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商品編號


AG-40T-0243-C050



品牌


Adipogen



公司


Adipogen



公司分類


Cancer



Size

50 ?g

商品信息


More Information



Product Details



Product Type

Protein



Properties



Source/Host

E. coli



Sequence

Two human ubiquitin (Accession Nr. P0CG47) covalently linked through an isopeptide bond at K63 residue of one ubiquitin molecule and the C-terminal glycine residue of another ubiquitin molecule and conjugated to TAMRA.



Crossreactivity

Human



Label/Conjugates

TAMRA



Formulation

Liquid. In 50mM Hepes pH 7.5, 150mM NaCl, 2mM DTT.



Other Product Data


Use:
Linkage-specific di-ubiquitin is a substrate for enzymes that cleave the isopeptide linkage between two ubiquitin molecules. This FRET-based DUB substrate with isopeptide bonds between ubiquitin moieties is superior to gel densitometry assays. Since DUBs recognize and cleave substrates with specific steric conditions, each substrate varies in the position of the fluorophore and quencher and must be empirically tested for individual enzymes. Ideal for use as a substrate for ubiquitin-specific hydrolases with activity toward K63 linkages. We recommend an assay buffer consisting of 50mM Hepes pH 7.5, 150mM NaCl, 2mM DTT. Fluorescence can be monitored with an excitation wavelength of 544nM and an emission wavelength of 572nM. Reaction conditions will need to be optimized for each specific application. We recommend an initial protein concentration of 100-500nM.



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.
Protect from light.



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





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.