NUDT5 (NM_014142) Human Recombinant Protein

Specifications

Product Data
Species	Human
Expression Host	HEK293T
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) >RC200204 protein sequence Red=Cloning site Green=Tags(s) MESQEPTESSQNGKQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTRKEQTADGVAVIPVLQR TLHYECIVLVKQFRPPMGGYCIEFPAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPGLSNCT IHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDLLQRLDALVAEEHLTVDARVYSYALALKHANAK PFEVPFLKF TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag	C-Myc/DDK
Predicted MW	24.1 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.
Reference Data
RefSeq	NP_054861
Locus ID	11164
UniProt ID	Q9UKK9
Refseq Size	1224
Cytogenetics	10p14
Refseq ORF	657
Synonyms	hNUDT5; YSA1; YSA1H; YSAH1
Summary	This gene belongs to the Nudix (nucleoside diphosphate linked moiety X) hydrolase superfamily. The encoded enzyme catalyzes the hydrolysis of modified nucleoside diphosphates, including ADP-ribose (ADPR) and 8-oxoGua-containing 8-oxo-dADP and 8-oxo-dGDP. Protein-bound ADP ribose can be hazardous to the cell because it can modify some amino acid residues, resulting in the inhibition of ATP-activated potassium channels. 8-oxoGua is an oxidized form of guanine that can potentially alter genetic information by pairing with adenine and cytosine in RNA. Presence of 8-oxoGua in RNA results in formation of abnormal proteins due to translational errors. [provided by RefSeq, Aug 2013]
Protein Pathways	Purine metabolism

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