Recombinant Human Phospho-Ubiquitin (S65) Protein, CF

R&D Systems | Catalog # U-102

R&D Systems
Loading...

Key Product Details

  • R&D Systems E. coli-derived Recombinant Human Phospho-Ubiquitin (S65) Protein (U-102)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession Number

Applications

Bioactivity
Loading...

Product Specifications

Source

E. coli-derived human Ubiquitin protein
Met1 - Gly76
Phosphorylated on Ser 65.

Purity

>98%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Predicted Molecular Mass

8.6 kDa

Activity

Reaction conditions will need to be optimized for each specific application.

Reviewed Applications

Read 1 review rated 5 using U-102 in the following applications:

Formulation, Preparation, and Storage

U-102
Formulation Supplied as a solution in HEPES.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Ubiquitin

Serine/Threonine kinase PINK1 (PTEN-induced putative kinase protein 1) plays a critical role in preventing mitochondrial dysfunction during cellular stress. PINK is translated in the cytosol, then translocated to the outer mitochondrial membrane where it is rapidly cleaved and degraded as a part of normal mitochondrial function. In damaged (depolarized) mitochondria PINK becomes stabilized and accumulates, resulting in the subsequent phosphorylation of numerous proteins on the mitochondrial surface including Mfn2.  Ultimately PARK2 (E3 Ubiquitin Ligase Parkin) is recruited to the damaged mitochondria where it is activated by PINK-mediated phosphorylation of PARK2 at serine 65, and PARK2 interaction with phosphorylated Ubiquitin (also phosphorylated by PINK on serine 65). This signaling cascade is critical for clearing the damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PARK2.


References

  1. Matsuda N. et al. (2010) J. Cell Biol. 189: 211.
  2. Kane L.A. et al. (2014) J. Cell Biol. 205:143.
  3. Ordureau A. et al. (2014) Mol Cell. 56: 360.
  4. Vives-Bauza C. et al. (2010) Proc. Natl. Acad. Sci. 107: 378.
  5. Wall C.E. et al. (2019) Cell Reports  29: 3280.
  6. Wauer T. et al. (2015) EMBO J. 34: 307.

Alternate Names

UBB

Entrez Gene IDs

7314 (Human); 298693 (Rat)

Gene Symbol

UBB

UniProt

Additional Ubiquitin Products

Product Documents for Recombinant Human Phospho-Ubiquitin (S65) Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot or batch number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Phospho-Ubiquitin (S65) Protein, CF

For research use only

Citations for Recombinant Human Phospho-Ubiquitin (S65) Protein, CF

Customer Reviews for Recombinant Human Phospho-Ubiquitin (S65) Protein, CF (1)

5 out of 5
1 Customer Rating
5 Stars
100%
4 Stars
0%
3 Stars
0%
2 Stars
0%
1 Stars
0%

Have you used Recombinant Human Phospho-Ubiquitin (S65) Protein, CF?

Submit a review and receive an Amazon gift card!

$25/€18/£15/$25CAN/¥2500 Yen for a review with an image

$10/€7/£6/$10CAN/¥1110 Yen for a review without an image

Submit a review
Amazon Gift Card

Customer Images


Showing  1 - 1 of 1 review Showing All
Filter By:
  • Recombinant Human Phospho-Ubiquitin (S65) Protein, CF
    Name: Anonymous
    Application: ELISA
    Verified Customer | Posted 01/16/2025
    Recombinant Human Phospho-Ubiquitin (S65) Protein, CF U-102

There are no reviews that match your criteria.

Showing  1 - 1 of 1 review Showing All

FAQs

No product specific FAQs exist for this product.

View all FAQs for Proteins and Enzymes
Loading...