商品编号


AG-40T-0562-C050



品牌


Adipogen



公司


Adipogen



公司分类


Proteins



Size

50 ?g


商品信息


More Information



Product Details



Synonyms

Ubiquitin C-terminal Hydrolase 22; Deubiquitinating Enzyme 22; Ubiquitin Thioesterase 22; Ubiquitin-specific-processing Protease 22



Product Type

Protein



Properties



Source/Host

Sf21 cells



Sequence

Human
USP
22 (Accession Nr. AAI26899.1) fused to N-terminal His-tag.



Crossreactivity

Human



MW

~60kDa



Purity

≥95% (SDS-PAGE)



Accession Number

AAI26899.1



Formulation

Liquid. In 50mM HEPES pH 7.5, 100mM NaCl, 10% Glycerol (v/v) and 2mM TCEP.



Other Product Data


Use:
Ubiquitin-specific deconjugating enzyme. Reaction conditions will need to be optimized for each specific application. We recommend an initial protein concentration of 20-100nM when using Ubiquitin (human) (rec.) (AMC) (AG-40T-0459MC) or Ubiquitin (human) (rec.) (Rhodamine) (AG-40T-0459RH) as substrate.
Note:
Recombinant human
USP
22 is not active toward poly-Ubiquitin chains, ubiquitinated histones and other ubiquitinated protein substrates in the absence of adapter proteins such as ATXN7L or ENY2.



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


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Product Specification Sheet



Datasheet


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USP
22 is a member of the SAGA (Spt-Ada-Gcn5 acetyltransferase) complex, a 2 MDa protein machine that mediates the acetylation and deubiquitination of histones as well as non-histone substrates. Within SAGA,
USP
22 binds directly with ATXN7L3 and provides the activity required to deubiquitinate mono-ubiquitinated histone H2B.
USP
22 is required for nuclear receptor-mediated transactivation and cell cycle progression. Recent findings suggest
USP
27X and
USP
51, which function independently of SAGA may compete with
USP
22 for ATXN7L3 and ENY2 binding, and that imbalances in these activities may contribute to human diseases including cancer.