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AB165841

Recombinant Human UBR1 protein (GST tag N-Terminus)

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Recombinant Human UBR1 protein (GST tag N-Terminus) is a Human Fragment protein, in the 2 to 100 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

E3 ubiquitin-protein ligase UBR1, N-recognin-1, Ubiquitin-protein ligase E3-alpha-1, Ubiquitin-protein ligase E3-alpha-I, UBR1

1 Images
SDS-PAGE - Recombinant Human UBR1 protein (GST tag N-Terminus) (AB165841)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human UBR1 protein (GST tag N-Terminus) (AB165841)

ab165841 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

Q8IWV7

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"ADEEAGGTERMEISAELPQTPQRLASWWDQQVDFYTAFLHHLAQLVPEIYFAEMDPDLEKQEESVQMSIFTPLEWYLFGEDPDICLEKLKHSGAFQLCG","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":100,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q8IWV7","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

UBR1 also known as E3 ubiquitin-protein ligase UBR1 is a component of the N-end rule pathway. This protein has a mass of approximately 220 kDa and functions as an E3 ubiquitin ligase. It recognizes proteins with destabilizing N-terminal residues and facilitates their polyubiquitination marking them for proteasomal degradation. UBR1 is expressed abundantly in tissues such as the heart pancreas and brain which suggests its significant role in cellular processes across multiple organ systems.
Biological function summary

In cellular regulation and homeostasis UBR1 plays a critical role. As a part of the larger ubiquitin-proteasome system it maintains protein quality control and modulates turnover rates of key proteins which ensures normal cellular functions. Although not directly a part of a complex it interacts with other UBR family members like UBR2 under overlapping pathways which can influence the degradation of specific proteins thereby impacting various signaling cascades.

Pathways

UBR1 is an integral regulator within the proteolytic pathways particularly the N-end rule pathway and ubiquitin-mediated proteolysis. In the N-end rule pathway it cooperates closely with other components like UBR2 which together target specific substrates for degradation therefore impacting processes like cell cycle regulation and stress responses. These pathways ensure balanced protein levels influencing processes such as cell growth and apoptosis vital for maintaining cellular integrity.

UBR1 mutations or dysfunction are strongly associated with Johanson-Blizzard Syndrome and pancreatic insufficiency. Patients with these conditions often present genetic mutations that impair UBR1's normal function leading to disrupted protein degradation and developmental abnormalities. The disruptions in UBR1 function also show interactions with proteins involved in growth and development suggesting its broader role in maintaining physiological stability and highlighting its potential as a therapeutic target.
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Specifications

Form

Liquid

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General info

Function

E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (PubMed : 15548684, PubMed : 16311597, PubMed : 18162545, PubMed : 20835242, PubMed : 28392261). Recognizes and binds proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed : 18162545, PubMed : 20835242, PubMed : 28392261). Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed : 18162545). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed : 20835242). In contrast, it strongly binds methylated N-degrons (PubMed : 28392261). Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (PubMed : 20298436).

Sequence similarities

Belongs to the E3 ubiquitin-protein ligase UBR1-like family.

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Product protocols

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Target data

E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (PubMed : 15548684, PubMed : 16311597, PubMed : 18162545, PubMed : 20835242, PubMed : 28392261). Recognizes and binds proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed : 18162545, PubMed : 20835242, PubMed : 28392261). Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed : 18162545). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed : 20835242). In contrast, it strongly binds methylated N-degrons (PubMed : 28392261). Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (PubMed : 20298436).
See full target information UBR1
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