normal physiology and disease states. With high sequence identity to DYNLL1, DYNLL2 also shares functional similarities, yet DYNLL2 is uniquely involved in specific interactions that can influence cellular dynamics and signaling pathways.

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DYNLL2 Antibody (1G7) References:

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2. Cytoplasmic dynein functions as a gear in response to load.  |  Mallik, R., et al. 2004. Nature. 427: 649-52. PMID: 14961123
3. The dynein heavy chain family.  |  Asai, DJ. and Wilkes, DE. 2004. J Eukaryot Microbiol. 51: 23-9. PMID: 15068262
4. The offloading model for dynein function: differential function of motor subunits.  |  Lee, WL., et al. 2005. J Cell Biol. 168: 201-7. PMID: 15642746
5. Genetic analysis of the cytoplasmic dynein subunit families.  |  Pfister, KK., et al. 2006. PLoS Genet. 2: e1. PMID: 16440056
6. The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain.  |  Wagner, W., et al. 2006. Biochemistry. 45: 11564-77. PMID: 16981716
7. Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster.  |  Dick, T., et al. 1996. Mol Cell Biol. 16: 1966-77. PMID: 8628263
8. PIN: an associated protein inhibitor of neuronal nitric oxide synthase.  |  Jaffrey, SR. and Snyder, SH. 1996. Science. 274: 774-7. PMID: 8864115