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Catalog Number | orb1231536 |
---|---|
Category | Proteins |
Description | SARS-CoV S Recombinant Protein (R667A, K968P, V969P) |
Tested applications | ELISA, WB |
Tag | His Tag |
Dilution range | This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 136.3 kDa. The protein migrates as 190-210 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. |
Form/Appearance | Lyophilized |
Purity | > 95% as determined by SDS-PAGE. |
MW | 136.3 kDa |
Protein Sequence | Ser 14 - Pro 1195 |
Source | HEK293 cells |
NCBI | K968, R667, V969, AAP13567.1 |
Storage | Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles. |
Buffer/Preservatives | PBS |
Alternative names | Spike,S protein,Spike glycoprotein,S glycoprotein Read more... |
Note | For research use only |
Application notes | This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 136.3 kDa. The protein migrates as 190-210 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. |
Expiration Date | 6 months from date of receipt. |
SARS S protein (R667A, K968P, V969P), His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Immobilized Human ACE2, Fc Tag at 2 ug/ml (100 uL/well) can bind SARS S protein (R667A, K968P, V969P), His Tag with a linear range of 2-20 ng/mL.
Unconjugated | |
95% | |
136.3 kDa | |
SARS S protein (R667A, K968P, V969P), His Tag (orb750333) is expressed from human 293 cells (HEK293). It contains AA Ser 14 - Pro 1195 (Accession # AAP13567.1 (R667A, K968P, V969P)). The recombinant protein is expressed with T4 fibritin trimerization motif and a polyhistidine tag at the C-terminus. Proline substitutions (K968P, V969P) and alanine substitutions (R667A) are introduced to stabilize the trimeric prefusion state of SARS-CoV S protein and abolish the furin cleavage site, respectively. |
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