DYNLL1 (1-89, His-tag) Human Protein

Specifications

Product Data
Species	Human
Expression Host	E. coli
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) MGSSHHHHHH SSGLVPRGSH MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG
Tag	His-tag
Predicted MW	12.5 kDa
Concentration	lot specific
Purity	>90%
Buffer	Presentation State: Purified State: Liquid purified protein Buffer System: 20 mM Tris-HCl buffer (pH 8.0) containing 0.2M NaCl, 1 mM DTT, 10% glycerol
Preparation	Liquid purified protein
Protein Description	Recombinant human DYNLL1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Storage	Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -70°C for longer. Avoid repeated freezing and thawing.
Stability	Shelf life: one year from despatch.
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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