Comparison

KIT UBI trap-A for Western-blot  European Partner

Item no. UBI-TRAP-A-WB
Manufacturer B Molecular
Amount 200 µg
Category
Type Reagents
Format Liquid
Specific against other
Conjugate/Tag GST
Purity > 95% by RP-HPLC and SDS-PAGE
Dry ice Yes
Citations (1) Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities. Hjerpe R, Aillet F, Lopitz-Otsoa F, Lang V, England P, Rodriguez MS.EMBO Rep. 2009 Nov;10(11):1250-8.
(2) Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling. Sims JJ, Scavone F, Cooper EM, Kane LA, Youle RJ, Boeke JD, Cohen RE.Nat Methods. 2012 Feb 5;9(3):303-9.
(3) Using Ubiquitin Binders to Decipher the Ubiquitin Code. Mattern M, Sutherland J, Kadimisetty K, Barrio R, Rodriguez MS.Trends Biochem Sci. 2019 Jul;44(7):599-615.
(4)Role of monoubiquitylation on the control of IκBα degradation and NF-κB activity. Da Silva-Ferrada E, Torres-Ramos M, Aillet F, Campagna M, Matute C, Rivas C, Rodríguez MS, Lang V. PLoS One. 2011;6(10):e25397.
(5) Tetramerization-defects of p53 result in aberrant ubiquitylation and transcriptional activity. Lang V, Pallara C, Zabala A, Lobato-Gil S, Lopitz-Otsoa F, Farrás R, Hjerpe R, Torres-Ramos M, Zabaleta L, Blattner C, Hay RT, Barrio R, Carracedo A, Fernandez-Recio J, Rodríguez MS, Aillet F. Mol Oncol. 2014 Jul;8(5):1026-42.
(6) Inhibition of the proteasome and proteaphagy enhances apoptosis in FLT3-ITD-driven acute myeloid leukemia. Lopez-Reyes RG, Quinet G, Gonzalez-Santamarta M, Larrue C, Sarry JE, Rodriguez MS. FEBS Open Bio. 2021 Jan;11(1):48-60.
(7) Analysis of defective protein ubiquitylation associated to adriamycin resistant cells. Lang V, Aillet F, Xolalpa W, Serna S, Ceccato L, Lopez-Reyes RG, Lopez-Mato MP, Januchowski R, Reichardt NC, Rodriguez MS. Cell Cycle. 2017;16(24):2337-2344.
(8) Activation of AHR mediates the ubiquitination and proteasome degradation of c-Fos through the induction of Ubcm4 gene expression. Mejía-García A, González-Barbosa E, Martínez-Guzmán C, Torres-Ramos MA, Rodríguez MS, Guzmán-León S, Elizondo G. Toxicology. 2015 Nov 4;337:47-57.
(9) Activation of aryl hydrocarbon receptor regulates the LPS/IFNgamma-induced inflammatory response by inducing ubiquitin-proteosomal and lysosomal degradation of RelA/p65. Domínguez-Acosta O, Vega L, Estrada-Muñiz E, Rodríguez MS, Gonzalez FJ, Elizondo G. Biochem Pharmacol. 2018 Sep;155:141-149.
(10) Efficient monitoring of protein ubiquitylation levels using TUBEs-based microarrays. Serna S, Xolalpa W, Lang V, Aillet F, England P, Reichardt N, Rodriguez MS.FEBS Lett. 2016 Aug;590(16):2748-56.
(11) New insights into host-parasite ubiquitin proteome dynamics in P. falciparum infected red blood cells using a TUBEs-MS approach. Mata-Cantero L, Azkargorta M, Aillet F, Xolalpa W, LaFuente MJ, Elortza F, Carvalho AS, Martin-Plaza J, Matthiesen R, Rodriguez MS.J Proteomics. 2016 Apr 29;139:45-59.
(12) Isolation of ubiquitylated proteins using tandem ubiquitin-binding entities. Aillet F, Lopitz-Otsoa F, Hjerpe R, Torres-Ramos M, Lang V, Rodríguez MS.Methods Mol Biol. 2012;832:173-83.
ECLASS 10.1 42051003
ECLASS 11.0 42051003
UNSPSC 12000000
Available
Description
UBI traps are used to isolate and identify ubiquitylated proteins from cells, tissues or organs. Multiple ubiquitin binding domains (UBDs) contribute to enhance their affinity for polyubiquitin chains compared to single UBD. (1-3). Prototype UBI traps interfere with the action of de-ubiquitylating enzymes (DUBs) and the proteasome which contribute to increase the yield of ubiquitylated proteins purified and facilitate the detection of low abundance proteins. These unique properties are not observed with any other technologies that can be used in a large panel of applications (3).
UBI trap-B is based on UBDs with preference for K63 linked polyubiquitin chains but other chains can also be captured (1-3). Furthermore, differences can be observed depending on the relative chain abundance in distinct cell lines and response to various treatments. GST control is provided for a single control reaction. KIT UBI trap-B contains all reagents and solutions required for the capture of Ubiquitylated proteins from cell lines, tissues and organs (see below).
Molecular Weight
55, 647 kDa
Solubility
>30 mg/mL
Concentration
Variable (5-10 mg/mL)
Storage
-80°C, avoid freeze/thaw cycles
Applications info
Pull down of poly-ubiquitylated proteins from cell and tissue lysates using glutathione beads. Captured proteins can be analyzed by Western blot or Mass spectrometry with the appropriate adaptations.
Protection of poly-ubiquitylated proteins from both deubiquitylation and degradation by the proteasome
Quantitative or semiquantitative methods using different supports.
Benefits
Up to 1000-fold higher affinity than the single UBD
Avoid overexpression of tagged ubiquitin for pull downs
Protect poly-ubiquitin chains without inhibitors specific to the proteasome or DUBs activity
Replace ubiquitin specific antibodies for enrichment of poly-ubiquitylated proteins
Examples of use
UBI trap-B can be used to detect ubiquitylated cellular factors implicated in the regulation of signaling pathways regulating inflammation, oncogenesis, neurodegenerative diseases and multiple infections (4-8). The ubiquitylated status of these factors can be followed in response to a treatment and determine if cells are responding well (9-10). The ubiquitylation of crucial cellular factors can also be followed after infection with various microorganisms (11). Among other examples. A UBI traps step by step protocol has also been reported (12).

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 200 µg
Available: In stock
available

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