DYNLL1 (NM_001037494) Human Recombinant Protein

SKU TP720193L

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

Product Data

• Species: Human
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  Met1-Gly89
• Tag: N-His
• Predicted MW: 12.5 kDa
• Concentration: lot specific
• Purity: >95% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: Lyophilized from a 0.2 um filtered solution of 20mM Tris-HCl, 200mM NaCl, 1mM DTT, pH 8.0.
• Endotoxin: < 0.1 EU per µg protein as determined by LAL test
• Reconstitution Method: 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: Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
• Stability: Stable for at least 6 months from date of receipt under proper storage and handling conditions.
• Shipping: Ambient

Reference Data

• RefSeq: NP_001032583
• Locus ID: 8655
• UniProt ID: P63167
• 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]