Analytical Data
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Gene name
loiP
- Application
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Alternative Names
loiP；yggG；Metalloprotease LoiP
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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
P25894
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Expression Region
19-252aa
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AA Sequence
CQNMDSNGLLSSGAEAFQAYSLSDAQVKTLSDQACQEMDSKATIAPANSE YAKRLTTIANALGNNINGQPVNYKVYMAKDVNAFAMANGCIRVYSGLMDM MTDNEVEAVIGHEMGHVALGHVKKGMQVALGTNAVRVAAASAGGIVGSLS QSQLGNLGEKLVNSQFSQRQEAEADDYSYDLLRQRGISPAGLATSFEKLA KLEEGRQSSMFDDHPASAERAQHIRDRMSADGIK
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Molecular Weight
29 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
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Protein Description
LoiP is a recombinant protein that has garnered significant attention in the fields of molecular biology and biotechnology due to its unique structural and functional properties. Initially isolated from specific microbial sources, LoiP exhibits remarkable stability and activity under extreme conditions, making it an attractive candidate for various industrial applications, including enzyme catalysis and bioremediation. Its distinct folding and activity patterns have sparked interest in understanding the underlying mechanisms that govern its functionality. Researchers have focused on the genetic engineering of LoiP to enhance its characteristics, allowing for tailored modifications to improve performance in practical applications. Additionally, studies on LoiP’s potential role in synthetic biology aim to explore its uses in the development of novel biomaterials and therapeutic agents. The ongoing research into LoiP not only aims to unlock its potential utility in various industries but also contributes to broader scientific knowledge about protein engineering and the evolution of extremophiles, paving the way for innovative solutions to complex biological and environmental challenges.
