URM1 Human
Ubiquitin Related Modifier 1 Human Recombinant
Cat. No.
BT23131
Source
Escherichia Coli.
Synonyms
Ubiquitin-related modifier 1 homolog, URM1, C9orf74, MGC2668, RP11-339B21.4.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
URM1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101 a.a.) and having a molecular mass of 13.5kDa.
URM1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
URM1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
URM1, also known as ubiquitin-related modifier 1 homolog protein, is a protein primarily involved in post-translational modification through the urmylation pathway. In this pathway, URM1 forms a covalent bond with its activating enzyme, Uba4p (E1 enzyme). Studies using Saccharomyces cerevisiae have shown that this URM1-Uba4p complex conjugates to alkyl hydroperoxide reductase (Ahp1). This interaction suggests a potential role for URM1 in the mammalian oxidative stress response.
Description
The URM1 protein, expressed in E. coli, is a single polypeptide chain without any glycosylation. It consists of 121 amino acids, with amino acids 1 to 101 representing the URM1 sequence, resulting in a molecular weight of 13.5 kDa. A 20 amino acid His-tag is fused to the N-terminus of URM1 to facilitate purification, which is carried out using proprietary chromatographic methods.
Physical Appearance
The product is a clear, colorless solution that has been sterilized by filtration.
Formulation
The URM1 protein is supplied in a solution at a concentration of 1 mg/ml. The solution also contains 20mM Tris-HCl buffer with a pH of 8.0, 10% glycerol, and 1mM DTT.
Stability
For short-term storage (up to 4 weeks), the URM1 solution should be kept at a refrigerated temperature of 4°C. For extended storage periods, it is recommended to store the solution in a frozen state at -20°C. To ensure optimal protein stability during long-term storage, the addition of a carrier protein, such as HSA or BSA, at a concentration of 0.1% is advised. Repeated freezing and thawing of the URM1 solution should be avoided.
Purity
The purity of the URM1 protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Ubiquitin-related modifier 1 homolog, URM1, C9orf74, MGC2668, RP11-339B21.4.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAPLSVEVE FGGGAELLFD GIKKHRVTLP GQEEPWDIRN LLIWIKKNLL KERPELFIQG DSVRPGILVL INDADWELLG ELDYQLQDQD SVLFISTLHG G.
Product Science Overview
Introduction
Ubiquitin Related Modifier 1 (URM1) is a protein coding gene that plays a crucial role in various cellular processes. It is part of the ubiquitin-like protein family, which is involved in the post-translational modification of proteins. URM1 is particularly significant due to its dual function as both a sulfur carrier and a ubiquitin-like protein (UBL).
Gene and Protein Structure
Functions
URM1 serves multiple functions within the cell:
- Sulfur Carrier Activity: URM1 is essential for the 2-thiolation of cytosolic tRNAs, specifically tRNA(Lys), tRNA(Glu), and tRNA(Gln). This process is crucial for the proper functioning of these tRNAs during protein synthesis .
- Ubiquitin-like Modification: URM1 can be covalently attached to target proteins via an isopeptide bond. This modification is similar to ubiquitination and affects the stability, localization, and activity of the target proteins .
Mechanism of Action
URM1 undergoes a unique post-translational modification where it is thiocarboxylated at its C-terminus by the enzyme MOCS3. This thiocarboxylated form of URM1 then acts as a sulfur donor in the 2-thiolation reaction of tRNAs. Additionally, URM1 can form conjugates with other proteins, particularly under oxidative stress conditions .
Clinical Significance
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