UPP1 Protein (AA 1-310) (His tag)
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- Target Alle UPP1 Proteine anzeigen
- UPP1 (Uridine Phosphorylase 1 (UPP1))
- Protein-Typ
- Recombinant
- Proteineigenschaft
- AA 1-310
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Spezies
- Human
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Quelle
- Escherichia coli (E. coli)
- Aufreinigungstag / Konjugat
- Dieses UPP1 Protein ist gelabelt mit His tag.
- Applikation
- SDS-PAGE (SDS)
- Produktmerkmale
- UPP1, 1-310aa, Human, His tag, E.coli
- Reinheit
- > 90 % by SDS - PAGE
- Top Product
- Discover our top product UPP1 Protein
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- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Liquid
- Konzentration
- 0.25 mg/ml (determined by Bradford assay)
- Buffer
- Liquid. In 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 40% glycerol, 200mM NaCl
- Lagerung
- 4 °C
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- Target
- UPP1 (Uridine Phosphorylase 1 (UPP1))
- Andere Bezeichnung
- UPP1 (UPP1 Produkte)
- Synonyme
- upp1 Protein, UDRPASE Protein, UP Protein, UPASE Protein, UPP Protein, im:6911242 Protein, zgc:110755 Protein, AI325217 Protein, UPase Protein, UdRPase Protein, Up Protein, Upp Protein, uridine phosphorylase 1 Protein, uridine phosphorylase Protein, upp1 Protein, NP_RS08675 Protein, Tsp_02326 Protein, UPP1 Protein, Upp1 Protein
- Hintergrund
- Uridine phosphorylase 1, also known as UPP1 catalyses the reversible phosphorolysis of uridine to uracil. The reaction products are then utilized as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. The expression levels and the enzymatic activity of UPP1 are higher in human solid tumors than in adjacent normal tissues. In addition, UPP1 controls the homeostatic regulation of uridine concentration in plasma and tissues and plays a role in the intracellular activation of 5-fluorouracil. Recombinant human UPP1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Synonyms: Uridine phosphorylase 1, UP, UPASE, UPP, UrdPase 1. NCBI no.: NP_853628
- Molekulargewicht
- 36 kDa (330aa), confirmed by MALDI-TOF
- Pathways
- Ribonucleoside Biosynthetic Process
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