Recombinant Zaire Ebolavirus Pre-Small/Secreted Glycoprotein (GP) Protein (His-SUMO)

Name: Recombinant Zaire Ebolavirus Pre-Small/Secreted Glycoprotein (GP) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10562P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Zaire Ebolavirus Pre-Small/Secreted Glycoprotein (GP) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P60171
Target Symbol	GP
Synonyms	GP; Pre-small/secreted glycoprotein; pre-sGP) [Cleaved into: Small/secreted glycoprotein; sGP); Delta-peptide]
Species	Zaire ebolavirus (strain Kikwit-95) (ZEBOV) (Zaire Ebola virus)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	IPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKTSLEKFAVKSCLSQLYQTEPKTSVVRVRRELLPTQGPTQQLKTTKSWLQKIPLQWFKCTVKEGKLQCRI
Expression Range	33-364aa
Protein Length	Full Length of Mature Protein
Mol. Weight	53.3kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	sGP seems to possess an anti-inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. Does not seem to be involved in activation of primary macrophages. Does not seem to interact specifically with neutrophils.; Viroporin that permeabilizes mammalian cell plasma membranes. It acts by altering permeation of ionic compounds and small molecules. This activity may lead to viral enterotoxic activity.
Subcellular Location	[Small/secreted glycoprotein]: Secreted.; [Delta-peptide]: Secreted.
Protein Families	Filoviruses glycoprotein family

Gene Functions References

Growth-Adaptive Mutations in the Ebola Virus Makona Glycoprotein Alter Different Steps in the Virus Entry Pathway. PMID: 30021890
the structure of the membrane proximal external region (MPER) connected to the TM domain: i.e., the missing parts of the EBOV GP2 structure. The structure, solved by solution NMR and EPR spectroscopy in membrane-mimetic environments, consists of a helix-turn-helix architecture that is independent of pH. PMID: 28874543
Ebola virus GP directly subverts the host's immune response by increasing the susceptibility of monocytes to Ebola virus infection. PMID: 28542576
report provides experimental evidence that the spontaneous mutation T544I is a tissue culture adaptation in certain cell lines and that it may be unique for the species Zaire ebolavirus; the mutation led to a marked increase in virus growth kinetics and conferred a robust growth advantage over wild-type rVSV-MAK-GP on Vero E6 cells PMID: 28539437
although Asn(563) and Asn(618) are not required for EBOV GP expression, they synergistically regulate its maturation, which determines its functionality. PMID: 28196864
Study determined the crystal structure of the primed GP (GPcl) of Ebola virus bound to domain C of NPC1 (NPC1-C); NPC1-C utilizes two protruding loops to engage a hydrophobic cavity on head of GPcl. Upon enzymatic cleavage and NPC1-C binding, conformational change in the GPcl further affects the state of the internal fusion loop, triggering membrane fusion. PMID: 26771495
GP1,2 expression levels have a profound effect on factors that contribute to virus fitness and RNA editing may be an important mechanism employed by EBOV to regulate GP1,2 expression in order to optimize virus production and infectivity. PMID: 25392212
Mucin-like domain is located at the apex and the sides of each glycoprotein monomer. PMID: 25008940
The glycoprotein's internal fusion loop is critical for viral entry and fusion. PMID: 24696482
GP play multiple functions including virus attachment and entry, cell rounding and cytotoxicity and down-regulation of host surface proteins.[review] PMID: 23757858
findings demonstrate that a GP mutant, GP-F88A, defective for entry into a variety of human cell types, including antigen-presenting cells (APCs) can mediate viral entry into mouse CD11b( ) APCs; studies suggest an important role for NPC1 in the differential entry of GP-F88A into mouse versus human APCs PMID: 23302883
Purified human NPC1 binds only to a cleaved form of Ebola virus spike glycoprotein that is generated within cells during entry, and only viruses containing cleaved glycoprotein can utilize a receptor retargeted to the cell surface. PMID: 22395071
Ebola virus GP forms a tandem beta-hairpin structure that binds deeply into a cleft in the antibody-combining site. PMID: 22171276
Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for efficient entry into cell lines and macrophages independent of TMPRSS2 expression. PMID: 22222211
Cathepsin L cleavage potentiates the Ebola virus GP to undergo a fusion-relevant conformational change. PMID: 22031933
R64 and K95 of GP1 are involved in receptor binding. PMID: 21667336
liposome fusion data and NMR structures for a complete (54-residue) disulfide-bonded internal fusion loop (Ebov FL) in a membrane mimetic PMID: 21690393
Axl enhances entry of Zaire ebolavirus without direct interactions with the viral glycoprotein. PMID: 21529875
While ssGP appears to share similar structural properties with sGP, it does not appear to have the same anti-inflammatory function on endothelial cells as sGP. PMID: 21411529
These findings suggest that Ebola virus GP uses a novel mechanism to circumvent tetherin restriction. PMID: 20444895
CatB cleavage is required to facilitate the triggering of viral membrane fusion by destabilizing the prefusion conformation of EBOV GP PMID: 19846533
Ebola virus GP cytotoxicity is regulated by dynamin-dependent cellular protein trafficking PMID: 15596847
The transmembrane region of GP2 modifies the permeability of the plasma membrane. PMID: 16927113
the crystal structure of EBOV GP in its trimeric, pre-fusion conformation (GP1+GP2) bound to a neutralizing antibody, KZ52, derived from a human survivor of the 1995 Kikwit outbreak PMID: 18615077
The authors show that the mucin domain from the highly pathogenic Zaire subtype of Ebola virus is sufficient to cause characteristic cytopathology when expressed in the context of a foreign glycoprotein. PMID: 19013626

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.