Recombinant Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein / GP1 (mucin domain deleted) Protein (aa:Met1-Asp320, His Tag)

Collections: Ebola, Featured viral antigens molecules, Recombinant proteins, Viral antigen

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Product Overview

Tag	His
Host Species	Ebola virus EBOV
Accession	Q7T9D9
Description	A DNA sequence encoding Sudan ebolavirus (strain Uganda-00) GP (Q7T9D9.1) (Met1-Asp320) was produced with a His tag at the C-terminus.
Source	Insect Cells
Predicted N Terminal	Met 33
AA Sequence	Met1-Asp320
Molecular Weight	The recombinant Sudan ebolavirus (strain Uganda-00) GP consists 299 amino acids and predicts a molecular mass of 33.8 kDa.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Formulation	This product was lyophilized from sterile 20 mM Tris, 500 mM NaCl, 10 % glycerol,pH 7.4.
Stability	Recombinant antigens are stable for up to 1 year from date of receipt at -80°C
Applications	ELISA; immunogen; WB, etc.
Usage	For Research Use Only
Storage	Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Please avoid repeated freeze-thaw cycles.

Target Details

Target Function	Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, downregulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion. Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1. This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes. Downregulates as well the function of host natural killer cells. Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells. However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation.; Functions as a decoy for anti-GP1,2 antibodies thereby contributing to viral immune evasion. Interacts and activates host macrophages and dendritic cells inducing up-regulation of cytokine transcription. This effect is mediated throught activation of host TLR4.; 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 dendritic cells (DCs) and endothelial cells. 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 removes the glycan cap and allows GP1 binding to the host entry receptor NPC1. NPC1-binding, Ca(2+) and acidic pH induce a conformational change of GP2, which unmasks its fusion peptide and permit membranes fusion.; 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.
Subcellular Location	[GP2]: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein.; [GP1]: Virion membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein.; [Shed GP]: Secreted.
Protein Families	Filoviruses glycoprotein family
Database References	KEGG: vg:3160774

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.