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商品編號


AG-40T-0361-C050



品牌


Adipogen



公司


Adipogen



公司分類


Proteins



Size

50 ?g

商品信息


More Information



Product Details



Synonyms

SUMO1 Activating Enzyme E1; SUA1; SAE1; UBA2; RHC31; E1 Ubiquitin-activating Protein AOS1



Product Type

Protein



Properties



Source/Host

E. coli



Sequence

Yeast SUMO E1 (Accession Nr. P52488) fused to a N-terminal GST-tag.



Crossreactivity

Yeast



Formulation

Liquid.



Other Product Data


Use:
Member of the SUMO-activating (E1) enzyme family that is required for the first step of the enzymatic cascade that subsequently utilizes a SUMO-conjugating (E2) enzyme to conjugate SUMO to substrate proteins. A SUMO ligase (E3) is sometimes utilized for SUMO conjugation, but is not always required. Reaction conditions will need to be optimized for each specific application. We recommend an initial protein concentration of 50-500nM.



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





SUMO Activating Enzyme Subunit 1 (SAE1) is the highly conserved human ortholog of yeast ubiquitin-activating enzyme E1-like (UBA2). These SUMO-activating (E1) enzymes are critical for the enzymatic attachment of SUMO molecules to a target protein by a post-translational modification process termed SUMOylation. The ATP-dependent E1 enzyme charges the SUMO by forming a high-energy thiol ester intermediate which is transferred to the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme. The second step is the trans-esterification reaction whereby SUMO is transferred to Cys93 of UbcH9. UBE2I/Ubc9 is the only known E2 that is able to mediate the conjugation of SUMO to lysine residues on a variety of cellular targets, usually in the absence of a ubiquitin ligase (E3). Although UBE2I/Ubc9 can directly recognize and modify lysine residues contained in a SUMOylation motif, E3-like factors most likely facilitate the SUMOylation of specific substrates. Conjugation of the ubiquitin-like modifier SUMO requires the activities of the heterodimeric E1 (Aos1/Uba2) and the UbcH9 E2 enzyme. The dimeric activating enzyme utilizes ATP to adenylate the C-terminal glycine residue of SUMO-1 (also SUMO-2 and SUMO-3), forming a high-energy thiolester bond with the cysteine residue of Uba2 and the release of AMP and PPi. The second step is the trans-esterification reaction whereby SUMO-1 is transferred to Cys93 of UbcH9.