PDF DatasheetHuman Spike glycoprotein Recombinant Protein Product Attributes
Product Type: Recombinant Protein
Recombinant Spike glycoprotein based upon sequence from Human
Host: QP7178 protein expressed in E.coli, Yeast..
Tag: His-SUMO
Protein Construction: A DNA sequence encoding the Homo sapiens (Human) Spike glycoprotein, was expressed in the hosts and tags indicated. Please select your host/tag option, above.
Recommended Applications: Immunogen, Protein Standard, Cell culture, or Other Cell Biology Applications.
Application Notes: Please contact us for application specific information for QP7178.
Bioactivity Data: Untested
Full Length? Partial (see sequence information for more details).
Expression Region: Val15 – Lys344
Amino Acid Sequence: VIGDLKCTSD NINDKDTGPP PISTDTVDVT NGLGTYYVLD RVYLNTTLFL NGYYPTSGST YRNMALKGSV LLSRLWFKPP FLSDFINGIF AKVKNTKVIK DRVMYSEFPA ITIGSTFVNT SYSVVVQPRT INSTQDGDNK LQGLLEVSVC QYNMCEYPQT ICHPNLGNHR KELWHLDTGV VSCLYKRNFT YDVNADYLYF HFYQEGGTFY AYFTDTGVVT KFLFNVYLGM ALSHYYVMPL TCNSKLTLEY WVTPLTSRQY LLAFNQDGII FNAEDCMSDF MSEIKCKTQS IAPPTGVYEL NGYTVQPIAD VYRRKPNLPN CNIEAWLNDK
Purity: Greater than 90% as determined by SDS-PAGE.
Reconstitution Instructions: Concentrated protein in liquid format. Reconstitution is not necessary.
Concentration of Human Spike glycoprotein Protein:
Endotoxin Levels: Not determined.
Buffer: Tris-based buffer, 50% glycerol
Storage Conditions: Store at -20C to -80C.
| Recombinant Human Spike glycoprotein Protein General Information | |
|---|---|
| Curated Database and Bioinformatic Data | |
| Gene Symbol | S |
| UniProt ID(s) | P36334 |
| General Description of Recombinant Human Spike glycoprotein Protein. | |
| S1 attaches the virion to the cell mbrane by interacting with sialic acid-containing cell receptors, initiating the infection.S2 is a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell mbrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell mbranes. | |
Limitations and Performance Guarantee
This is a life science research product (for Research Use Only). This product is guaranteed to work for a period of two years when stored at -70C or colder, and one year when aliquoted and stored at -20C.
There are no reviews yet.