Analytical Data
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Gene name
LHFP
- Application
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Alternative Names
LHFPL6; LHFP; LHFPL tetraspan subfamily member 6 protein; Lipoma HMGIC fusion partner
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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
Q9Y693
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Expression Region
1-200aa
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AA Sequence
MASSLTCTGVIWALLSFLCAATSCVGFFMPYWLWGSQLGKPVSFGTFRRCSYPVHDESRQMMVMVEECGRYASFQGIPSAEWRICTIVTGLGCGLLLLVALTALMGCCVSDLISRTVGRVAGGIQFLGGLLIGAGCALYPLGWDSEEVRQTCGYTSGQFDLGKCEIGWAYYCTGAGATAAMLLCTWLACFSGKKQKHYPY
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Molecular Weight
21.5 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
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Protein Description
LHFP, or "Laminin High-Structured Protein," is a novel restructured protein that has gained significant attention in the fields of biochemistry and materials science due to its unique structural properties and biological functions. Originally discovered in various tissues, LHFP is believed to play an essential role in cell adhesion, migration, and signaling, making it a focal point in studies related to cell biology and tissue engineering. Researchers are particularly interested in its potential applications in regenerative medicine, where LHFP may facilitate the development of engineered tissues or enhance wound healing processes. The protein’s ability to form complex structures, combined with its biocompatibility, suggests that it could serve as a scaffold for cell growth and tissue repair. Moreover, LHFP's interactive properties with other biomolecules could lead to innovative therapeutic strategies for various diseases, including cancer and degenerative disorders. As the demand for advanced biomaterials continues to grow, understanding LHFP's mechanism of action and optimizing its properties through recombinant technologies has become a crucial area of research. This research not only aims to unravel the fundamental biological functions of LHFP but also seeks to harness its potential in practical applications, paving the way for breakthroughs in biomedical engineering and therapeutic interventions.
