Storage instructionsShipped at 4°C. Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Storage bufferpH: 7.00
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 1.21% Tris, 0.75% Glycine, 20% Glycerol
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab153853 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500 - 1/3000. Predicted molecular weight: 34 kDa.|
|IHC-P||1/100 - 1/1000. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol. Alternatively Tris-EDTA buffer (pH8.0) may be used.|
FunctionSubstrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranlocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. Also involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to insure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication.
PathwayProtein modification; protein ubiquitination.
Sequence similaritiesContains 1 F-box domain.
Contains 1 FBA (F-box associated) domain.
- Information by UniProt
- F box protein that recognizes sugar chains 2 antibody
- F box G domain protein 2 antibody
- F box only protein 6 antibody
ab153853 has not yet been referenced specifically in any publications.