Abcam, ab19247, Anti-Ubiquitin antibody

Size: 100µg
Anti-Ubiquitin antibody (ab19247) is a rabbit polyclonal antibody detecting Ubiquitin in Western Blot . Suitable for Human, Mouse, Saccharomyces cerevisiae . - Over 60 publications - Trusted since 2005
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Human, Saccharomyces cerevisiae,
Applications:WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Native Full Length Protein corresponding to Cow UBB conjugated to Keyhole Limpet Haemocyanin.P0CG53,
Specificity:It can identify free ubiquitin as well as ubiquinated proteins. The antibody recognizes polyubiquitin chains more strongly than monoubiquitinated molecules.

Product details:
What is this antibody validated in?
Anti-Ubiquitin antibody (ab19247) is a rabbit polyclonal antibody and is validated for use in Western Blot (WB) in Human, Mouse, Saccharomyces cerevisiae samples.
What is the molecular weight of Ubiquitin?
Anti-Ubiquitin  (ab19247) specifically detects a band for Ubiquitin (UniProt: P0CG48) at a molecular weight of 10kDa.
Trusted by the scientific community
Anti-Ubiquitin  (ab19247) was first used in a scientific publication in 2005 and has been cited over 60 times in peer-reviewed journals.
Reviewed by scientists
Anti-Ubiquitin  (ab19247) has over 5 independent reviews from customers.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2Preservative: 0.09% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Ubiquitin is a small regulatory protein found in almost all tissues of eukaryotic organisms. It has a molecular weight of approximately 8.6 kilodaltons. It functions mechanically by attaching to proteins through a process called ubiquitination which involves the formation of an isopeptide bond. Ubiquitin molecules can form polyubiquitin chains through different lysine residues such as K48 and K63 that determine their function. These chains label substrate proteins for various fates including degradation. Ubiquitin is expressed ubiquitously in cells reflecting its essential role in maintaining protein homeostasis.
Biological function summary
The ubiquitin system plays a critical role in regulating protein turnover and quality control within cells. It is part of a larger complex known as the ubiquitin-proteasome system (UPS) which is responsible for degrading proteins that need to be turned over. This process is essential for cell cycle control response to oxidative stress and DNA repair. Ubiquitin's role in tagging proteins for degradation or signaling allows cells to respond quickly to changes in their environment and maintain balance.
Pathways
Ubiquitin functions in several important biological pathways including the Wnt and NF-kB pathways. In the Wnt signaling pathway ubiquitination modulates the stability of key components thereby affecting the pathway's overall activity. In the NF-kB signaling pathway ubiquitin labels inhibitor proteins for degradation which releases and activates NF-kB. These pathways highlight ubiquitin's interaction with proteins such as beta-catenin in Wnt and IkB in NF-kB illustrating how it regulates diverse cellular processes.
The dysfunction of the ubiquitin system is linked to neurodegenerative diseases and cancers. Ubiquitin-related defects in protein degradation can lead to the buildup of unwanted proteins contributing to conditions like Parkinson's disease. Connections with cancer are evident as ubiquitin controls cell cycle proteins and aberrant ubiquitination may drive tumor growth and progression. The protein p53 known to be controlled by ubiquitination plays a significant role in cancer related mechanisms when dysregulated. Understanding and targeting ubiquitin-related pathways may provide new therapeutic opportunities for treating these conditions.