DYNLL1 (NM_003746) Human Mass Spec Standard

CAT#: PH318752

DYNLL1 MS Standard C13 and N15-labeled recombinant protein (NP_003737)

Product Images

Coomassie blue staining of purified DYNLL1 protein (Cat# TP318752). The protein was produced from HEK293T cells transfected with DYNLL1 cDNA clone (Cat# RC218752) using MegaTran 2.0 (Cat# TT210002).

Specifications

Product Data

• Tag: C-Myc/DDK
• Species: Human
• Expression Host: HEK293
• Expression cDNA Clone or AA Sequence: RC218752
• Predicted MW: 10.4 kDa
• Protein Sequence:
  Sequence Link

  >RC218752 protein sequence
  Red=Cloning site Green=Tags(s)
  
  MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHET
  KHFIYFYLGQVAILLFKSG
  
  TRTRPLEQKLISEEDLAANDILDYKDDDDKV
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Concentration: >0.05 µg/µL as determined by microplate BCA method
• Labeling Method: Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
• Buffer: 25 mM Tris-HCl, 100 mM glycine, pH 7.3
• Storage: Store at -80°C. Avoid repeated freeze-thaw cycles.
• Stability: Stable for 3 months from receipt of products under proper storage and handling conditions.

Reference Data

• RefSeq: NP_003737
• RefSeq Size: 733
• RefSeq ORF: 267
• Synonyms: DLC1; DLC8; DNCL1; DNCLC1; hdlc1; LC8; LC8a; PIN
• Locus ID: 8655
• UniProt ID: P63167, Q6FGH9
• Cytogenetics: 12q24.31
• 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]