商品编号


AG-40T-0246-C025



品牌


Adipogen



公司


Adipogen



公司分类


Cancer



Size

25 ?g

商品信息


More Information



Product Details



Product Type

Protein



Properties



Source/Host

E. coli



Sequence

Two human ubiquitin L73P mutants (Accession Nr. P0CG47) covalently linked through an isopeptide bond at K11 residue of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule.



Crossreactivity

Human



Formulation

Lyophilized.



Other Product Data


Use:
Linkage-specific, non-hydrolyzable di-ubiquitin is resistant to the activity of enzymes (DUB’s) that cleave the isopeptide linkage between adjacent ubiquitin molecules. It can be used to investigate binding interactions between di-ubiquitin and proteins that contain elements such as ubiquitin-associated domains (UBAs) or ubiquitin-interacting motifs (UIMs) and exploring the role of unanchored (free C-terminus) ubiquitin chains in signaling pathways.
BIOLOG
ical roles of K11-linked polyubiquitin are less understood than K48- or K63-linked ubiquitin chains, though recent evidence points to a role for K11 linkages in the degradation of the anaphase-promoting complex (APC/C), and in TNFα-stimulated NF-κB activation. Typical concentrations will depend on specific assay conditions and method of detection.



Declaration

Manufactured by Boston Biochem



Shipping and Handling



Shipping

BLUE ICE



Short Term Storage

+4°C



Long Term Storage

-20°C



Handling Advice

Aliquot to avoid freeze/thaw cycles.



Use/St
ABI
lity

Stable for at least 1 year after receipt when stored at -20°C.



Documents



MSD
S

No



Product Specification Sheet



Datasheet


Download PDF





With a predicted molecular weight of 17 kDa, di-ubiquitin is composed of two ubiquitin monomers that are covalently linked through an isopeptide bond, which typically form between a lysine residue of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule. Each human ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa identity with yeast and mouse ubiquitin, respectively. Ubiquitin has seven lysine residues that can participate in the formation of poly-ubiquitin chains. The specific lysine residue used in ubiquitin conjugation is thought to determine the function of poly-ubiquitination in cellular processes such as protein degradation, signaling and trafficking.