Dynein light chain 1 Recombinant Protein | DYNLL1 recombinant protein

Recombinant Human Dynein light chain 1, cytoplasmic protein

Cat. Num. AAA717105

• Gene Names: DYNLL1; LC8; PIN; DLC1; DLC8; LC8a; DNCL1; hdlc1; DNCLC1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Dynein light chain 1; Recombinant Human Dynein light chain 1; cytoplasmic protein; 8 kDa dynein light chain; DLC8; Dynein light chain LC8-type 1; Protein inhibitor of neuronal nitric oxide synthase; PIN; DYNLL1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1-89aa; Full Length
• Sequence: MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
• Sequence Length: 89

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for DYNLL1 recombinant protein

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.

Product Categories/Family for DYNLL1 recombinant protein

Apoptosis

References

Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster.Dick T., Ray K., Salz H.K., Chia W.Mol. Cell. Biol. 16:1966-1977(1996) Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a molecular switch for its dimerization status and functions.Song C., Wen W., Rayala S.K., Chen M., Ma J., Zhang M., Kumar R.J. Biol. Chem. 283:4004-4013(2008) Biochemical and structural characterization of the Pak1-LC8 interaction.Lightcap C.M., Sun S., Lear J.D., Rodeck U., Polenova T., Williams J.C.J. Biol. Chem. 283:27314-27324(2008) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Structural basis for the interaction between dynein light chain 1 and the glutamate channel homolog GRINL1A.Garcia-Mayoral M.F., Martinez-Moreno M., Albar J.P., Rodriguez-Crespo I., Bruix M.FEBS J. 277:2340-2350(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and facilitates chromosome alignment.Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.J. Cell Biol. 192:959-968(2011) ATM substrate Chk2-interacting Zn2+ finger (ASCIZ) Is a bi-functional transcriptional activator and feedback sensor in the regulation of dynein light chain (DYNLL1) expression.Jurado S., Conlan L.A., Baker E.K., Ng J.L., Tenis N., Hoch N.C., Gleeson K., Smeets M., Izon D., Heierhorst J.J. Biol. Chem. 287:3156-3164(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structure of the PIN/LC8 dimer with a bound peptide.Liang J., Jaffrey S.R., Guo W., Snyder S.H., Clardy J.Nat. Struct. Biol. 6:735-740(1999) Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation.Gallego P., Velazquez-Campoy A., Regue L., Roig J., Reverter D.J. Biol. Chem. 288:12283-12294(2013)

NCBI and Uniprot Product Information

• NCBI GI #: 83267866
• NCBI GeneID: 8655
• NCBI Accession #: NP_001032583.1
• NCBI GenBank Nucleotide #: NM_001037494.1
• UniProt Accession #: P63167; Q15701
• Molecular Weight: 37.4 kDa
• NCBI Official Full Name: dynein light chain 1, cytoplasmic
• NCBI Official Synonym Full Names: dynein, light chain, LC8-type 1
• NCBI Official Symbol: DYNLL1
• NCBI Official Synonym Symbols: LC8; PIN; DLC1; DLC8; LC8a; DNCL1; hdlc1; DNCLC1
• NCBI Protein Information: dynein light chain 1, cytoplasmic
• UniProt Protein Name: Dynein light chain 1, cytoplasmic
• Protein Family: Dynein
• UniProt Gene Name: DYNLL1
• UniProt Synonym Gene Names: DLC1; DNCL1; DNCLC1; HDLC1; DLC8; PIN
• UniProt Entry Name: DYL1_HUMAN

NCBI Description

Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized. [provided by RefSeq, Jul 2008]

Uniprot Description

LC8: a highly conserved cytoplasmic protein of the dynein light chain family. Cytoplasmic dyneins are large enzyme complexes. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain. Interacts with and inhibits the activity of neuronal nitric oxide synthase (nNOS). A highly conserved protein, showing 92% amino acid similarity with the nematode homolog. Binding of this protein destabilizes the nNOS dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity.

Protein type: Motility/polarity/chemotaxis; Microtubule-binding; Motor

Chromosomal Location of Human Ortholog: 12q24.23

Cellular Component: centrosome; cytoplasm; cytoplasmic dynein complex; cytosol; kinetochore; membrane; microtubule; mitochondrion; nucleus; plasma membrane; signalosome

Molecular Function: enzyme binding; motor activity; nitric-oxide synthase regulator activity; protein binding; protein C-terminus binding; protein domain specific binding; protein homodimerization activity

Biological Process: actin cytoskeleton organization and biogenesis; anatomical structure morphogenesis; antigen processing and presentation of exogenous peptide antigen via MHC class II; apoptosis; cellular protein metabolic process; ER to Golgi vesicle-mediated transport; female gamete generation; G2/M transition of mitotic cell cycle; macroautophagy; mitotic cell cycle; negative regulation of phosphorylation; organelle organization and biogenesis; post-translational protein modification; programmed cell death; protein amino acid N-linked glycosylation via asparagine; regulation of catalytic activity; regulation of transcription, DNA-dependent; substantia nigra development; transcription, DNA-dependent; viral reproduction