Analytical Data
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Gene name
lpqE
- Application
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Alternative Names
/
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Species
Mycobacterium tuberculosis
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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
P9WK62
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Expression Region
30-182aa
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Molecular Weight
23.2 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 the lpqE recombinant protein is rooted in its significance within the context of infectious diseases, particularly in relation to Mycobacterium tuberculosis (M. tuberculosis), the causative agent of tuberculosis (TB). LpqE, a lipid-binding protein, plays a crucial role in the pathogenesis of M. tuberculosis by participating in the interaction between the bacterium and the host's immune system. Understanding the functions and mechanisms of lpqE is essential for unraveling the complex host-pathogen interactions that occur during TB infection. Additionally, lpqE's potential as a vaccine candidate and its relevance in the development of novel therapeutic strategies highlight the importance of this protein in the broader scope of tuberculosis research. Recent advances in recombinant DNA technology have facilitated the production and characterization of lpqE, allowing researchers to explore its structural properties and immunogenicity. Investigating lpqE not only enhances our comprehension of M. tuberculosis biology but also assists in identifying new targets for drug development and vaccine formulation, contributing to the global effort to combat tuberculosis, a disease that remains a major public health challenge worldwide. Thus, the ongoing research into the lpqE recombinant protein is pivotal in addressing the persistent threat of TB and improving the efficacy of intervention strategies.
