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Herpes Simplex Virus-8 Mosaic Recombinant ( HSV-8 M )
DescriptionThe E.Coli derived recombinant protein contains the C-terminal immunodominant regions from ORF65 140-170 a.a. and N-terminal regions from ORF8 32-62 a.a. The protein is fused with a GST tag.Purification MethodHSV-8 Mosaic was purified by
Data sheet
| Storage | HSV-8 Mosaic protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles. |
| Formulation | 100mM NaCl, 0.1% SDS and 50% glycerol. |
| Purity | HSV-8 Mosaic protein is >95% pure as determined by 10% PAGE (coomassie staining). |
| Applications | HSV-8 Mosaic antigen is suitable for ELISA and Western blots, excellent antigen for detection of HSV with minimal specificity problems. |
| Description | The E.Coli derived recombinant protein contains the C-terminal immunodominant regions from ORF65 140-170 a.a. and N-terminal regions from ORF8 32-62 a.a. The protein is fused with a GST tag. |
| Protein Background | Entry of HSV into the host cell involves interactions of several viral glycoproteins with cell surface receptors. The virus particle is covered by an envelope which, when bound to specific receptors on the cell surface, will fuse with the cell membrane and create an opening, or pore, through which the virus enters the host cell. The sequential stages of HSV entry are analagous to those of other viruses. At first, complementary receptors on the virus and cell surface bring the two membranes into proximity. In an intermediate state, the two membranes begin to merge, forming a hemifusion state. Finally, a stable entry pore is formed through which the viral envelope contents are introduced to the host cell. |
| Reagent Appearance | Sterile Filtered clear solution. |
| Purification Method | HSV-8 Mosaic was purified by proprietary chromatographic technique. |