Analytical Data
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Gene name
TRPV6
- Application
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Alternative Names
CAT1; CATL; ABP/ZF; ECAC2; ZFAB; Epithelial Calcium Channel 2; CaT-like; Calcium transport protein 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H1D0
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Expression Region
Met618~Ile765
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Molecular Weight
18&21kDa
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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
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Protein Description
TRPV6 (Transient Receptor Potential Vanilloid 6) is a calcium-permeable ion channel belonging to the TRP channel family, which plays a crucial role in various physiological processes, including calcium homeostasis, cellular signaling, and epithelial function. As a highly selective channel for calcium ions, TRPV6 is particularly significant in the absorption of calcium in the intestine and reabsorption in the kidneys. Its expression levels are notably elevated in several cancers, making it a potential biomarker and therapeutic target. Research into TRPV6 recombinant proteins has gained momentum due to their relevance in understanding the molecular mechanisms underlying calcium transport and the channel's involvement in pathophysiological conditions. To facilitate this, recombinant TRPV6 proteins can be expressed, purified, and characterized, providing valuable insights into their structure-function relationships. Furthermore, these studies can help identify small molecules or peptides that modulate TRPV6 activity, paving the way for novel therapeutic strategies in conditions such as osteomalacia or cancer. This multifaceted research endeavor not only enhances our understanding of calcium signaling pathways but also opens potential avenues for drug development targeting TRPV6, thereby emphasizing the significance of this ion channel in both basic and translational research.
