Analytical Data
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Gene name
lprG
- Application
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Alternative Names
lprG；CD209L；CD209L1；CD299；C-type lectin domain family 4 member M
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Species
E.coli
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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
P9WK44
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Expression Region
27-236aa
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AA Sequence
CSSGSKPSGGPLPDAKPLVEEATAQTKALKSAHMVLTVNGKIPGLSLKTLSGDLTTNPTAATGNVKLTLGGSDIDADFVVFDGILYATLTPNQWSDFGPAADIYDPAQVLNPDTGLANVLANFADAKAEGRDTINGQNTIRISGKVSAQAVNQIAPPFNATQPVPATVWIQETGDHQLAQAQLDRGSGNSVQMTLSKWGEKVQVTKPPVS
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Molecular Weight
29.2 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
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Protein Description
LprG is a lipoprotein found in Mycobacterium tuberculosis, the causative agent of tuberculosis (TB). Recent studies have highlighted its significant role in bacterial virulence and host-pathogen interactions, particularly in modulating the immune response. The LprG protein is believed to facilitate the transport of lipids to the cell surface, which is crucial for the bacteria's ability to evade the host immune system. Furthermore, LprG is implicated in the formation of the mycobacterial cell envelope, influencing the bacterium's structural integrity and stability. Research into the recombinant expression of LprG has become essential for understanding its functional mechanisms and potential as a target for therapeutic intervention. Utilizing techniques such as recombinant DNA technology, scientists aim to produce high-quality LprG protein for detailed analyses, including structural studies and immunological assays. This research could pave the way for the development of new TB vaccines or drugs that disrupt the functions of virulence factors like LprG, ultimately contributing to more effective treatment strategies against tuberculosis, a disease that still represents a major global health challenge.
