Recombinant Human URM1 Isoform 1 Protein, CF
Recombinant Human URM1 Isoform 1 Protein, CF Summary
Product Specifications
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
UL-950
| Formulation | X mg/ml (X μM) in 50 mM HEPES pH 7.5, 100 mM NaCl, 1 mM DTT |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles. |
Reconstitution Calculator
Background: URM1
Ubiquitin Related Modifier 1 (URM1) is a conserved, ubiquitously expressed cytoplasmic Ubiquitin-like protein (1). It is 101 amino acids (aa) in length with a predicted molecular weight of 11.4 kDa (1,2). Human URM1 shares 93% and 94% aa sequence identity with the mouse and rat orthologs, respectively. URM1 contains a core beta -grasp fold and a C-terminal glycine-glycine motif characteristic of Ubiquitin and Ubiquitin-like modifiers (1,2). URM1 is activated by the Ubiquitin-activating (E1)-like enzyme MOCS3, Uba4 in yeast, via the formation of a thiocarboxylate group at its C-terminus. More specifically, MOCS3 and Uba4 mediate the adenylation and subsequent addition of sulfur to the carboxyl group of the C-terminal glycine residue of URM1 (3-5). Thiocarboxylated URM1 functions as a sulfur carrier in the thiolation of eukaryotic cytoplasmic transfer RNA (6-8). URM1 can also be conjugated to lysine residues of several proteins including yeast Ahp1 and human MOCS3, CTU1, and CTU2 (4,7,9). URM1 has been implicated in oxygen stress tolerance and nutrient sensing, invasive growth, and budding in yeast (4,9,10). This recombinant human protein is untagged.
- Furukawa, K. et al. (2000) J. Biol. Chem. 275:7462.
- Singh, S. et al. (2005) Protein Sci. 14:2095.
- Schmitz, J. et al. (2008) Biochemistry 47:6479.
- Van der Veen, A.G. et al. (2011) Proc. Natl. Acad. Sci. USA 108:1763.
- Chowdhury, M.M. et al. (2012) J. Biol. Chem. 287:17297.
- Schlieker, C.D. et al. (2008) Proc. Natl. Acad. Sci. USA 105:18255.
- Pedrioli, P.G. et al. (2008) EMBO Rep. 9:1196.
- Leidel, S. et al. (2009) Nature 458:228.
- Goehring, A.S. et al. (2003) Eukaryot. Cell 2:930.
- Goehring, A.S. et al. (2003) Mol. Biol. Cell 14:4329.
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