Analytical Data
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Gene name
FBN1
- Application
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Alternative Names
FBN1；FBN；Fibrillin-1
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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
P35555
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Expression Region
2772-2871aa
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AA Sequence
SNKVRILELLPALTTLTNHNRYLIESGNEDGFFKINQKEGISYLHFTKKK PVAGTYSLQISSTPLYKKKELNQLEDKYDKDYLSGELGDNLKMKIQVLLH
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Molecular Weight
37 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
FBN1, or fibrillin-1, is a critical extracellular matrix protein that plays a significant role in the structure and function of connective tissues. It is a fundamental component of microfibrils, contributing to the integrity of various tissues, including skin, blood vessels, and ligaments. Mutations in the FBN1 gene are linked to Marfan syndrome, a genetic disorder characterized by features such as tall stature, cardiovascular issues, and ocular problems. The study of FBN1 recombinant proteins has gained traction in recent years as researchers aim to understand its structure-function relationships and pathophysiological roles. By producing recombinant FBN1 proteins, scientists can investigate the molecular mechanisms underlying fibrillin-1 interactions, assess the impact of specific mutations, and evaluate potential therapeutic strategies for related disorders. Additionally, the development of these recombinant proteins facilitates the exploration of fibrillin-1's role in tissue engineering and regenerative medicine, where it holds promise for enhancing scaffold materials or developing novel biomaterials. Overall, research on FBN1 recombinant proteins not only advances our understanding of connective tissue biology but also paves the way for potential clinical applications in treating genetic disorders and improving tissue regeneration.
