Analytical Data
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Gene name
PLVAP
- Application
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Alternative Names
FELS; PV-1; PV1; gp68; Fenestrated-Endothelial Linked Structure Protein; Plasmalemma vesicle protein 1
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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
Q9BX97
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Expression Region
Arg123~Lys393
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Molecular Weight
38kDa
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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
PLVAP (Plasmalemma Vesicle Associated Protein) is a key protein involved in the regulation of endothelial permeability and is primarily expressed in the blood vessels, particularly in the microvascular endothelium. Its expression is crucial for maintaining the integrity of the blood-brain barrier and other tissue-specific barriers. Research into PLVAP has gained momentum due to its potential implications in various pathophysiological conditions, such as inflammation, tumor metastasis, and vascular diseases. Studies have shown that PLVAP plays a significant role in transcytosis and vesicular trafficking processes, impacting the movement of molecules and cells across endothelial barriers. The recombinant production of PLVAP has become an important focus to better understand its structural and functional properties. By employing advanced recombinant DNA technology, researchers can generate high-purity PLVAP proteins, facilitating in-depth studies on their biochemical characteristics and interactions with other cellular components. Furthermore, investigating PLVAP in a recombinant form allows for the development of targeted therapeutic strategies aimed at modulating vascular permeability in diseases associated with dysregulated endothelial function. Overall, the study of recombinant PLVAP not only enhances our understanding of its role in vascular biology but also opens avenues for novel therapeutic interventions in diseases characterized by altered endothelial permeability.
