Recombinant Human Urm1 protein is a Human Full Length protein, in the 1 to 101 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
>95% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, MS
No
M G S S H H H H H H S S G L V P R G S H M A A P L S V E V E F G G G A E L L F D G I K K H R V T L P G Q E E P W D I R N L L I W I K K N L L K E R P E L F I Q G D S V R P G I L V L I N D A D W E L L G E L D Y Q L Q D Q D S V L F I S T L H G G
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as MOCS3, ATPBD3, CTU2, USP15 and CAS. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
C9orf74, C9orf74, URM1, Ubiquitin-related modifier 1
Recombinant Human Urm1 protein is a Human Full Length protein, in the 1 to 101 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
>95% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, MS
No
No
Human
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
M G S S H H H H H H S S G L V P R G S H M A A P L S V E V E F G G G A E L L F D G I K K H R V T L P G Q E E P W D I R N L L I W I K K N L L K E R P E L F I Q G D S V R P G I L V L I N D A D W E L L G E L D Y Q L Q D Q D S V L F I S T L H G G
Full Length
13.5 kDa
1 to 101
Recombinant
His tag N-Terminus
Liquid
ab105598 was purified by using anion-exchange chromatography (DEAE sepharose resin) and gel-filtration chromatography (Sephacryl S-200) with 20mM Tris pH 7.5, 2mM EDTA.
Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as MOCS3, ATPBD3, CTU2, USP15 and CAS. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
Belongs to the URM1 family.
C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
Urm1 also known as ubiquitin-related modifier 1 is a small protein with a mass of approximately 11 kDa. It belongs to the ubiquitin-like protein family and is expressed in a wide range of tissues notably in human tissues at the cellular level. Urm1 functions as a molecular tag influencing a variety of cellular processes through its conjugation to substrate proteins. It shares structural similarities with ubiquitin and employs a similar conjugation pathway involving E1-like activating enzymes.
Urm1 acts in the thiolation of tRNA and as part of the ubiquitin-related modifier system which affects protein modification and signaling. It plays roles in regulating sulfur metabolism and is important in the biosynthesis of thiolated tRNAs. Urm1 is also involved in oxidative stress response by being part of a complex that modifies proteins in reaction to environmental stressors. As a result Urm1 impacts cellular homeostasis and the stability of various proteins within the cell.
Urm1 influences the tRNA modification pathway an important mechanism for proper protein synthesis and function. It also participates in the cellular response to oxidative stress primarily through its interaction with cellular signaling proteins such as ROS-responsive transcription factors. In these pathways Urm1-related conjugations modify proteins affecting their activity during cellular defense mechanisms and the maintenance of protein structure under stress conditions.
Urm1 impacts conditions related to cellular redox states such as cancer and neurodegenerative disorders. Aberrant regulation of Urm1 and its pathways can lead to increased oxidative stress and faulty protein synthesis contributing to these diseases. Urm1's interaction with other proteins such as p53 in tumorigenesis highlights its relevance in the cellular processes that when deregulated can lead to cancer progression. In neurodegenerative diseases diminished Urm1 function can result in the accumulation of misfolded proteins exacerbating disease phenotypes.
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15% SDS-PAGE analysis of 3μg ab105598.
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