Analytical Data
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Gene name
Fibulin-3
- Application
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Alternative Names
EFEMP1; DHRD; DRAD; FBNL; MLVT; MTLV; S1-5; EGF-Containing Fibulin-Like Extracellular Matrix Protein 1; Fibrillin-Like; Extracellular protein S1-5
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q12805
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Expression Region
Cys258~Phe493
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Molecular Weight
27kDa
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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
Fibulin-3, also known as EFEMP1, is an extracellular matrix protein that plays a crucial role in various biological processes, including cell adhesion, tissue remodeling, and angiogenesis. Its significance has been highlighted in several studies linking it to various pathologies, particularly in the context of ocular diseases, such as age-related macular degeneration (AMD). Research has shown that Fibulin-3 is involved in the regulation of matrix metalloproteinases (MMPs) and may influence the stability and composition of the extracellular matrix, which are critical for maintaining normal tissue architecture. Mutations and aberrant expression of Fibulin-3 have been associated with increased susceptibility to AMD and other degenerative conditions. As a result, the recombinant form of Fibulin-3 has emerged as a vital tool in both basic and translational research. Scientists are exploring its potential as a biomarker for disease diagnosis and progression, as well as a therapeutic target for strategies aimed at modulating its activity to counteract the effects of matrix dysregulation. By producing recombinant Fibulin-3, researchers can investigate its function in various cellular contexts, study its interactions with other matrix components, and identify potential pathways for intervention in fibrotic conditions and degenerative diseases. This research offers promising avenues for the development of new therapeutic strategies, highlighting the importance of Fibulin-3 in both normal physiology and pathological conditions.
