Analytical Data
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Gene name
NHE1
- Application
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Alternative Names
NHE1；APNH1；NHE1；Sodium/hydrogen exchanger 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P19634
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Expression Region
31-130aa
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AA Sequence
VLRSHGLQLSPTASTIRSSEPPRERSIGDVTTAPPEVTPESRPVNHSVTDHGMKPRKAFPVLGIDYTHVRTPFEISLWILLACLMKIGFHVIPTISSIVP
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Molecular Weight
36 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
The NHE1 (sodium-hydrogen exchanger 1) protein is a crucial membrane transporter involved in maintaining cellular pH and sodium homeostasis, playing a vital role in various physiological and pathological processes. Research on NHE1 has gained significance due to its implications in cardiovascular health, cancer progression, and neurodegenerative disorders. Altered NHE1 activity can lead to pathological conditions such as hypertension, heart failure, and tumor proliferation, making it an attractive target for therapeutic intervention. Recombinant NHE1 proteins have been developed to better understand its structure-function relationships and to facilitate the exploration of its regulatory mechanisms. Studies utilizing these recombinant proteins assist in identifying the specific molecular interactions and pathways involved in NHE1 regulation, as well as its role in cellular signaling. Moreover, the characterization of NHE1 can lead to the development of selective inhibitors that could provide novel treatment strategies for diseases associated with dysregulated ion homeostasis. As such, ongoing research in the area of NHE1 recombinant proteins holds promise for advancing our understanding of its biological roles and therapeutic potential.
