Analytical Data
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Gene name
LT
- Application
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Alternative Names
LT；Igb3s；Alpha-1.3-galactosyltransferase 2
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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
P01860
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Expression Region
99-377aa
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AA Sequence
ELKTPLGDTT HTCPRCPEPK SCDTPPPCPR CPEPKSCDTP PPCPRCPEPK SCDTPPPCPR CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVQFKWY VDGVEVHNAK TKPREEQYNS TFRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK TKGQPREPQV YTLPPSREEM TKNQVSLTCL VKGFYPSDIA VEWESSGQPE NNYNTTPPML DSDGSFFLYS KLTVDKSRWQ QGNIFSCSVM HEALHNRFTQ KSLSLSPGK
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Molecular Weight
31 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
LT (Lethal Toxin) recombinant protein has garnered significant attention in biomedical research due to its unique properties and potential applications. Originating from the bacterium *Bacillus anthracis*, LT is a pivotal virulence factor of anthrax, consisting of two components: protective antigen (PA) and lethal factor (LF). The interaction between PA and LF enables the toxin to enter host cells and disrupt critical signaling pathways, ultimately leading to cell death. This mechanism positions LT as a powerful tool for studying cellular processes and developing targeted therapies. Researchers have been exploring LT as a delivery system for therapeutic genes and vaccines, capitalizing on its ability to efficiently enter cells. Additionally, its apoptotic properties are being investigated for potential cancer treatments, where selective induction of cell death can be beneficial. The adaptability of LT in recombinant forms allows for modifications that enhance its efficacy and specificity, making it a valuable candidate in both fundamental research and clinical applications. Thus, the study of LT recombinant protein not only aids in our understanding of anthrax pathogenesis but also paves the way for innovative approaches in drug development and the treatment of various diseases.
