Analytical Data
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Gene name
Serpinf1
- Application
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Alternative Names
Serpinf1；PEDF；Pigment epithelium-derived factor
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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
P36955
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Expression Region
20-418aa
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AA Sequence
QNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVR SSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIH GTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVL TGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVT KFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLT GSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKL SYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGA GTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP
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Molecular Weight
44 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
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Protein Description
Serpinf1, also known as Serpin F1 or antitrypsin-related protein, is a member of the serpin (serine protease inhibitor) superfamily, which plays critical roles in regulating proteinases involved in various physiological processes. It is primarily known for its functions in the extracellular matrix and as a modulator of inflammatory responses. Research has indicated that Serpinf1 exhibits neuroprotective effects and is implicated in several pathological conditions, including Alzheimer's disease and age-related macular degeneration. Its role in inhibiting proteolytic enzymes, such as cathepsins, suggests potential therapeutic applications in diseases characterized by excessive proteolytic activity. Furthermore, studies have shown that Serpinf1 expression is influenced by factors like inflammation, hypoxia, and oxidative stress, highlighting its involvement in tissue remodeling and repair. Given the significance of Serpinf1 in health and disease, recombinant Serpinf1 protein has become a focal point for researchers aiming to understand its biological functions and explore its potential as a biomarker and therapeutic agent. The development of recombinant Serpinf1 enables detailed investigations into its molecular mechanisms and interactions, paving the way for novel strategies to address diseases associated with protease dysregulation and tissue damage.
