Analytical Data
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Gene name
hcp1
- Application
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Alternative Names
hcp1；G21；HCP1；PCFT；Proton-coupled folate transporter
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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
Q9I747
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Expression Region
24.9 kDa
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AA Sequence
MAVDMFIKIGDVKGESKDKTHAEEIDVLAWSWGMSQSGSMHMGGGGGAGKVNVQDLSFTKYIDKSTPNLMMACSSGKHYPQAKLTIRKAGGENQVEYLIITLKEVLVSSVSTGGSGGEDRLTENVTLNFAQVQVDYQPQKADGAKDGGPVKYGWNIRQNVQA
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Molecular Weight
24.9 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
HCP1 (Human Copper Transporter 1) is a vital protein involved in the regulation of copper homeostasis in the body. Research on HCP1 has gained prominence due to the critical role copper plays in various biological processes, including enzymatic reactions, oxidative stress response, and mitochondrial function. Dysregulation of copper transport can lead to pathological conditions such as Wilson's disease and Menkes disease, both of which are associated with severe neurological and developmental issues. Understanding the molecular structure and function of HCP1 is essential for elucidating its role in copper metabolism and its implications in disease states. Recent advancements in recombinant protein technology have enabled the production of HCP1 in significant quantities, facilitating in-depth studies of its biochemical properties and interactions. The ability to characterize HCP1 using techniques such as X-ray crystallography and NMR spectroscopy will provide insights into its mechanism of action and potential as a therapeutic target. Additionally, the study of HCP1 may reveal new avenues for drug development aimed at correcting copper transport dysregulation, thus contributing to the treatment of related disorders. As research progresses, HCP1 is emerging as an important player in the field of molecular biology and medicine, underscoring the necessity for further exploration of its functions and therapeutic potential.
