Analytical Data
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Gene name
FBLN3
- Application
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Alternative Names
FBLN3;FBLN3;FBNL;EGF-containing fibulin-like extracellular matrix Protein 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
Q12805
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Expression Region
1-493aa
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AA Sequence
MLKALFLTMLTLALVKSQDTEETITYTQCTDGYEWDPVGQQCKDIDECDI VPDACKGGMKCVNHYGGYLCLPKTAQIIVNNEQPQQETQPAEGTSGATTG VVAASSMATSGVLPGGGFVASAAAVAGPEMQTGRNNFVIRRNPADPQRIP SNPSHRIQCAAGYEQSEHNVCQDIDECTAGTHNCRADQVCINLRGSFACQ CPPGYQKRGEQCVDIDECTIPPYCHQRCVNTPGSFYCQCSPGFQLAANNY TCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRT SSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMC WNYHGGFRCYPRNPCQDPYILTPENRCVCPVSNAMCRELPQSIVYKYMSI RSDRSVPSDIFQIQATTIYANTINTFRIKSGSENGEFYLRQTSPVSAMLV LVKSLSGPREHIVDLEMLTASSIGTFRTSSVLRLTIIVGPFSF
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Molecular Weight
80 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
FBLN3, or fibulin-3, is a member of the fibulin family of extracellular matrix proteins, which play critical roles in tissue development, maintenance, and repair. The research on FBLN3 has gained momentum due to its implications in various pathological conditions, particularly in cancer and fibrotic diseases. Studies have shown that FBLN3 is involved in modulating cell adhesion, migration, and proliferation through its interactions with various extracellular matrix components and cell surface receptors. Additionally, aberrant expression of FBLN3 has been linked to tumor progression and metastasis, highlighting its potential as a diagnostic and therapeutic target. Recent advances in recombinant protein technology have facilitated the production of FBLN3 in a tractable format, allowing researchers to investigate its structure-function relationships and biological activities in greater detail. Understanding the specific mechanisms by which FBLN3 influences cell behavior could provide insight into its role in disease progression and open avenues for developing novel therapeutic strategies. Overall, the study of recombinant FBLN3 protein is essential for unraveling its biological functions and therapeutic potential, making it a significant focus in biomedical research.











