Analytical Data
-
Gene name
MINDY2
- Application
-
Alternative Names
FAM63B; KIAA1164
-
Species
Human
-
Source
E. coli
-
Tag
GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8NBR6-1
-
Expression Region
S241-V504
-
Protein Length
Partial
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
MINDY2, a member of the MINDY family of proteins, plays a crucial role in cellular processes, particularly in the degradation of misfolded proteins through the ubiquitin-proteasome pathway. This protein is characterized by its unique domain architecture, which includes a Zf-C3HC4 type RING finger, suggesting its involvement in ubiquitin ligase activity. Aberrations in proteostasis, including the accumulation of misfolded proteins, are linked to various diseases, such as neurodegenerative disorders and certain cancers. Recent studies have highlighted the significance of MINDY2 in mediating the autophagic degradation of substrates, thereby maintaining cellular homeostasis. The exploration of MINDY2's functional mechanisms could provide insights into its potential as a therapeutic target for diseases characterized by protein misfolding and aggregation. As researchers continue to elucidate the biological functions and regulatory networks associated with MINDY2, its implications in health and disease contexts become increasingly apparent, marking it as a promising candidate for future investigations. Understanding the role and regulation of MINDY2 could pave the way for novel therapeutic strategies aimed at enhancing proteostasis and combating associated pathologies.
