Sumo1 (Small Ubiquitin-related Modifier) (human) (rec.)

CHF 358.00
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YIF-LF-P03260.5 mgCHF 358.00
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Product Details
Synonyms GMP1; SMT3C; SUMO1; Smt3C; SUMO-1; Sentrin; SMT3 Homolog 3; GAP-modifying Protein 1; Ubiquitin-like Protein UBL1; Ubiquitin-like Protein SMT3C; Small Ubiquitin-related Modifier 1; Ubiquitin-Homology Domain Protein PIC1
Product Type Protein
Source/Host E. coli
Crossreactivity Human
Biological Activity

Activity has not been tested.

Purity ≥95% (SDS-PAGE)
Formulation Lyophilized from 20mM Tris, pH 8.0 / 10mM NaCl.
Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability After reconstitution, store at -80°C.
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Product Specification Sheet
Datasheet Download PDF

The small ubiquitin-related modifier (SUMO) belongs to the growing family of ubiquitin-related proteins involved in posttranslational protein modification. It is present in all eukaryotic kingdoms and is highly conserved from yeast to humans. The SUMO family are composed of three types; SUMO1, SUMO2 and SUMO3. Like ubiquitin, SUMO1 is conjugated to target proteins by an enzymatic cascade involving E1, E2 enzyme and E3 lygase (known as sumoylation). It has been known that many substrates such as RanGAP1, PML and IkBa proteins are present in cells. In contrast to ubiquitination, sumoylation does not tag proteins for degradation by the 26S proteosome. Sumoylation participates in diverse events such as nuclear transport, transcriptional regulation, chromosome segregation and cell cycle control. Also the modification is associated with pathological conditions (neurodegeneration, diabetes and Inflammation).

Product References

1) Muller S. et al., (2001) Nat Rev Mol Cell Biol. 2:202-210. (General)
2) Gill G, (2004) Genes Dev. 18(17):2046-2059. (General)
3) Hay RT, (2005) Mol Cell. 18(1):1-12. (General)
4) Degerny C et al., (2005) J Biol Chem. 280(26):24330-24338. (General)

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