Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 µg/ml. Dissolve the lyophilized protein in 1X PBS.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.
8 kDa dynein light chain
Cytoplasmic dynein light polypeptide
Dynein , cytoplasmic, light chain 1
Dynein light chain 1 cytoplasmic
Dynein light chain 1, cytoplasmic
Dynein light chain LC8 type 1
Dynein light chain LC8-type 1
Dynein, cytoplasmic, light polypeptide 1
Dynein, light chain, LC8-type 1
Protein inhibitor of neuronal nitric oxide synthase
Protein inhibitor of neuronal NOS
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures. Binds and inhibits the catalytic activity of neuronal nitric oxide synthase. Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1. Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.
Belongs to the dynein light chain family.
Phosphorylation at Ser-88 appears to control the dimer-monomer transition. According to PubMed:15193260, it is phosphorylated at Ser-88 by PAK1, however, according to PubMed:18650427, the DYNLL1 dimer is not accessible for PAK1 and the phosphorylation could not be demonstrated in vitro.
Cytoplasm, cytoskeleton. Nucleus. Mitochondrion. Upon induction of apoptosis translocates together with BCL2L11 to mitochondria.