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商品編號


AG-40T-0367-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 1; GAP-modifying Protein 1; SMT3C, SMT3H3, UBL1; Sentrin; Ubiquitin-homology Domain Protein PIC1



Product Type

Protein



Properties



Source/Host

E. coli



Sequence

Human SUMO1 K16R/K17R mutant (Accession Nr. P63165).



Crossreactivity

Human



Formulation

Liquid. In HEPES, NaCl and DTT.



Other Product Data


Use:
SUMO1 chains do not re
ADI
ly form
in vitro
. Mutation of lysines 16 and 17 to arginine is useful to investigate mono-SUMOylation requirements or to reduce poly-SUMO chain formation. Utilizing this protein will ensure that K16 and K17-linked chains will not be formed. 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 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. 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. In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p. 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-β peptide by promoting the accumulation of BACE-1. Covalent modification of PTEN by SUMO1 is thought to regulate tum
Origen
esis by retaining PTEN at the plasma membrane, an effect that suppresses PI 3-Kinase/Akt-dependent tumor growth. Human SUMO-1 does not contain the exact ψκXE consensus sequence found in SUMO-2 and SUMO-3. Within this motif ψ represents a large hydrophobic amino acid (I, L, or V), K is the lysine that becomes modified, X is any residue and E is glutamic acid. Many known SUMO-1 conjugation sites occur within this consensus sequence, but SUMOylation also occurs on lysine residues located within non-consensus regions. SUMO-1 has been shown to form chains
in vitro
and
in vivo
but often the linkage is uncharacterized, and the function of SUMO chains has not yet been fully elucidated. SUMO-1 multimerization
in vitro
has been shown to occur predominantly via lysines K7, K16 and K17.