Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P20895 |
express system | HEK293 |
product tag | N-His |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Glycoprotein G (gG) here refers to the adhesion protein on the surface of RSV, It is a type II glycoprotein and one of the two main envelope glycoproteins of RSV. Glycoprotein G can bind to the host cell membrane receptor and mediate the entry of the virus into the host cell. |
molecular weight | The protein has a predicted MW of 26.29 kDa. Due to glycosylation, the protein migrates to 90-110 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
HRSV (A, strain Long) Glycoprotein G Protein 2856
$225.00 – $750.00
Summary
- Expression: HEK293
- Pure: Yes (HPLC)
- Amino Acid Range: His67-Gln298
HRSV (A, strain Long) Glycoprotein G Protein 2856
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Glycoprotein G (gG) here refers to the adhesion protein on the surface of RSV, It is a type II glycoprotein and one of the two main envelope glycoproteins of RSV. Glycoprotein G can bind to the host cell membrane receptor and mediate the entry of the virus into the host cell. |
Protein names Major surface glycoprotein G (Attachment glycoprotein G) (Membrane-bound glycoprotein) (mG) [Cleaved into: Mature secreted glycoprotein G (Mature sG)] |
Gene names G,G |
Protein family Pneumoviruses glycoprotein G family |
Mass 11250Da |
Function [Isoform Membrane-bound glycoprotein G]: Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities.; [Isoform Secreted glycoprotein G]: Helps the virus escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fc-gamma receptors. |
Catalytic activity #N/A |
Subellular location [Isoform Membrane-bound glycoprotein G]: Virion membrane ; Single-pass type II membrane protein. Host cell membrane ; Single-pass type II membrane protein .; [Isoform Secreted glycoprotein G]: Secreted. Note=The protein is shed from infected cells before the appearance of progeny virus (PubMed:3373568). The initiation at the downstream methionine removes a portion of the transmembrane domain. The remaining hydrophobic portion of the sG protein is essential for translocating it into the lumen of the ER during translation and would likely maintain its membrane association until a proteolytic event releases the mature sG protein into the medium (Probable). |
Structure [Isoform Membrane-bound glycoprotein G]: Homooligomer. Interacts (via N-terminus) with protein M. Part of a complex composed of F1, F2 and G glycoproteins. Interacts with protein SH. Interacts with host heparate sulfate; this interaction probably participates in the viral attachment to the host cell. Interacts with host CX3CR1; this interaction plays an important role in viral entry. Interacts with the host lectins CD209/DC-SIGN and CD209L/L-SIGN on dendritic cells; these interactions stimulate the phosphorylation of MAPK3/ERK1 and MAPK1/ERK2, which inhibits dendritic cell activation and could participate in the limited immunity against RSV reinfection. |
Post-translational modification [Isoform Secreted glycoprotein G]: Cleaved to give rise to the mature sG protein which lacks the transmembrane domain. |
Domain [I |
Target Relevance information above includes information from UniProt accession: P20895 |
The UniProt Consortium |
Data
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