DYNLL1 (NM_001037494) Human Recombinant Protein

SKU TP319822L

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

Product Data

• Species: Human
• Expression Host: HEK293T
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  >RC219822 representing NM_001037494; Red=Cloning site Green=Tags(s); ; MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHET; KHFIYFYLGQVAILLFKSG; ; TRTRPLEQKLISEEDLAANDILDYKDDDDKV
• Tag: C-Myc/DDK
• Predicted MW: 10.2 kDa
• Concentration: >0.05 µg/µL as determined by microplate BCA method
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: 25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
• Preparation: Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
• Note: For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
• Storage: Store at -80°C.
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
• Shipping: Dry Ice

Reference Data

• RefSeq: NP_001032583
• Locus ID: 8655
• UniProt ID: P63167
• Cytogenetics: 12q24.31
• RefSeq Size: 820
• RefSeq ORF: 267
• 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]