Recombinant human UBPY/USP8 protein is a Human Full Length protein, in the 2 to 1118 aa range, expressed in Baculovirus infected Sf9, with >=70% purity and suitable for SDS-PAGE, FuncS.
P A V A S V P K E L Y L S S S L K D L N K K T E V K P E K I S T K S Y V H S A L K I F K T A E E C R L D R D E E R A Y V L Y M K Y V T V Y N L I K K R P D F K Q Q Q D Y F H S I L G P G N I K K A V E E A E R L S E S L K L R Y E E A E V R K K L E E K D R Q E E A Q R L Q Q K R Q E T G R E D G G T L A K G S L E N V L D S K D K T Q K S N G E K N E K C E T K E K G A I T A K E L Y T M M T D K N I S L I I M D A R R M Q D Y Q D S C I L H S L S V P E E A I S P G V T A S W I E A H L P D D S K D T W K K R G N V E Y V V L L D W F S S A K D L Q I G T T L R S L K D A L F K W E S K T V L R N E P L V L E G G Y E N W L L C Y P Q Y T T N A K V T P P P R R Q N E E V S I S L D F T Y P S L E E S I P S K P A A Q T P P A S I E V D E N I E L I S G Q N E R M G P L N I S T P V E P V A A S K S D V S P I I Q P V P S I K N V P Q I D R T K K P A V K L P E E H R I K S E S T N H E Q Q S P Q S G K V I P D R S T K P V V F S P T L M L T D E E K A R I H A E T A L L M E K N K Q E K E L R E R Q Q E E Q K E K L R K E E Q E Q K A K K K Q E A E E N E I T E K Q Q K A K E E M E K K E S E Q A K K E D K E T S A K R G K E I T G V K R Q S K S E H E T S D A K K S V E D R G K R C P T P E I Q K K S T G D V P H T S V T G D S G S G K P F K I K G Q P E S G I L R T G T F R E D T D D T E R N K A Q R E P L T R A R S E E M G R I V P G L P S G W A K F L D P I T G T F R Y Y H S P T N T V H M Y P P E M A P S S A P P S T P P T H K A K P Q I P A E R D R E P S K L K R S Y S S P D I T Q A I Q E E E K R K P T V T P T V N R E N K P T C Y P K A E I S R L S A S Q I R N L N P V F G G S G P A L T G L R N L G N T C Y M N S I L Q C L C N A P H L A D Y F N R N C Y Q D D I N R S N L L G H K G E V A E E F G I I M K A L W T G Q Y R Y I S P K D F K I T I G K I N D Q F A G Y S Q Q D S Q E L L L F L M D G L H E D L N K A D N R K R Y K E E N N D H L D D F K A A E H A W Q K H K Q L N E S I I V A L F Q G Q F K S T V Q C L T C H K K S R T F E A F M Y L S L P L A S T S K C T L Q D C L R L F S K E E K L T D N N R F Y C S H C R A R R D S L K K I E I W K L P P V L L V H L K R F S Y D G R W K Q K L Q T S V D F P L E N L D L S Q Y V I G P K N N L K K Y N L F S V S N H Y G G L D G G H Y T A Y C K N A A R Q R W F K F D D H E V S D I S V S S V K S S A A Y I L F Y T S L G P R V T D V A T
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Hydrolase 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 controls 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. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation (PubMed:27302062).
KIAA0055, UBPY, USP8, Ubiquitin carboxyl-terminal hydrolase 8, Deubiquitinating enzyme 8, Ubiquitin isopeptidase Y, Ubiquitin thioesterase 8, Ubiquitin-specific-processing protease 8, hUBPy
Recombinant human UBPY/USP8 protein is a Human Full Length protein, in the 2 to 1118 aa range, expressed in Baculovirus infected Sf9, with >=70% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.72% Sodium chloride, 0.71% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride
Affinity purified.
Hydrolase 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 controls 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. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation (PubMed:27302062).
Belongs to the peptidase C19 family.
Phosphorylation 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.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
UBPY also known as USP8 (ubiquitin-specific-processing protease 8) functions as a deubiquitinating enzyme. This protein removes ubiquitin from specific substrates regulating their stability and turnover. USP8 has a molecular mass of approximately 125 kDa. It is widely expressed in various tissues with higher expression levels reported in the brain liver and kidneys. The enzyme plays a significant role in protein homeostasis and cellular signaling through its deubiquitinating activity.
The deubiquitinating enzyme USP8 participates in endocytosis and lysosomal protein degradation processes. It does not function alone but associates with different protein complexes to regulate trafficking and degradation of membrane receptors. Through its action USP8 influences receptor tyrosine kinases like EGFR and impacts the sorting and degradation of these receptors. The enzyme's activity on these receptors is critical for controlling their signal transduction pathways and cellular responses.
USP8 plays a role in the EGFR signaling pathway and the Wnt pathway. In the EGFR pathway its deubiquitinating action on EGFR affects receptor degradation and recycling impacting cell growth and differentiation. Within the Wnt pathway USP8 associates with proteins such as Axin and APC contributing to the regulation of β-catenin levels. By managing these pathways USP8 controls both normal physiological processes and pathological conditions when dysregulated.
USP8 associates with conditions like Cushing's disease and certain types of cancers. Cushing's disease results from pituitary adenomas overexpressing USP8 leading to excessive adrenocorticotropic hormone (ACTH) production. In cancer the regulation of EGFR by USP8 becomes disrupted resulting in unregulated cell growth and proliferation. These disorders highlight the important role of USP8 in maintaining cellular homeostasis and the potential of targeting this enzyme for therapeutic interventions.
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4-20% SDS-PAGE analysis of ab198666 (0.5 μg) with Coomassie staining.
Example of specific activity of ab198666.
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