Analytical Data
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Gene name
LTA
- Application
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Alternative Names
LTA；TNFB；TNFSF1；Lymphotoxin-alpha
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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
P01374
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Expression Region
35-205aa
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AA Sequence
LPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL
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Molecular Weight
20.8 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
LTA (Lipoteichoic Acid) is a significant component of the cell wall of Gram-positive bacteria, playing a crucial role in their structural integrity, adherence, and pathogenicity. As researchers continue to explore the immune response and potential therapeutic targets related to bacterial infections, the study of LTA and its recombinant forms has gained prominence. The recombinant expression of LTA offers a unique opportunity to investigate its biochemical properties, interactions with host cells, and immunogenicity. Understanding the structure-function relationships of LTA can aid in developing novel vaccines and adjuvants, contributing to enhanced immunity against bacterial pathogens. Additionally, the study of LTA may reveal insights into its role in bacterial virulence and resistance to immune responses, thus providing valuable information for the design of new antibacterial strategies. As antibiotic resistance becomes an increasing global concern, the development of effective alternatives such as LTA-based immunotherapies could play a pivotal role in public health. Consequently, the research into the recombinant production and characterization of LTA is vital for advancing our understanding of bacterial biology and host-pathogen interactions, ultimately aiding in the development of innovative therapeutic approaches.
