Product Details
Synonyms
PVR, FLJ25946, PVS, CD155, TAGE4, HVED, NECL5
Source
Biotinylated Mouse CD155, Fc,Avitag (CD5-M82F7) is expressed from human 293 cells (HEK293). It contains AA Asp 29 - Leu 348 (Accession # Q8K094-1).
Predicted N-terminus: Asp 29
Request for sequenceMolecular Characterization

Other Tags and Version Biotin & Other Labeled Version
This protein carries a human IgG1 Fc tag at the C-terminus, followed by an Avi tag (Avitag™).
The protein has a calculated MW of 63.5 kDa. The protein migrates as 90-120 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Labeling
Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
Protein Ratio
Passed as determined by the SABA assay / HABA assay / binding ELISA.
Purity
>95% as determined by SDS-PAGE.
>95% as determined by SEC-MALS.
Formulation
Lyophilized from 0.22 μm filtered solution in Tris with Glycine, Arginine and NaCl, pH7.5 with trehalose as protectant.
Contact us for customized product form or formulation.
Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Shipping and Storage
This product is shipped at ambient temperature.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
ACRO Quality Management System
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Data Display
SDS-PAGE

Biotinylated Mouse CD155, Fc,Avitag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.
SEC-MALS

The purity of Biotinylated Mouse CD155, Fc,Avitag (Cat. No. CD5-M82F7) is more than 95% and the molecular weight of this protein is around 150-180 kDa verified by SEC-MALS.
Report
Bioactivity-ELISA

Immobilized Mouse TIGIT, Fc Tag (Cat. No. TIT-M5257) at 5 μg/mL (100 μL/well) can bind Biotinylated Mouse CD155, Fc,Avitag (Cat. No. CD5-M82F7) with a linear range of 0.005-0.313 μg/mL (QC tested).
Protocol
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FAQ
- product
Can lyophilized proteins remain stable during room-temperature shipping or temporary room-temperature exposure?
In general, lyophilized proteins remain stable during room-temperature shipping or temporary exposure to room-temperature conditions.
Many ACROBiosystems recombinant proteins are supplied in lyophilized (freeze-dried) form. The lyophilization process effectively removes moisture from the product, helping reduce degradation-related reactions and improve protein stability during transportation and storage.
To evaluate the stability of lyophilized proteins under normal temperature conditions, ACROBiosystems conducted a stability study on 11 representative lyophilized protein products at 37°C. The study demonstrated that these proteins maintained good quality stability after storage at 37°C for approximately 20 days. Based on these validation results, temporary room-temperature exposure during shipping or handling is generally not expected to have a significant impact on product quality or downstream application performance.
To ensure optimal long-term stability, products should be stored according to the storage conditions specified in the product Certificate of Analysis (COA) upon receipt.
Supporting Document
Background Introduction
CD155/PVR was originally isolated based on its ability to mediate polio virus attachment to host cells. The fulllength (or CD155 alpha isoform) is synthesized as a 417 amino acid (aa) precursor that contains a 20 aa signal sequence, a 323 aa extracellular region, a 24 aa TM segment and a 50 aa cytoplasmic tail. The extracellular region contains one N terminal V type and two C2 type Ig like domains.
CD155 is a transmembrane protein with 3 extracellular immunoglobulin-like domains, D1-D3, where D1 is recognized by the virus. Low resolution structures of CD155 complexed with poliovirus have been obtained using electron microscopy while a high resolution structures of theectodomain D1 and D2 of CD155 were solved by x-ray crystallography.
Frontier Progress
- English Name:
Poliovirus receptor
- Category:
- Listed Drugs Count:
0 Details
- Clinical Drugs Count:
2 Details
- Highest R&D Stage:
Phase 2 Clinical



















