Analytical Data
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Gene name
QT
- Application
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Alternative Names
QT；CTRP1；Complement C1q tumor necrosis factor-related Protein 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
Q9BXJ1
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Expression Region
26-281aa
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AA Sequence
RVPHVQGEQQEWEGTEELPSPPDHAERAEEQHEKYRPSQDQGLPASRCLRCCDPGTSMYPATAVPQINITILKGEKGDRGDRGLQGKYGKTGSAGARGHTGPKGQKGSMGAPGERCKSHYAAFSVGRKKPMHSNHYYQTVIFDTEFVNLYDHFNMFTGKFYCYVPGLYFFSLNVHTWNQKETYLHIMKNEEEVVILFAQVGDRSIMQSQSLMLELREQDQVWVRLYKGERENAIFSEELDTYITFSGYLVKHATEP
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Molecular Weight
31.7 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 study of QT recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including medicine, biotechnology, and molecular biology. QT proteins, often derived from certain species, play crucial roles in cellular signaling and regulating physiological processes. Understanding the structure and function of these proteins can provide insights into their mechanisms of action and their involvement in disease pathways. Research has shown that modifications to QT proteins can enhance their stability, efficacy, and specificity, making them suitable candidates for drug development and therapeutic interventions. Moreover, advances in recombinant DNA technology have enabled the efficient production of QT proteins with desired characteristics, facilitating their use in experimental and clinical settings. Investigating QT recombinant proteins not only contributes to the fundamental understanding of cellular machinery but also opens avenues for innovative treatments for various conditions, including cancers and genetic disorders. As the field progresses, ongoing research aims to uncover the diverse functionalities of QT proteins and harness their therapeutic potential, underscoring their importance in both scientific inquiry and practical applications.
