商品编号


AG-40T-0245-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 monomers (Accession Nr. P0CG47) covalently linked through the N-terminal amino group of methionine (Met1-linked) on one ubiquitin that is conjugated with the C-terminal carboxy group of another ubiquitin.



Crossreactivity

Human



MW

~17kDa



Purity

≥95% (SDS-PAGE)



Concentration

1mg/ml



Formulation

Liquid. In sterile, deionized water.



Other Product Data


Use:
Formed with wild-type human recombinant ubiquitin and linkage-specific enzymes. Validated by Ub-AQUA, an LCMS-based technique that provides extremely accurate information on the composition of Poly-ubiquitin samples. Ideal for investigating ubiquitin-binding proteins and as substrates for ubiquitin-specific isopeptidases. Reaction conditions will need to be optimized for each specific application.
IMPORTANT:
Heating this product in SDS-PAGE buffer or terminating reactions containing this product with heated SDS-PAGE buffer could lead to unexpected, high apparent molecular weight banding or smearing on gels that is not representative of product purity. For optimal results, we recommend incubation in SDS-PAGE buffer + DTT at <40°c for="" 20="" minutes="" prior="" to="" gel="" electrophoresis.="">40°c>



Declaration

Manufactured by Boston Biochem



Shipping and Handling



Shipping

DRY ICE



Short Term Storage

-20°C



Long Term Storage

-80°C



Handling Advice

Avoid freeze/thaw cycles.



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. The so-called linear ubiquitin chains have a linkage between the N-terminal amino group of methionine on one ubiquitin that is conjugated with the C-terminal carboxy group of the incoming ubiquitin. 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. Ubiquitin is not expressed directly as free ubiquitin but rather as linear fusions either to itself or to certain ribosomal protein subunits. These ubiquitin-fusion precursors are proteolyzed by deubiquitinating enzymes (DUBs) at the appropriate junction points to yield active ubiquitin monomers with C-termini ending in GG. There are likely several intracellular DUBs which perform this essential processing role.