Analytical Data
-
Gene name
MELT
- Application
-
Alternative Names
MELT；KIAA1692；VEPH；Ventricular zone-expressed PH domain-containing Protein homolog 1
-
Species
Apis mellifera carnica
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01501
-
Expression Region
44-69aa
-
AA Sequence
GIGAVLKVLTTGLPALISWIKRKRQQ
-
Molecular Weight
2.8 kDa
-
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
MELT (Mediating E3 Ligase Targeting) is a novel protein domain characterized by its ability to facilitate the interaction between E3 ubiquitin ligases and their substrates, playing a crucial role in the regulation of various cellular processes, including protein degradation, cell cycle control, and stress responses. The study of MELT-containing proteins has gained attention due to their involvement in critical signaling pathways and their potential implications in cancer and other diseases. Recent research has revealed that the MELT domain often serves as a molecular hub, coordinating multiple protein-protein interactions that modulate cellular functions. Understanding the structural and functional dynamics of MELT proteins can offer insights into their roles in pathological conditions, paving the way for targeted therapeutic approaches. The exploration of MELT domain-restricted interactions is particularly vital for dissecting the mechanisms underlying aberrant E3 ligase activity in malignancies, where dysregulation of ubiquitin-proteasome pathways is frequently observed. As such, ongoing studies aim to delineate the interactions and regulatory networks involving MELT proteins, contributing to a deeper comprehension of cellular homeostasis and the development of novel strategies for intervention in diseases marked by proteolytic dysregulation.
