Analytical Data
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Gene name
FIBIN
- Application
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Alternative Names
FIBIN；Fin bud initiation factor homolog
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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
Q8TAL6
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Expression Region
19-211aa
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AA Sequence
YFDGPLYPEMSNGTLHHYFVPDGDYEENDDPEKCQLLFRVSDHRRCSQGEGSQVGSLLSLTLREEFTVLGRQVEDAGRVLEGISKSISYDLDGEESYGKYLRRESHQIGDAYSNSDKSLTELESKFKQGQEQDSRQESRLNEDFLGMLVHTRSLLKETLDISVGLRDKYELLALTIRSHGTRLGRLKNDYLKV
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Molecular Weight
38.1 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
FIBIN, a protein implicated in various biological processes, has garnered significant interest in recent years due to its potential roles in cell adhesion, migration, and tissue development. Initially identified as a key component of the extracellular matrix, FIBIN's structure suggests it may interact with other matrix proteins, influencing cellular behaviors critical for wound healing and development. Research has shown that FIBIN expression can be altered in pathological conditions, such as fibrosis and cancer, highlighting its potential as a biomarker for disease progression and a target for therapeutic interventions. The recombinant production of FIBIN has enabled researchers to study its function and interaction dynamics in greater detail, facilitating advances in understanding its biological role. Recent studies utilizing recombinant FIBIN have revealed insights into its molecular mechanisms, paving the way for innovative applications in regenerative medicine and targeted therapies. As investigations into the multifaceted functions of FIBIN continue, it holds promise for contributing to the development of novel strategies for treating diseases associated with extracellular matrix dysregulation.
