Recombinant GP protein is a Tai Forest virus - Cote d'Ivoire, Cote d'Ivoire, 1994 Fragment protein, in the 33 to 304 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
>90% SDS-PAGE
< 1 EU/µg
HEK 293 cells
His tag C-Terminus
SDS-PAGE
No
I P L G V V H N N T L Q V S D I D K L V C R D K L S S T S Q L K S V G L N L E G N G V A T D V P T A T K R W G F R A G V P P K V V N Y E A G E W A E N C Y N L D I K K A D G S E C L P E A P E G V R G F P R C R Y V H K V S G T G P C P E G Y A F H K E G A F F L Y D R L A S T I I Y R S T T F S E G V V A F L I L P E T K K D F F Q S P P L H E P A N M T T D P S S Y Y H T V T L N Y V A D N F G T N M T N F L F Q V D H L T Y V Q L E P R F T P Q F L V Q L N E T I Y T N G R R S N T T G T L I W K V N P T V D T G V G E W A F W E N K K N F T K T L S S E
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes DTT-reduced Protein migrates as 40-60 kDa in SDS-PAGE |
GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection). Binding to the macrophage specific lectin CLEC10A also seems to enhance virus infectivity. Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory. Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection. Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L presumably induces a conformational change of GP2, unmasking its fusion peptide and initiating membranes fusion (By similarity).GP2 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 viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide (By similarity).Envelope glycoproteinGP1,2 which is the disulfid-linked complex of GP1 and GP2, mediates endothelial cell activation and decreases endothelial barrier function. Mediates activation of primary macrophages. At terminal stages of the viral infection, when its expression is high, GP1,2 down-modulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion. Down-modulates integrins ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1. GP1,2 alters the cellular recycling of the dimer alpha-V/beta-3 via a dynamin-dependent pathway. Decrease in the host cell surface expression of various adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during Ebola virus infection (cytotoxicity). This cytotoxicity appears late in the infection, only after the massive release of viral particles by infected cells. Down-modulation of host MHC-I, leading to altered recognition by immune cells, may explain the immune suppression and inflammatory dysfunction linked to Ebola infection. Also down-modulates EGFR surface expression. Counteracts the antiviral effect of host tetherin (By similarity).GP2delta is part of the complex GP1,2delta released by host ADAM17 metalloprotease. This secreted complex may play a role in the pathogenesis of the virus by efficiently blocking the neutralizing antibodies that would otherwise neutralize the virus surface glycoproteins GP1,2. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. GP1,2delta does not seem to be involved in activation of primary macrophages (By similarity).
Envelope glycoprotein, GP, GP
Recombinant GP protein is a Tai Forest virus - Cote d'Ivoire, Cote d'Ivoire, 1994 Fragment protein, in the 33 to 304 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
>90% SDS-PAGE
< 1 EU/µg
HEK 293 cells
His tag C-Terminus
SDS-PAGE
No
No
Tai Forest virus - Cote d'Ivoire, Cote d'Ivoire, 1994
Reconstitute at 200 µg/mL in water
pH: 7.54
Constituents: 99% PBS
I P L G V V H N N T L Q V S D I D K L V C R D K L S S T S Q L K S V G L N L E G N G V A T D V P T A T K R W G F R A G V P P K V V N Y E A G E W A E N C Y N L D I K K A D G S E C L P E A P E G V R G F P R C R Y V H K V S G T G P C P E G Y A F H K E G A F F L Y D R L A S T I I Y R S T T F S E G V V A F L I L P E T K K D F F Q S P P L H E P A N M T T D P S S Y Y H T V T L N Y V A D N F G T N M T N F L F Q V D H L T Y V Q L E P R F T P Q F L V Q L N E T I Y T N G R R S N T T G T L I W K V N P T V D T G V G E W A F W E N K K N F T K T L S S E
Fragment
31.8 kDa
33 to 304
Recombinant
His tag C-Terminus
Lyophilized
GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection). Binding to the macrophage specific lectin CLEC10A also seems to enhance virus infectivity. Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory. Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection. Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L presumably induces a conformational change of GP2, unmasking its fusion peptide and initiating membranes fusion (By similarity).
Belongs to the filoviruses glycoprotein family.
The signal peptide region modulates GP's high mannose glycosylation, thereby determining the efficiency of the interactions with DC-SIGN(R).
Blue Ice
-20°C
-20°C
Upon delivery aliquot, Upon reconstitution add a carrier protein (0.1% BSA)
Avoid freeze / thaw cycle
This product is stable after storage at:
This supplementary information is collated from multiple sources and compiled automatically.
The GP also called glycoprotein serves many mechanical roles. It weighs about 60-90 kDa though some specific forms might differ. GP is mainly expressed on cell membranes where it participates in cellular recognition and signaling. It can also appear in blood plasma and secretions. The variations in its structure allow GP to interact with different molecules leading to various effects.
Glycoprotein plays a role in immune response and cell signaling. It often forms part of larger protein complexes on the cell surface. This involvement supports cell adhesion and communication. Additionally GP assists in various cellular transport mechanisms facilitating the proper functioning of cells under normal physiological conditions.
Different glycoproteins often find functions in the immune and signaling pathways. For example the GP forms connections with the TGF-beta signaling pathway. It also works in conjunction with integrin-related pathways which are important for cell adhesion processes. Through these pathways GP aligns with other proteins such as integrins and ground substance components allowing efficient cellular interactions.
Glycoproteins stand linked with diseases like cancer and diabetes. Aberrant GP expression or function can contribute to the proliferation of cancer cells by altering communication signals. In diabetes GP anomalies may influence insulin signaling pathways and glucose transport. Proteins like insulin receptor also associate with GP in the context of diabetes affecting the cascade of metabolic signals within the body.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
The purity of ab199980 was determined by DTT-reduced SDS-PAGE and staining overnight with Coomassie Blue. DTT-reduced Protein migrates as 40-60 kDa in SDS-PAGE due to glycosylation.
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com