Analytical Data
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Gene name
fbpB
- Application
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Alternative Names
fbpB；FCNL；Ficolin-2
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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
A1KJU9
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Expression Region
41-325aa
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AA Sequence
FSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETLLTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVYCGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWEYWGAQLNAMKGDLQSSLGAG
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Molecular Weight
37.5 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
FBPB (Fattoush Binding Protein B), a crucial protein involved in various biological processes, has garnered significant attention in recent years due to its potential applications in biomedicine and biotechnology. Initially identified in the context of signaling pathways, FBPB plays a pivotal role in cellular communication and metabolism. Researchers have increasingly focused on the recombinant expression of FBPB to better understand its structure-function relationship and to explore its potential therapeutic uses. The ability to produce FBPB in a recombinant form allows for detailed functional studies, including binding assays and interaction with other cellular components. Moreover, its unique properties make FBPB a candidate for drug delivery systems and diagnostic tools in disease management. The study of FBPB and its recombinant protein variants provides insights into not only its biological significance but also the molecular mechanisms underlying various diseases. This research background highlights the importance of FBPB in both fundamental biology and its prospective role in healthcare advancements, paving the way for novel therapeutic strategies and biotechnological innovations.
