Analytical Data
-
Gene name
RPH3AL
- Application
-
Alternative Names
No C2 domains proteinRabphilin-3A-like protein
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UNE2
-
Expression Region
1-315aa
-
Molecular Weight
50.5 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
RPH3AL, a member of the RPH3 protein family, has garnered considerable attention in recent years due to its potential roles in neuronal function and disease mechanisms. This protein is implicated in synaptic vesicle trafficking and neurotransmitter release, processes that are crucial for effective communication between neurons. Research has identified RPH3AL as a key player in the regulation of synaptic plasticity, which underlies learning and memory. Additionally, mutations or dysregulation of RPH3AL have been linked to neurodegenerative disorders and various psychiatric conditions, highlighting its relevance in neuroscience. Comparative studies across different species suggest evolutionary conservation of its function, indicating its fundamental role in brain physiology. Given the increasing prevalence of neuropsychiatric diseases globally, understanding the molecular mechanisms of RPH3AL could pave the way for novel therapeutic strategies. As such, the study of RPH3AL not only enhances our knowledge of basic neural functions but also opens avenues for addressing critical health challenges associated with neuronal dysfunction.











