小鼠单克隆抗体[5C3-1] to UBXN6
ab80659 recognizes both isoforms of UBXN6
Recombinant Human UBXN6 purified from bacteria.
- U2OS cotransfected with pBabepuro and pSuper based plasmid encoding anti
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Preservative: 0.02% Sodium Azide
Constituents: 50% Glycerol, 0.5% PBS, 0.1% BSA
Concentration information loading...
Protein A purified
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in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ICC/IF: Use at a concentration of 0.05 - 0.5 µg/ml.
IP: Use at 1-2µg/500 3µg protein extract.
WB: Use at a concentration of 0.3 µg/ml.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Acts in a complex with VCP and cooperates with USP7 in promoting MDM2 deubiquitination and stabilization. MDM2 stabilization leads to MDM2-dependent TP53 degradation.
Enhanced expression in testis.
Contains 1 PUB (PUG) domain.
Contains 1 UBX domain.
The UBX domain lacks key residues critical for VCP binding.
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Localizes at the centrosome both in interphase and during mitosis.
Information by UniProt
- UBX domain containing 1 antibody
- UBX domain containing 2 antibody
- UBX domain containing protein 1 antibody
Western blot - Anti-UBXN6 antibody [5C3-1] (ab80659)
Lanes 1-2 :
Anti-UBXN6 antibody [5C3-1] (ab80659) at 0.3 µg/ml (in PBS/Tween)Lanes 3-4 :
Ponceau S RedLanes 1 & 3 :
U2OS were co-transfected with pBabepuro
and pSuper based plasmid encoding anti-
UBXD1 shRNALanes 2 & 4 :
U2OS were co-transfected with mismatch controlObserved band size:
54 kDa (why is the actual band size different from the predicted?
)Additional bands at:
49 kDa (possible isoform)
A picture of the Ponceau S stained blot after processing is shown to demonstrate equivalent loading of protein.
has not yet been referenced specifically in any publications.
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