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AB127080

Recombinant Human USP35 protein

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Recombinant Human USP35 protein is a Human Fragment protein, in the 56 to 264 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

KIAA1372, USP34, USP35, Ubiquitin carboxyl-terminal hydrolase 35, Deubiquitinating enzyme 35, Ubiquitin thioesterase 35, Ubiquitin-specific-processing protease 35

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9P2H5

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

Constituents: 0.58% Sodium chloride, 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":"23.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":264,"aminoAcidStart":56,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q9P2H5","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

USP35 also known as Ubiquitin Specific Peptidase 35 is an enzyme involved in the removal of ubiquitin from ubiquitinated proteins. It functions critically in protein degradation by interacting with the ubiquitin-proteasome system. The molecular weight of USP35 is around 119 kDa. USP35 is expressed in multiple tissues including the brain heart and testis indicating a potential for various biological functions in different organ systems.
Biological function summary

USP35 plays a role in regulating protein stability and turnover. As part of deubiquitinating enzymes (DUBs) it helps reverse the ubiquitination process that marks proteins for degradation. It contributes to maintaining protein homeostasis which is important for cell function and survival. USP35 may function as part of larger protein complexes although specific complexes have not been definitively described. Its regulatory role can impact cellular processes significantly.

Pathways

The ubiquitin-proteasome pathway involves USP35 in maintaining protein balance by removing ubiquitin chains. USP35 interacts with other DUBs as well as the proteasome system itself. It is also associated with the ER-associated degradation (ERAD) pathway which controls protein quality in the endoplasmic reticulum. USP35 interacts closely with proteins like HRD1 which is another E3 ubiquitin ligase involved in ERAD highlighting the interconnected nature of protein regulation pathways.

USP35 shows a connection to neurodegenerative disorders such as Parkinson’s disease. Dysregulation of ubiquitin-related processes can lead to an accumulation of misfolded proteins contributing to disease pathogenesis. USP35 may also have a role in cancer where its dysfunction could influence the stability of proteins that control cell growth and apoptosis. Interaction with proteins such as p53 which regulates cell cycle and apoptosis emphasizes the importance of USP35 in maintaining cellular health and preventing disease progression.

Specifications

Form

Lyophilized

Additional notes

Purified via His tag

General info

Function

Deubiquitinase that plays a role in different processes including cell cycle regulation, mitophagy or endoplasmic reticulum stress (PubMed : 26348204, PubMed : 29449677, PubMed : 37004621). Inhibits TNFalpha-induced NF-kappa-B activation through stabilizing TNIP2 protein via deubiquitination (PubMed : 26348204). Plays an essential role during mitosis by deubiquitinating and thereby regulating the levels of Aurora B/AURKB protein (PubMed : 29449677). In addition, regulates the protein levels of other key component of the chromosomal passenger complex (CPC) such as survivin/BIRC5 or Borealin/CDCA8 by enhancing their stability (PubMed : 34438346). Regulates the degradation of mitochondria through the process of autophagy termed mitophagy (PubMed : 25915564).

Sequence similarities

Belongs to the peptidase C19 family.

Post-translational modifications

Ubiquitinated by CHIP/STUB1 in an HSP90-dependent manner; leading to proteasomal degradation. This ubiquitination can be reversed through auto-deubiquitinating activity.

Product protocols

Target data

Deubiquitinase that plays a role in different processes including cell cycle regulation, mitophagy or endoplasmic reticulum stress (PubMed : 26348204, PubMed : 29449677, PubMed : 37004621). Inhibits TNFalpha-induced NF-kappa-B activation through stabilizing TNIP2 protein via deubiquitination (PubMed : 26348204). Plays an essential role during mitosis by deubiquitinating and thereby regulating the levels of Aurora B/AURKB protein (PubMed : 29449677). In addition, regulates the protein levels of other key component of the chromosomal passenger complex (CPC) such as survivin/BIRC5 or Borealin/CDCA8 by enhancing their stability (PubMed : 34438346). Regulates the degradation of mitochondria through the process of autophagy termed mitophagy (PubMed : 25915564).
See full target information USP35

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