Analytical Data
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Gene name
PLVAP
- Application
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Alternative Names
PLVAP；FELS；PV1；Plasmalemma vesicle-associated Protein
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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
Q9BX97
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Expression Region
1-442aa
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AA Sequence
MGLAMEHGGSYARAGGSSRGCWYYLRYFFLFVSLIQFLIILGLVLFMVYGNVHVSTESNLQATERRAEGLYSQLLGLTASQSNLTKELNFTTRAKDAIMQMWLNARRDLDRINASFRQCQGDRVIYTNNQRYMAAIILSEKQCRDQFKDMNKSCDALLFMLNQKVKTLEVEIAKEKTICTKDKESVLLNKRVAEEQLVECVKTRELQHQERQLAKEQLQKVQALCLPLDKDKFEMDLRNLWRDSIIPRSLDNLGYNLYHPLGSELASIRRACDHMPSLMSSKVEELARSLRADIERVARENSDLQRQKLEAQQGLRASQEAKQKVEKEAQAREAKLQAECSRQTQLALEEKAVLRKERDNLAKELEEKKREAEQLRMELAIRNSALDTCIKTKSQPMMPVSRPMGPVPNPQPIDPASLEEFKRKILESQRPPAGIPVAPSSG
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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
PLVAP (plastin-like vascular-associated protein) is an endothelial-specific protein primarily expressed in the vascular endothelium and plays a crucial role in maintaining endothelial barrier integrity and regulating angiogenesis. Research into PLVAP's function has gained momentum due to its implications in pathological conditions such as inflammation, cancer, and cardiovascular diseases. Studies have shown that PLVAP is involved in the modulation of endothelial cell junctions and can influence leukocyte trafficking across the endothelium, making it a significant player in immune responses. Additionally, PLVAP has been linked to the process of tumor progression, as its expression is often upregulated in various tumors, potentially facilitating cancer cell dissemination through the vascular system. The recombinant expression of PLVAP in various systems allows researchers to investigate its structure-function relationships, interaction with other vascular proteins, and potential as a therapeutic target. These studies aim to elucidate the molecular mechanisms by which PLVAP contributes to endothelial functions and pathology, opening new avenues for targeted therapies and strategies to enhance endothelial barrier function in disease contexts. The ongoing exploration of PLVAP's role in vascular biology continues to shed light on its potential significance in both normal physiology and disease states.
