Anti-Syncytin-1 Polyclonal Antibody is a Rabbit antibody targeting Syncytin-1. Anti-Syncytin-1 Polyclonal Antibody can be used in WB.

IgG

Human,Mouse

1. Sample:
Brain (Mouse) Lysate at 40 μg
Primary: Anti-Syncytin 1 (TMAB-01803) at 1/300 dilution
Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution
Predicted band size: 33/58 kDa
Observed band size: 58 kDa
2. Sample:
Lane 1: JEG-3 (Human) Cell Lysate at 30 μg
Lane 2: JAR (Human) Cell Lysate at 30 μg
Lane 3: U2os (Human) Cell Lysate at 30 μg
Lane 4: U251 (Human) Cell Lysate at 30 μg
Lane 5: SH-SY5Y (Human) Cell Lysate at 30 μg
Lane 6: HT1080 (Human) Cell Lysate at 30 μg
Primary: Anti-Syncytin 1 (TMAB-01803) at 1/1000 dilution
Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution
Predicted band size: 58 kDa
Observed band size: 60 kDa

WB: 1:500-2000

Polyclonal

KLH conjugated synthetic peptide: human Syncytin 1

Human

ERVW-1

Endogenous retrovirus group W member 1

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).3 PublicationsEndogenous 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.