DYNLL1 (NM_001037494) Human Recombinant Protein

CAT#: TP720193

Recombinant protein of human dynein, light chain, LC8-type 1 (DYNLL1), transcript variant 1

Size: 10 ug 50 ug 500 ug 1 mg


  View other "DYNLL1" proteins (12)

USD 330.00

7 Weeks*

Size
    • 10 ug

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Frequently bought together (1)
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    • 100 ul

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Specifications

Product Data
Species Human
Expression Host E. coli
Expression cDNA Clone or AA Sequence
Tag N-His
Predicted MW 12.5 kDa
Concentration lot specific
Purity >95% as determined by SDS-PAGE and Coomassie blue staining
Buffer Provided lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl
Endotoxin < 0.1 EU per µg protein as determined by LAL test
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. Dissolve the lyophilized protein in ddH2O. It is not recommended to reconstitute a concentration less than 100 µg/ml. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Store at -80°C.
Stability Stable for at least 6 months from date of receipt under proper storage and handling conditions.
Reference Data
RefSeq NP_001032583
Locus ID 8655
UniProt ID P63167, Q6FGH9
Cytogenetics 12q24.31
Synonyms DLC1; DLC8; DNCL1; DNCLC1; hdlc1; LC8; LC8a; PIN
Summary 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]

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