Recombinant Human HA-SUMO2 Vinyl Sulfone Protein, CF
Recombinant Human HA-SUMO2 Vinyl Sulfone Protein, CF Summary
Contains an N-terminal HA (YPYDVPDYA) tag and a mixture of C-terminal underivatized and Vinyl Sulfone derivatized protein, quantity is by derivatized content.
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.
1.2 mg/ml (100 μM) in 50 mM MES, pH 6.0, 100 mM NaCl, 10% (v/v) Glycerol
|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.
Human Small Ubiquitin-like Modifier 2 (SUMO2), also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), propeptide with a predicted 11 kDa. SUMO2 contains a two aa C-terminal prosegment and an 18 aa N-terminal protein interacting region between aa 33-50. Human SUMO2 shares 100% aa sequence identity with mouse SUMO2. SUMO2 also has very high aa sequence identity with SUMO3 and SUMO4, 86% and 85%, respectively. SUMO2 shares only 44% aa 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 SUMO2 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO2 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 aa sequence identity most studies report effects of SUMO2/3. For example, post-translational 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 SUMOylation with 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).
This N-terminal HA-tagged SUMO is a potent, irreversible and specific inhibitor of SUMO-specific proteases (SENPs). This protein inhibits the hydrolysis of poly-SUMO chains on substrate proteins in vitro and thus enhances poly-SUMO chain accumulation. The HA peptide sequence (YPYDVPDYA) is derived from the influenza Hemagglutinin protein. This epitope allows for the sensitive identification or purification of SENP activities since it is specifically recognized by anti-HA antibodies and/or anti-HA-agarose.
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Citations for Recombinant Human HA-SUMO2 Vinyl Sulfone Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 2
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Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
Authors: DS Hewings, J Heideker, TP Ma, AP AhYoung, F El Oualid, A Amore, GT Costakes, D Kirchhofer, B Brasher, T Pillow, N Popovych, T Maurer, C Schwerdtfe, WF Forrest, K Yu, J Flygare, M Bogyo, IE Wertz
Nat Commun, 2018;9(1):1162.
Sample Types: Protein
Control of neuronal apoptosis by reciprocal regulation of NFATc3 and Trim17.
Authors: Mojsa B, Mora S, Bossowski J, Lassot I, Desagher S
Cell Death Differ, 2015;22(2):274-86.
Sample Types: Whole Cells
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