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Product Details
Synonyms
PVR, FLJ25946, PVS, CD155, TAGE4, HVED, NECL5
Source
Human CD155, His Tag (CD5-H5223) is expressed from human 293 cells (HEK293). It contains AA Trp 21 - Asn 343 (Accession # NP_006496.4).
Predicted N-terminus: Trp 21
Request for sequenceMolecular Characterization
Other Tags and Version Biotin & Other Labeled Version
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 35.9 kDa. The protein migrates as 55-65 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Endotoxin
Less than 0.01 EU per μg by the LAL method / rFC method.
Purity
>95% as determined by SDS-PAGE.
>95% as determined by SEC-MALS.
Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 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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Performance Data
SDS-PAGE
Human CD155, His Tag 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 Human CD155, His Tag (Cat. No. CD5-H5223) is more than 95% and the molecular weight of this protein is around 50-60 kDa verified by SEC-MALS.
Report
Bioactivity-BLI
Loaded Human TIGIT, Fc Tag (Cat. No. TIT-H5254) on Protein A Biosensor, can bind Human CD155, His Tag (Cat. No. CD5-H5223) with an affinity constant of 0.89 μM as determined in BLI assay (ForteBio Octet Red96e) (QC tested).
Protocol
Loaded Human DNAM-1, Fc Tag (Cat. No. DN1-H5257) on Protein A Biosensor, can bind Human CD155, His Tag (Cat. No. CD5-H5223) with an affinity constant of 1.6 μM as determined in BLI assay (ForteBio Octet Red96e) (Routinely 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
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.
Recent Advances
Drug Development Progress- English Name：
Poliovirus receptor
- Category：
- Approved Drugs：
0 Details
- Drugs in Clinical Trials：
2 Details
- Highest Development Stage：
Phase 2 Clinical
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