Recombinant Human Syncytin-1 (ERVW-1), partial

Category: Proteins
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CSB-EP891578HU
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Product Name Recombinant Human Syncytin-1 (ERVW-1), partial
Description This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449, PubMed:12050356, PubMed:23492904).Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane 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 membranes.
Synonyms Endogenous retrovirus group W member 1
Env-W
Envelope polyprotein gPr73
Enverin
HERV-7q Envelope protein
HERV-W envelope protein
HERV-W_7q21.2 provirus ancestral Env polyprotein
Syncytin
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Alternative name(s):
gp50
Transmembrane protein
Short name:
TM
Alternative name(s):
gp24
Host E.coli
Molecular Weight 63
Amino Acid Sequence APPPCRCMTSSSPYQEFLWRMQRPGNIDAPSYRSLSKGTPTFTAHTHMPRNCYHSATLCMHANTHYWTGKMINPSCPGGLGVTVCWTYFTQTGMSDGGGVQDQAREKHVKEVISQLTRVHGTSSPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWICLPLNFRPYVSIPVPEQWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTTYTTNSQCIRWVTPPTQIVCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYSYVISKPRNKRVPILPFVIGAGVLGALGTGIGGITTSTQFYYKLSQELNGDMERVADSLVTLQDQLNSLAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNTGPWGLLSQ
Protein Length Extracellular Domain, 21-443aa
Tag N-terminal 6xHis-SUMO-tagged
Reactivity Human
Applications SDS-PAGE
Form Liquid, in Tris-based buffer, 50% glycerol
Purity Greater than 90% as determined by SDS-PAGE.
References "Molecular characterization and placental expression of HERV-W, a new human endogenous retrovirus family."Blond J.-L., Beseme F., Duret L., Bouton O., Bedin F., Perron H., Mandrand B., Mallet F.J. Virol. 73:1175-1185(1999)
Background This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449, PubMed:12050356, PubMed:23492904).Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane 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 membranes.
Supplier Cusabio

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