Lifesensors
HOME    |    SITEMAP    |    VIEW CART    |    SEARCH >  
ABOUT US      CONTACT US
PRODUCTS         SERVICES      |       RESEARCH
LifeSensors - Expression Systems

UBIQUITIN RESEARCH TOOLS

Ubiquitin (Ub), a small (76 amino acids) polypeptide, is highly conserved among all living eukaryotes. Ubiquitin is covalently attached to cellular proteins and can regulate the levels, activity and localization of these proteins. Several ubiquitin-like proteins have been identified including SUMO, NEDD8 and ISG15. All of these UBLs utilize a similar mechanism for conjugation to target proteins. Briefly, energy is required to activate ubiquitin at its carboxy terminus; activation is catalysed by E1, which binds the Ub C-terminus to a side chain cysteine of the enzyme. The second enzyme of the series, E2 (called the ubiquitin conjugating protein), receives Ub as a thioester (Ub-CO-S-E1 - Ub-CO-S-E2); E2 then transfers Ub to a target polypeptide, which is bound to the third enzyme in the sequence, called E3, or Ubiquitin ligase. Thus, the E3 primarily determines the specificity of ubiquitylation. Poly-Ub chains can be formed via linkage of another Ub moiety to lysine 48 of the previous Ub protein. Other lysines may also serve as linkage sites in chain formation including lysine 63. It is important to note that not every Ub attachment results in formation of a poly-Ub tag. Attachment of a single Ub moiety to its target protein can modulate activity or localization. Ubiquitin is cleaved from substrates by deubiquitylating enzymes (also called ubiquitin hydrolases or ubiquitin isopeptidases). Isopeptidases are a family of cysteine proteases that specifically cleave ubiquitin-derived substrates of the general structure ubiquitin-X, where X = any number of leaving groups ranging from small thiols and amines to ubiquitin and other proteins. Thus, isopeptidases act to reverse the modification of proteins by ubiquitin or ubiquitin-like proteins. Modulation of cellular processes can be controlled by regulating protein ubiquitylation via modulation of E3 ligase and isopeptidase activity.
Fig 1. Ubiquitin conjugation pathway. Protein modification by ubiquitin requires sequential action of three enzymes: Ubiquitin activated by a specific activating enzyme (E1) to form a Ub-E1-thiolester. Activated Ub is transferred to a carrier protein or 'conjugase' E2, and then transferred to a ligase (E3) and linked via isopeptide bond to a lysine residue on the substrate protein. After linkage of Ub to the substrate, a polyUb chain can be formed in some cases. Ubiquitylated proteins can be deubiquitylated by specific isopeptidases.


LifeSensors has the largest collection of ubiquitin research tools commercially available for studying the enzymes involved in this complex pathway. Using these tools scientists will be able to characterize enzyme function, identify substrates, discover modulators of this pathway, and make scientific breakthroughs that will deepen our understanding of the ubiquitin pathway.


LifeSensors News

NEED HELP?

LifeSensors News
 
SPEAK RIGHT NOW
TO A SALES OR TECHNICAL HELP REPRESENTATIVE


To speak with a scientist about your specific requirements or to order over the phone,
please call...

610.644.8845


International: +1.610.644.8845 or email us directly.
 
LifeSensors News LifeSensors News
LifeSensors News

HEADLINES

LifeSensors News
 
LifeSensors' Gender Sorting Technology Discussed
Feb 9th 2010 | From The Economist online
Dr Butt’s new device is an oestrogen sniffer. It relies on the fact that female embryos produce this hormone in quantity and male ones do not. The sensor uses a fine needle to penetrate both the shell and the allantoic sac of an egg. This sac is a fluid-filled membrane that cushions the embryo and helps it trade carbon dioxide for oxygen from the air. (It is also the membrane that can make peeling a hard-boiled egg such a frustrating affair.)
Visit Site >>
LifeSensors

LifeSensors Publishes in Journal of Animal Science
2010 Jan 15.
An estrogen sensor for poultry gender sorting.

Tran HT, Ferrell W, Butt TR.

The need for segregation of poultry based on sex is driven by gender-related differences in growth rate, market age, management practices, and nutritional requirements. Each day, global poultry industry staff would ideally like to determine the gender of >150 million newly hatched birds. Currently, this can be done only manually at the hatchery, which is a virtually impossible undertaking. LifeSensors has developed a facile, rapid, and low cost yeast-based assay that distinguishes male from female embryonated eggs before hatching based on the estrogen level of their allantoic fluid.
Visit Site >>
LifeSensors

LifeSensors Launches New Website
LifeSensors launched its new website on October 9th, 2009. The new site will allow researchers all over the world to learn more about what has made LifeSensors' SUMO fusion technologies and novel ubiquitin research tools successful.
Read More >>
 
LifeSensors News READ ALL HEADLINES > LifeSensors News

EXPRESSION SYSTEMS

UBIQUITIN RESEARCH TOOLS
LifeSensors

LIFESENSORS
EXPRESSION SYSTEMS   •    UBIQUITIN RESEARCH TOOLS   •    SERVICES   •    RESEARCH                ABOUT US   •    CONTACT US   •    CAREERS
271 Great Valley Parkway   Malvern, PA 19335     [P] 610.644.8845    [F] 610.644.8616     info@lifesensors.com
©2009 LifeSensors Inc. All Rights Reserved.        Privacy Policy | Terms & Conditions | Sitemap