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商品編號(hào)


AG-40T-0380-C250



品牌


Adipogen



公司


Adipogen



公司分類


Proteins



Size

250 ?g

商品信息


More Information



Product Details



Synonyms

Small Ubiquitin-related Modifier 2; HSMT3; SMT3 Homolog 2; Sentrin-2; Ubiquitin-like Protein SMT3A



Product Type

Protein



Properties



Source/Host

E. coli



Sequence

Human SUMO2 K11R mutant (Accession Nr. P61956).



Crossreactivity

Human



Formulation

Liquid. In HEPES, NaCl, DTT and Glycerol.



Other Product Data


Use:
Ideal for investigating SUMO chain linkages. Prevents the modification of K11 within SUMO and/or poly-SUMO chains. Reaction conditions will need to be optimized for each specific application. We recommend an initial protein concentration of 10-50?M.



Declaration

Manufactured by Boston Biochem



Shipping and Handling



Shipping

DRY ICE



Short Term Storage

-20°C



Long Term Storage

-80°C



Handling Advice

Aliquot to avoid freeze/thaw cycles.



Use/St
ABI
lity

Stable for at least 1 year after receipt when stored at -80°C.



Documents



MSD
S

No



Product Specification Sheet



Datasheet


Download PDF





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. 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. In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p. 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. 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. 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. SUMOylation can occur without the requirement of a specific E3 ligase activity, where SUMO is transferred directly from UbcH9 to specific substrates. SUMOylated substrates are primarily localized to the nucleus (RanGAP-1, RANBP2, PML, p53, Sp100, HIPK2), but there are also cytosolic substrates (IκBα, GLUT1, GLUT4). SUMO modification has been implicated in functions such as nuclear transport, chromosome segregation, transcriptional regulation, cancer and protein st
ABI
lity. Mutation of lysine 11 to arginine renders SUMO2 unable to form poly-SUMO multimers and is useful to investigate mono-SUMOylation or can be used to reduce poly-SUMO chain formation. Human SUMO2 contains the VK11TE sequence which allows for the formation of poly-SUMO chains. K11 is the conserved lysine that becomes modified and is the point of attachment for the C-terminal glycine of the preceding SUMO2. The function of SUMO chains has not yet been fully elucidated.