Recombinant Human SUMO1 Agarose Protein, CF Summary
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-740
Formulation | Supplied as a solution of 20% (v/v) Ethanol in deionized water |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Do not freeze.
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Reconstitution Calculator
Background: SUMO1
Human Small Ubiquitin-like Modifier 1 (SUMO1), also known as Sentrin, UBL1, and SMT3C, is synthesized as a 101 amino acid (aa) propeptide with a predicted molecular weight of 11.5 kDa. Human SUMO1 is the most unique of the four identified SUMO proteins and shares only 44%, 47%, and 41% aa sequence identity with SUMO2, SUMO3, and SUMO4, respectively. In contrast, human SUMO1 shares 100% aa sequence identity with the mouse ortholog. 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 cleavage of a four aa C-terminal prosegment, the C-terminal glycine residue of SUMO1 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO1 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). SUMOylation can occur without the requirement of a specific SUMO ligase (E3), where SUMO1 is transferred directly from UBE2I/Ubc9 to specific substrates. In Alzheimer"s disease models SUMO1 has been shown to influence the generation of Amyloid-beta peptide by promoting the accumulation of BACE-1 (7). Covalent modification of Phosphatase and Tensin Homolog Deleted on Chromosome (PTEN) by SUMO1 is thought to regulate tumorigenesis by retaining PTEN at the plasma membrane, an effect that suppresses PI 3-Kinase/Akt-dependent tumor growth (8).
SUMO1 is covalently coupled to agarose beads via primary amines allowing for a fully functional C-terminus. Useful for affinity binding of SUMO1 activating enzyme, SUMO conjugating E2 enzyme UBE2I, SUMO1 ligases, SUMO C-terminal hydrolases, and other proteins/enzymes that have an affinity for SUMO1. The Ubiquitin-like SUMO1 is conjugated to a variety of proteins in the presence of UBE2I and the SAE1/SAE2 activating enzyme. SUMO modification has been implicated in functions such as nuclear transport, chromosome segregation, and transcriptional regulation.
- 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.
- Yun, S.M. et al. (2012) Neurobiol Aging. [Epub ahead of print].
- Huang, J. et al. (2012) Nat. Commun. 3:911.
Citation for Recombinant Human SUMO1 Agarose 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.
1Citation: Showing 1 - 1
- ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome StabilityAuthors: P Haahr, N Borgermann, X Guo, D Typas, D Achuthanku, S Hoffmann, R Shearer, TK Sixma, N MailandMol. Cell, 2018;0(0):.Species: HumanSample Types: Cell LysatesApplications: Bioassay
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