glycoprotein/G Protein, HRSV (sf9, His)

A glycoprotein/G protein critical in the immune response forms the interleukin-31 receptor with OSMR.This receptor activates STAT3 and, to a lesser extent, STAT1 and STAT5, playing a critical role in skin immunity and mediating IL31-induced itch, possibly involving TRPA1 and TRPV1.glycoprotein/G Protein, HRSV (sf9, His) is the recombinant Virus-derived glycoprotein/G protein, expressed by Sf9 insect cells , with C-His labeled tag.

The glycoprotein/G Protein, a crucial component of the immune response, forms the interleukin-31 receptor by associating with OSMR. This receptor plays a vital role in activating STAT3, as well as STAT1 and STAT5 to a lesser extent. It is known to be involved in skin immunity and is responsible for mediating IL31-induced itch, potentially by relying on cation channels TRPA1 and TRPV1. Moreover, the glycoprotein/G Protein positively regulates the numbers and cycling status of immature subsets of myeloid progenitor cells in the bone marrow, both in vivo and in vitro, thereby enhancing myeloid progenitor cell survival. It forms a heterodimer with OSMR and interacts with JAK1 and STAT3 to carry out its functions. In terms of viral infection, this glycoprotein/G Protein attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection process. It also interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike other paramyxovirus attachment proteins, it lacks both neuraminidase and hemagglutinating activities. Additionally, it aids the virus in escaping antibody-dependent restriction of replication by acting as an antigen decoy and modulating the activity of leukocytes bearing Fc-gamma receptors.

Virus

Sf9 insect cells

C-His

P27022 (N66-R297)

/

Partial

NHKITSTTTIIQDATNQIKNTTPTYLTQNPQLGISPSNPSDITSLITTILDSTTPGVKSTLQSTTVGTKNTTTTQAQPNKPTTKQRQNKPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKRTTTKPTKKPTPKTTKKGPKPQTTKSKEAPTTKPTEEPTINTTKTNIITTLLTSNTTRNPELTSQMETFHSTSSEGNPSPSQVSITSEYPSQPSSPPNTPR

Approximately 40-55 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.