Product Overview
Description
CLPP-00150572 is recombinant human DYNLL1 protein
Applications
Mass Spectrometry, SDS-PAGE
Protein Length
Full length protein
Nature
Recombinant Protein
Sequence
MGSSHHHHHHSSGLVPRGSHMCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Sequence Similarities
Belongs to the dynein light chain family.
Predicted Molecular Weight
13 kDa including tags
Target Information
Alternative Names
8 kDa dynein light chain; 8kDLC; Cytoplasmic dynein light polypeptide; DLC1; DLC8; DNCL1; DNCLC1; DYL1_HUMAN; 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; DYNLL1; HDLC1; LC8; LC8a; MGC126137; MGC126138; MGC72986; PIN; Protein inhibitor of neuronal nitric oxide synthase; Protein inhibitor of neuronal NOS
Protein Function
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.
Tissue Specificity
Ubiquitous.
Shipping & Handling
Constituents
0.0154% DTT, 0.316% Tris HCl, 10% Glycerol (glycerin, glycerine), 1.16% Sodium chloride.
Shipping
Shipped at 4 °C.
Storage
Store at -20 °C or -80 °C.
