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商品編號(hào)


AG-40T-0377B-C050



品牌


Adipogen



公司


Adipogen



公司分類


Proteins



Size

50 ?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 (Accession Nr. P61956) conjugated to biotin.



Crossreactivity

Human



Label/Conjugates

Biotin



Formulation

Liquid. In 50mM Hepes pH 7.5, 100mM NaCl.



Other Product Data


Use:
Modified with biotin via primary amine coupling results in modification of lysine residues as well as the N-terminus. Although having a fully functional C-terminus, lysine modification may limit the
ABI
lity of this reagent to propagate poly-SUMO chains. Can be detected using avidin-linked reagents for higher efficiency and sensitivity than with antibodies. Depending on experimental conditions and detection method, suggested
in vitro
concentrations for thiolester formation is 5-20μM.



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.