Application notesIs unsuitable for Flow Cyt or IHC-P.
FunctionE3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4.
Tissue specificityHighly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung.
PathwayProtein modification; protein ubiquitination.
Immunofluorescent staining of STUB1 in HeLa cells using ab109103 at 1/100 dilution.
References for Anti-STUB1 antibody [EPR4448] (ab109103)
This product has been referenced in:
El-Kasaby A et al. A cytosolic relay of heat shock proteins HSP70-1A and HSP90ß monitors the folding trajectory of the serotonin transporter. J Biol Chem289:28987-9000 (2014).
Read more (PubMed: 25202009) »