Human PVRIG Protein, His Tag (MALS verified)

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PVG-H52H5-100ug
$360.00
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PVG-H52H5-1mg
$2,615.00
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PVG-H52H5
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Synonyms

C7orf15, C7orf15MGC138295, CD112R, MGC104322, MGC138297, MGC2463, PVRIG, CD112 receptor

Source

Human PVRIG, His Tag (PVG-H52H5) is expressed from human 293 cells (HEK293). It contains AA Thr 41 - Asp 171 (Accession # Q6DKI7-1).

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 15.7 kDa. The protein migrates as 22-30 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>90% 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.

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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.

Background

Human PVRIG (poliovirus receptor related immunoglobulin domain-containing protein), also known as CD112 receptor (CD112R), is an approximately 34 kDa single transmembrane protein in the poliovirus receptor-like protein (PVR) family. The CD112R gene encodes a putative single transmembrane protein, which is composed of a single extracellular IgV domain, one transmembrane domain, and a long intracellular domain. Notably, the intracellular domain of phatases. The extracellular domain sequence of human and mouse CD112R have 65.3% similarity. CD112R may act as a coinhibitory receptor that suppresses T-cell receptor-mediated signals.