Analytical Data
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Gene name
LNP1
- Application
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Alternative Names
LNP1; NP3Leukemia NUP98 fusion partner 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A1A4G5
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Expression Region
1-178aaa
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AA Sequence
MEHKDDDDDDVSFAKWMSSFWGHSWREEDQRGLRERHRLQATSHRKTSLPCPLPVLPRIPSSDCHPRRHSHEDQEFRCRSHVRDYRKYSEDGSFKEPLESKGRSHSKIEKFSESFERQLCFRTKRSASLGPESRKERNERECLRMEIKSRKKVEEERSSRKEEHGEAHMAPLFEKGPE
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Molecular Weight
19.6 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
LNP1, a recombinant protein derived from the fusion of lipocalin and a specific peptide sequence, has garnered attention in the field of biomedicine due to its unique structural and functional properties. Lipocalins, a family of small, extracellular proteins, are known for their capacity to bind small hydrophobic molecules and play crucial roles in various biological processes, including transport, signaling, and immune responses. The study of LNP1 not only seeks to understand its inherent biochemical characteristics but also explores its potential applications in drug delivery systems, as a biotherapeutic agent, and in the development of biomaterials. Research indicates that LNP1 exhibits remarkable stability and solubility, making it a promising candidate for targeting specific tissues or cells. Furthermore, its ability to transport and deliver therapeutic agents to desired sites enhances its significance in developing targeted therapies for various diseases, including cancer and metabolic disorders. The ongoing investigation into LNP1’s structure-function relationship is vital for optimizing its applications, paving the way for innovative therapeutic strategies that may improve patient outcomes and transform existing treatment paradigms. This vibrant area of research reflects a broader interest in harnessing protein engineering and biochemistry to create effective medical solutions, highlighting the impact of recombinant proteins in advancing healthcare technology.
