Recombinant Human His6-Pro-SUMO3 Protein, CF
Recombinant Human His6-Pro-SUMO3 Protein, CF Summary
Product Specifications
Contains an N-terminal 6-His tag
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-761
Formulation | X mg/ml (X µM) in 50 mM HEPES pH 8.0, 150 mM NaCl, 1mM 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.
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Reconstitution Calculator
Background: SUMO3
Human Small Ubiquitin-like Modifier 3 (SUMO3), also known as SMT3A, is synthesized as a 103 amino acid (aa), propeptide with a predicted 11.5 kDa. SUMO3 contains a two aa C-terminal prosegment. Human SUMO3 shares 83% sequence identity with mouse SUMO3. SUMO3 also has high aa sequence homology to SUMO2 and SUMO4, 87% and 75%, respectively. SUMO3 shares only 47% sequence identity with SUMO1. SUMOs are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed SUMOylation (1-3). All SUMO proteins share a conserved Ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following prosegment cleavage, the C-terminal glycine residue of SUMO3 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO3 is conjugated to a variety of molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme (4,5). In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p (6). Because of the high level of sequence homology most studies report effects of SUMO2/3. For example, addition of SUMO2/3 was shown to modulate the function of ARHGAP21, a RhoGAP protein known to be involved in cell migration (7). Other reports indicate that the conjugation by SUMO2/3, but not SUMO1, may represent an important mechanism to protect neurons during episodes of cerebral ischemia (8,9). However, studies suggest that SUMO2/3 expression is regulated in an isoform-specific manner since oxidative stress downregulated the transcription of SUMO3 but not SUMO2 (10).
All SUMO isoforms are translated with additional C-terminal residues that have to be removed to generate the active protein. Pro-SUMO3 (103 amino acids) is the inactive precursor of SUMO3 (92 amino acids) and is processed at the C-terminus by SUMO3 specific proteases (SENPs).The resulting SUMO3 protein has the conserved C-terminal Gly-Gly residues that function in activation and conjugation reactions. This protein can be used as a negative control in SUMOlyation reactions or as a substrate for SENPs. This His-6 tag is at the N-terminus. NCBIAccession # NM_006936.
- Desterro, J.M. et al. (1997) FEBs. Lett. 417:297.
- Bettermann, K. et al. (2012) Cancer Lett. 316:113.
- Praefcke, G.J. et al. (2012) Trends Biochem. Sci. 37:23.
- Okuma, T. et al. (1999) Biochem. Biophys. Res. Commun. 254:693.
- Tatham, M.H. et al. (2001) J. Biol. Chem. 276:35368.
- Johnson, E.S. et al. (1997) EMBO J. 16:5509.
- Bigarella, C.L. et al. (2012) FEBS Lett. 586:3522.
- Datwyler, A.L. et al. (2012) J. Cereb. Blood Flow Metab. 31:2152.
- Wang, Z. et al. (2012) Protein Expr. Purif. 82:174.
- Sang, J. et al. (2012) Biochem. J. 435:489.
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