Analytical Data
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Gene name
bEP
- Application
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Alternative Names
bEP；LPDLR；MPAPLA1；PLA1B；Lipase member H
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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
Q8WWY8
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Expression Region
19-451aa
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AA Sequence
EE TCPSFTRLSF HSAVVGTGLN VRLMLYTRKN LTCAQTINSS AFGNLNVTKK TTFIVHGFRP TGSPPVWMDD LVKGLLSVED MNVVVVDWNR GATTLIYTHA SSKTRKVAMV LKEFIDQMLA EGASLDDIYM IGVSLGAHIS GFVGEMYDGW LGRITGLDPA GPLFNGKPHQ DRLDPSDAQF VDVIHSDTDA LGYKEPLGNI DFYPNGGLDQ PGCPKTILGG FQYFKCDHQR SVYLYLSSLR ESCTITAYPC DSYQDYRNGK CVSCGTSQKE SCPLLGYYAD NWKDHLRGKD PPMTKAFFDT AEESPFCMYH YFVDIITWNK NVRRGDITIK LRDKAGNTTE SKINHEPTTF QKYHQVSLLA RFNQDLDKVA AISLMFSTGS LIGPRYKLRI LRMKLRSLAH PERPQLCRYD LVLMENVETV FQPILCPELQ L
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Molecular Weight
50.8 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
The research on bEP (bacterial endotoxin-binding protein) recombinant proteins has gained significant attention due to their potential applications in biomedicine and biotechnology. bEPs are known for their ability to bind and neutralize endotoxins, which are toxic components of the outer membrane of Gram-negative bacteria. Endotoxins can trigger severe inflammatory responses in humans and animals, leading to conditions such as septic shock and systemic inflammatory response syndrome (SIRS). The development of recombinant bEPs presents an opportunity to create effective therapeutics for treating endotoxin-related diseases. By utilizing recombinant DNA technology, researchers can produce bEPs in controlled environments, allowing for the optimization of their properties and functions. This includes enhancing their binding affinity and specificity for endotoxins, as well as improving their stability and bioavailability. The investigation into bEPs also intersects with the growing field of immunotherapy, as these proteins can be conjugated with other therapeutic agents to enhance their efficacy. Advances in understanding the molecular mechanisms of bEP action and the pathways involved in endotoxin-mediated inflammation further bolster the potential for developing novel treatments. Overall, the research on recombinant bEPs holds promise for creating innovative solutions to mitigate the harmful effects of bacterial infections and improve patient outcomes in various clinical contexts.
