protein

ERVW-1 Protein, Human (His-SUMO)

HY-P71654

20 μg;50 μg

180;360 USD

ERVW-1 Protein, Human (His-SUMO)

proteins

E. coli

20 μg;50 μg

180;360 USD

The ERVW-1 protein is an endogenous retroviral envelope protein that retains fusogenic properties critical for trophoblast fusion and syncytium formation during placental morphogenesis. Its fusion ability involves binding to SLC1A4 and SLC1A5. ERVW-1 Protein, Human (His-SUMO) is the recombinant human-derived ERVW-1 protein, expressed by E. coli , with N-His, N-SUMO labeled tag.

Human

The endogenous retroviral envelope protein ERVW-1 has preserved its inherent fusogenic properties, playing a pivotal role in trophoblast fusion and the establishment of a syncytium during placental morphogenesis. Its capacity for inducing fusion is facilitated through the binding of SLC1A4 and SLC1A5. Endogenous envelope proteins, like ERVW-1, may exhibit varied evolutionary fates, maintaining, losing, or altering their original functions over time. Retroviral envelope proteins, comprising a surface protein (SU) for receptor recognition and a transmembrane protein (TM) acting as a class I viral fusion protein, are critical for receptor recognition and membrane fusion in early infection. ERVW-1 likely adopts three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. In the context of viral and target cell membrane fusion, the coiled coil regions (heptad repeats) transition to a trimer-of-hairpins structure, bringing the fusion peptide close to the ectodomain's C-terminal region—a structural arrangement believed to drive membrane apposition and subsequent fusion.

ERVW-1; ERVWE1; Syncytin-1; Endogenous retrovirus group W member 1; Env-W; Envelope polyprotein gPr73; Enverin

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized after extensive dialysis against solution in 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.