商品编号


AG-40T-0401-R100



品牌


Adipogen



公司


Adipogen



公司分类


Proteins



Size

100 ?l

商品信息


More Information



Product Details



Product Type

Protein



Properties



Source/Host

E. coli



Sequence

Three human ubiquitin L73P mutants (Accession Nr. P0CG47) covalently linked through isopeptide bonds at K48 residues of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule, and coupled to agarose.



Crossreactivity

Human



Label/Conjugates

Agarose



Formulation

Liquid. In 20% Ethanol.



Other Product Data


Use:
Linkage-specific, non-hydrolyzable tri-ubiquitin is resistant to the activity of deubiquitinating enzymes (DUB's) that cleave the isopeptide linkage between adjacent ubiquitin molecules. May be useful for investigating ubiquitin-binding proteins and exploring the role of unanchored (free C-terminus) ubiquitin chains in signaling pathways. Useful for the enrichment of known ubiquitin chain-interacting proteins as well as the discovery of novel ubiquitin chain-interacting proteins. We recommend equilibrating the resin by washing with 10 volumes of your desired aqueous buffer.



Declaration

Manufactured by Boston Biochem



Shipping and Handling



Shipping

BLUE ICE



Short Term Storage

+4°C



Long Term Storage

+4°C



Handling Advice

Do not freeze.



Use/St
ABI
lity

Stable for at least 3 months after receipt when stored at +4°C.



Documents



MSD
S

No



Product Specification Sheet



Datasheet


Download PDF





With a predicted molecular weight of 26 kDa, tri-ubiquitin chains are composed of three ubiquitin monomers that are covalently linked through isopeptide bonds, which typically form between a lysine residue of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin. Each human ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa sequence identity with yeast and mouse ubiquitin, respectively. Seven of the 76 aa in ubiquitin are lysine residues that can participate in poly-ubiquitin chain formation. Linkage through specific lysine residues is thought to serve as a signal that affects protein degradation, signaling, trafficking and other cellular processes.