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Human NUDT5 Protein 2453

$300.00$1,000.00

Summary

  • Expression: E.coli
  • Pure: Yes (HPLC)
  • Amino Acid Range: Met1-Phe219
SKU: 2453parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

Q9UKK9

express system

E.coli

product tag

N-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

NUDIX hydrolase type 5 (NUDT5) is a kind of ADP-ribose pyrophosphatase and nucleotide metabolizing enzyme in cell metabolism. NUDT5 expression affected chromosome remodeling, involved in cell adhesion, cancer stem cell maintenance and epithelial to mesenchyme transition in breast cancer cells.

molecular weight

The protein has a predicted MW of 25.29 kDa. The protein migrates to 30-35 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human NUDT5 Protein 2453

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
NUDIX hydrolase type 5 (NUDT5) is a kind of ADP-ribose pyrophosphatase and nucleotide metabolizing enzyme in cell metabolism. NUDT5 expression affected chromosome remodeling, involved in cell adhesion, cancer stem cell maintenance and epithelial to mesenchyme transition in breast cancer cells.
Protein names
ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5) (hNUDT5) (YSA1H)
Gene names
NUDT5,NUDT5 NUDIX5 HSPC115
Protein family
Nudix hydrolase family
Mass
9606Da
Function
Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (PubMed:27257257). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10567213, PubMed:10722730, PubMed:17052728, PubMed:19699693, PubMed:21389046). Can also hydrolyze other nucleotide sugars with low activity (PubMed:19699693, PubMed:21389046). In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP synthesis takes place when dephosphorylated at Thr-45 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity).
Catalytic activity
BINDING 28; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 46..47; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 51; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 84; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 96; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 98; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000269|PubMed:17052728"; BINDING 112; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 112; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 116; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 116; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"; BINDING 133; /ligand="substrate"; /ligand_note="ligand shared between dimeric partners"; /note="in other chain"; /evidence="ECO:0000269|PubMed:17052728"; BINDING 166; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126"
Subellular location
Nucleus .
Tissues
Widely expressed. Most abundant in liver.
Structure
Homodimer (PubMed:17052728, PubMed:18462755, PubMed:21768126, PubMed:27257257). Interacts with PARG (PubMed:27257257).
Post-translational modification
Phosphorylation at Thr-45 is required for homodimer stability; dephosphorylation results in destabilization of the homodimer. Dephosphorylation at Thr-45 promotes the ATP-synthesis activity.
Target Relevance information above includes information from UniProt accession: Q9UKK9
The UniProt Consortium

HPLC of Human NUDT5 Protein
The purity of Human NUDT5 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human NUDT5 Protein
Human NUDT5 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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We haven't added any publications to our database yet.
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

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