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AB101152

Recombinant Human Uridine Phosphorylase 1 protein (His tag N-Terminus)

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(1 Publication)

Recombinant Human Uridine Phosphorylase 1 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 310 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

UP, UPP1, Uridine phosphorylase 1, UPase 1, UrdPase 1

1 Images
SDS-PAGE - Recombinant Human Uridine Phosphorylase 1 protein (His tag N-Terminus) (AB101152)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Uridine Phosphorylase 1 protein (His tag N-Terminus) (AB101152)

ab101152 at 3 μg, 15% SDS-PAGE

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

Q16831

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 40% Glycerol (glycerin, glycerine), 1.16% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMAATGANAEKAESHNDCPVRLLNPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCPGRDYPNICAGTDRYAMYKVGPVLSVSHGMGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKKKLSKA","proteinLength":"Full Length","predictedMolecularWeight":"36 kDa","actualMolecularWeight":null,"aminoAcidEnd":310,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q16831","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Uridine Phosphorylase 1 (UPP1) also known as UPase is a pyrimidine-nucleoside phosphorylase enzyme with a molecular mass of approximately 34 kDa. The enzyme catalyzes the reversible phosphorolysis of uridine and 2'-deoxyuridine to uracil and ribose 1-phosphate or deoxyribose 1-phosphate. This reaction is an important step in the pyrimidine salvage pathway where it contributes to nucleotide pool balance. UPP1 is expressed in a variety of tissues including liver kidney and colon reflecting its diverse physiological roles.
Biological function summary

Uridine Phosphorylase 1 plays an important role in the salvage pathway that maintains nucleotide homeostasis. This process is essential for the efficient recycling of nucleotides which supports DNA and RNA synthesis especially under conditions of limited de novo synthesis. UPP1 does not function as part of a larger enzyme complex operating independently for its specific biochemical activity. The enzyme helps maintain an adequate supply of uracil and cytosine which are important for many cellular processes including cell growth and division.

Pathways

Uridine Phosphorylase 1 is significantly involved in the pyrimidine salvage pathway and is also interconnected with the broader nucleotide metabolism pathway. These pathways are essential for the recycling and synthesis of nucleotides required for nucleic acid production. UPP1 works closely with thymidine phosphorylase (TYMP) and uridine-cytidine kinase both of which are vital in maintaining cellular nucleotide balance. These interactions between enzymes help ensure that cells have the necessary components for vital functions like DNA replication and repair.

Uridine Phosphorylase 1 has been linked to cancer and metabolic disorders. Overexpression of UPP1 is often observed in particular cancers including colorectal cancer where its activity may contribute to cancer progression. In cancer UPP1 shows interaction with proteins like thymidine phosphorylase (TYMP) which is also overexpressed and enhances angiogenesis and tumor growth. Additionally altered UPP1 activity impacts pyrimidine metabolism which can lead to metabolic disorders that disrupt nucleotide balance further linking it to pathological states.

Specifications

Form

Liquid

General info

Function

Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate which can then be utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (PubMed : 7488099). Shows broad substrate specificity and can also accept deoxyuridine and other analogous compounds (Probable).

Sequence similarities

Belongs to the PNP/UDP phosphorylase family.

Product protocols

Target data

Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate which can then be utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (PubMed : 7488099). Shows broad substrate specificity and can also accept deoxyuridine and other analogous compounds (Probable).
See full target information UPP1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

International journal of biological sciences 20:1389-1409 PubMed38385072

2024

UPP1 enhances bladder cancer progression and gemcitabine resistance through AKT.

Applications

Unspecified application

Species

Unspecified reactive species

Wenzhi Du,Sheng Tu,Wenxiu Zhang,Yi Zhang,Wei Liu,Kangping Xiong,Fenfang Zhou,Na Li,Renjie Zhang,Jingtian Yu,Mingxing Li,Wan Xiang,Kaiyu Qian,Gang Wang,Yu Xiao,Xinghuan Wang,Lingao Ju
View all publications

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