Product nameAnti-UBPY/USP8 antibody
See all UBPY/USP8 primary antibodies
DescriptionRabbit polyclonal to UBPY/USP8
Tested applicationsSuitable for: WB, IP, IHC-P, ICC/IFmore details
Species reactivityReacts with: Mouse, Human
Predicted to work with: Rhesus monkey
Recombinant fragment within Human UBPY/USP8 (internal sequence). The exact sequence is proprietary.
Database link: P40818
- ICC/IF: A549 cells. IHC-P: Human colon carcinoma tissue. WB: NCI-H1299 and HCT-116 whole cell lysate. IP: HCT-116 whole cell extracts.
Storage bufferpH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: PBS, 1% BSA, 20% Glycerol
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab228572 in the following tested applications.
|WB||1/1000 - 1/10000. Predicted molecular weight: 128 kDa.|
|IP||1/100 - 1/500.|
|IHC-P||1/100 - 1/1000.|
|ICC/IF||1/100 - 1/1000.|
FunctionHydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1.
Sequence similaritiesBelongs to the peptidase C19 family.
Contains 1 MIT domain.
Contains 1 rhodanese domain.
Contains 1 USP domain.
DomainThe MIT domain is required for endosomal localization, CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR degradation.
The rhodanese domain is sufficient for RNF41-binding.
modificationsPhosphorylation of Ser-718 is essential for interaction with YWHAE and for cytosol localization. Undergoes dephosphorylation at Ser-718 in the M phase. Tyrosine-phosphorylated in its N-terminal half in an EGFR-dependent manner.
Ubiquitinated. Inactive form is mostly monoubiquitinated, but polyubiquitination happens too. Ubiquitination is increased in EGF-stimulated cells. Ubiquitination of active form is undetectable, suggesting a possibility that USP8 deubiquitinates itself, thereby regulating its own function.
Cellular localizationCytoplasm. Nucleus. Endosome membrane. Cell membrane.
- Information by UniProt
- Deubiquitinating enzyme 8 antibody
- FLJ34456 antibody
- hUBPy antibody
All lanes : Anti-UBPY/USP8 antibody (ab228572) at 1/5000 dilution
Lane 1 : NCI-H1299 (human lung carcinoma cell line) whole cell lysate
Lane 2 : HCT-116 (human colorectal carcinoma cell line) whole cell lysate
Lysates/proteins at 30 µg per lane.
Developed using the ECL technique.
Predicted band size: 128 kDa
A549 (human lung carcinoma cell line) cells stained for UBPY/USP8 (green) using ab228572 (1/500 dilution) in ICC/IF. Cells were fixed in 4% paraformaldehyde at RT for 15 minutes. Counterstain: Hoechst 33342 (blue).
Paraffin-embedded human colon carcinoma tissue stained for UBPY/USP8 with ab228572 at 1/500 dilution in immunohistochemical analysis.
UBPY/USP8 was immunoprecipitated from HCT-116 (human colorectal carcinoma cell line) whole cell extract using 5 µg of ab228572. Western blot was performed from the immunoprecipitate using ab228572.
Lane 1: HCT-116 whole cell extract (Input).
Lane 2: Control IgG IP in HCT-116 whole cell extract.
Lane 3: ab228572 IP in HCT-116 whole cell extract.
ab228572 has not yet been referenced specifically in any publications.