Analytical Data
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Gene name
Neuropilin-1
- Application
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Alternative Names
CD304; BDCA4; VEGF165R; Vascular endothelial cell growth factor 165 receptor
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9QWJ9
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Expression Region
Asn150~Val264
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Molecular Weight
15kDa
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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
Neuropilin-1 (NRP1) is a membrane protein that plays a crucial role in various biological processes, including neuronal guidance, angiogenesis, and immune responses. Initially identified as a receptor for class 3 semaphorins, NRP1 has garnered interest for its involvement in regulating axon pathfinding during nervous system development. Beyond its role in the nervous system, NRP1 also contributes to tumor development and progression by modulating the tumor microenvironment and promoting angiogenesis. The interplay between NRP1 and vascular endothelial growth factor (VEGF) signaling highlights its significance in both developmental biology and cancer therapy. Given its multifaceted functions, there is a growing interest in the therapeutic potential of targeting NRP1, particularly in cancer treatment. The production of recombinant NRP1 proteins is essential for elucidating its mechanisms of action and testing potential inhibitors or therapeutic agents. By utilizing advanced molecular biology techniques, researchers can generate recombinant NRP1 proteins to study their structural characteristics, specific binding properties, and functional roles in various cellular contexts. This research is pivotal in expanding our understanding of NRP1's involvement in pathophysiological conditions and developing novel therapeutic strategies aimed at modulating its activity for beneficial outcomes in diseases such as cancer and neurodegenerative disorders.
