Analytical Data
-
Gene name
FXYD3
- Application
-
Alternative Names
FXYD3；MAT8；PLML；FXYD domain-containing ion transport regulator 3
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q14802
-
Expression Region
21-38aa
-
AA Sequence
NDLEDKNSPFYYDWHSLQ
-
Molecular Weight
20.5 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
FXYD3, a member of the FXYD gene family, encodes a small glycoprotein that plays a critical role in the regulation of ion transport and homeostasis, particularly in epithelial tissues. Research has shown that FXYD3 interacts with the Na+/K+ ATPase, influencing its activity and stability, which is essential for maintaining the electrochemical gradients across cell membranes. This modulation of Na+/K+ ATPase not only affects cellular excitability but also impacts various physiological processes, including muscle contraction and neuronal signaling. Alterations in FXYD3 expression have been implicated in several pathological conditions, including cardiac diseases, renal dysfunction, and certain types of cancer. Understanding the molecular mechanisms underlying FXYD3's function and its potential as a biomarker or therapeutic target is of great interest. Recent studies involve the generation of recombinant FXYD3 proteins to elucidate their structural properties and interactions with other proteins. Such research is pivotal for advancing our knowledge of ion transport mechanisms and developing novel strategies for disease intervention, highlighting FXYD3 as a vital component in the landscape of biomedical research.
