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商品編號


AG-40T-0248-R250



品牌


Adipogen



公司


Adipogen



公司分類


Cancer



Size

250 ?l

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 K48 residue 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. Resin supplied as a 50% slurry in 20% ethanol.



Other Product Data


Use:
Linkage-specific, non-hydrolyzable di-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.
Polyubiquitin-agarose can be re-used if properly maintained. After use, clean resin with a wash cycle of 5 volumes 100mM HEPES pH 8.0, 500mM NaCl followed by 5 volumes 100mM NaOAc pH4.5, 500mM NaCl. Repeat twice, then rinse resin with a low salt 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 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.