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Rabbit
Anti-Syncytin 1/PE-Cy7
Cat. Number:
bs-2962R-PE-Cy7
Quantity size:
100ul
Concentration:
1mg/ml Buffer = 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
Background:
Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has retained its original fusogenic properties and participates in trophoblast fusion during placenta morphogenesis.
SU mediates receptor recognition. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). Seems to recognize the type D mammalian retrovirus receptors SLC1A4 and SLC1A5, as it induces fusion of cells expressing these receptors in vitro.
The transmembrane protein (TM) acts as 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 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.
SU mediates receptor recognition. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). Seems to recognize the type D mammalian retrovirus receptors SLC1A4 and SLC1A5, as it induces fusion of cells expressing these receptors in vitro.
The transmembrane protein (TM) acts as 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 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.
Also known as:
HERV-W_7q21.2 provirus ancestral Env polyprotein; Endogenous retrovirus group W member 1; env; Env-W; Envelope polyprotein gPr73; Enverin; ENW1_HUMAN; ERVW; ERVW-1; Gp24; Gp50; HERV-7q Envelope protein; HERV-W envelope protein; HERVW; SU; Syncytin 1; Syncytin; Syncytin-1; TM; Transmembrane protein; Surface protein.
Specificity:
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Rabbit Polyclonal IgG, affinity purified by Protein A.
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Reacts with:
(predicted: )
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Immunogen: KLH conjugated synthetic peptide derived from human Syncytin 1.
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Predicted Molecular Weight: 33/58kDa.
Storage:
0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Application:
Excitation spectrum: 488nm,561nm,743nm
Emission spectrum: 785nm
Not yet tested in other applications.
Optimal working dilutions must be determined by the end user.
Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.