Analytical Data
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Gene name
hcp1
- Application
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Species
Pseudomonas aeruginosa
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Source
E. coli
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Tag
N- His & C- Myc
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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
1-162aa
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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, or high-affinity cation transporter 1, is a critical protein involved in the transport of essential metal ions across cellular membranes, particularly in plants and some microorganisms. Its role in metal ion homeostasis is vital for various biological processes, including nutrient uptake, stress response, and cellular signaling. Research into HCP1 recombinant proteins has gained momentum due to their potential applications in agriculture and biotechnology. Understanding the functional mechanisms of HCP1 can provide insights into how plants manage metal ion concentrations, which is crucial in mitigating the effects of metal toxicity and improving nutrient bioavailability in crops. Additionally, HCP1’s ability to transport specific cations makes it an attractive target for engineering plant varieties with enhanced resistance to metal stress or increased nutrient efficiency. Recent advances in molecular biology techniques have facilitated the production of HCP1 recombinant proteins, allowing researchers to study their structure-function relationships, interaction with other cellular components, and potential applications in novel agricultural practices. This research not only contributes to the fundamental understanding of metal transport mechanisms in plants but also holds promise for developing sustainable solutions to address food security and environmental challenges linked to metal ion management.
