Analytical Data
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Gene name
FBN2
- Application
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Alternative Names
FBN2；Fibrillin-2
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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
P35556
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Expression Region
2776-2876aa
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AA Sequence
RQKRSIHEPDPTAVEQISLESVDMDSPVNMKFNLSHLGSKEHILELRPAI QPLNNHIRYVISQGNDDSVFRIHQRNGLSYLHTAKKKLMPGTYTLEITSI P
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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
FBN2, or fibrillin-2, is a critical extracellular matrix protein that plays a significant role in the structural integrity and function of connective tissues. It is a member of the fibrillin family, which is vital for the formation of elastic fibers in various tissues, including skin, blood vessels, and ligaments. Mutations in the FBN2 gene have been associated with various connective tissue disorders, such as congenital contractural arachnodactyly, highlighting its importance in maintaining tissue elasticity and stability. Research on the recombinant form of FBN2 has gained traction as scientists seek to unravel its complex biological functions and mechanisms in health and disease. Studying FBN2 as a recombinant protein allows researchers to investigate its molecular interactions, functional roles in elastic fiber assembly, and potential therapeutic applications. Additionally, recombinant FBN2 can serve as a valuable tool for exploring the pathophysiology of related disorders and developing targeted treatment strategies. This research may open new avenues for understanding and addressing connective tissue diseases, ultimately contributing to the advancement of tissue engineering and regenerative medicine.
