Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

GPC

Uniprot No.

P09991

Alternative Names

GPC; GP-C; Segment; S; Pre-glycoprotein polyprotein GP complex; Pre-GP-C

Species

Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV)

Source

E.coli

Expression Region

266-498aa

Target Protein Sequence

GTFTWTLSDSSGVENPGGYCLTKWMILAAELKCFGNTAVAKCNVNHDAEFCDMLRLIDYNKAALSKFKEDVESALHLFKTTVNSLISDQLLMRNHLRDLMGVPYCNYSKFWYLEHAKTGETSVPKCWLVTNGSYLNETHFSDQIEQEADNMITEMLRKDYIKRQGSTPLALMDLLMFSTSAYLVSIFLHLVKIPTHRHIKGGSCPKPHRLTNKGICSCGAFKVPGVKTVWKRR
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

42.4kDa

Protein Length

Partial

Tag Info

N-terminal 6xHis-SUMO-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The Glycoprotein precursor (GPC) is a crucial protein found in arenaviruses that undergoes posttranslational cleavage to produce the components forming the GP complex. The GPC is expressed as a polyprotein that is co-translationally cleaved to yield the stable signal peptide (SSP), GP1, and GP2 subunits [1][2]. Maturation of the GPC involves proteolytic cleavage into the SSP, GP1 attachment glycoprotein, and GP2 fusion glycoprotein [3]. The mature GPC complex is metastable and is primed to mediate membrane fusion in response to acidic pH [4]. The virion form of GPC is a trimer of heterodimers containing the receptor-binding subunit GP1 and the fusion-mediating subunit GP2 [5]. The GPC precursor is proteolytically cleaved by the cellular subtilase SKI-1/S1P to yield the mature glycoproteins G1 and G2 [6].

The GPC is essential for the assembly and function of arenaviruses, playing a critical role in viral entry into host cells and serving as a target for antibody-mediated neutralization [5]. The processing of the GPC precursor is a highly regulated mechanism involving cellular enzymes and proteases [7]. The signal peptide of the GPC is myristoylated and forms an essential subunit of the mature G1-G2 complex [6]. Additionally, the GPC precursor undergoes cleavage to generate the GP1 and GP2 subunits, which are crucial for viral attachment and membrane fusion [8].

References:
[1] A. Capul, M. Perez, E. Burke, S. Kunz, M. Buchmeier, & J. Torre, "Arenavirus z-glycoprotein association requires z myristoylation but not functional ring or late domains", Journal of Virology, vol. 81, no. 17, p. 9451-9460, 2007. https://doi.org/10.1128/jvi.00499-07
[2] R. Iheozor-Ejiofor, L. Levanov, J. Hepojoki, T. Strandin, Å. Lundkvist, A. Plyusninet al., "Vaccinia virus-free rescue of fluorescent replication-defective vesicular stomatitis virus and pseudotyping with puumala virus glycoproteins for use in neutralization tests", Journal of General Virology, vol. 97, no. 5, p. 1052-1059, 2016. https://doi.org/10.1099/jgv.0.000437
[3] R. Pryce, W. Ng, A. Zeltina, Y. Watanabe, K. Omari, A. Wagneret al., "Structure-based classification defines the discrete conformational classes adopted by the arenaviral gp1", Journal of Virology, vol. 93, no. 1, 2019. https://doi.org/10.1128/jvi.01048-18
[4] E. Messina, J. York, & J. Nunberg, "Dissection of the role of the stable signal peptide of the arenavirus envelope glycoprotein in membrane fusion", Journal of Virology, vol. 86, no. 11, p. 6138-6145, 2012. https://doi.org/10.1128/jvi.07241-11
[5] K. Hastie, M. Zandonatti, L. Kleinfelter, M. Heinrich, M. Rowland, K. Chandranet al., "Structural basis for antibody-mediated neutralization of lassa virus", Science, vol. 356, no. 6341, p. 923-928, 2017. https://doi.org/10.1126/science.aam7260
[6] J. York, V. Romanowski, M. Lu, & J. Nunberg, "The signal peptide of the junín arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature g1-g2 complex", Journal of Virology, vol. 78, no. 19, p. 10783-10792, 2004. https://doi.org/10.1128/jvi.78.19.10783-10792.2004
[7] D. Burri, G. Pasqual, C. Rochat, N. Seidah, A. Pasquato, & S. Kunz, "Molecular characterization of the processing of arenavirus envelope glycoprotein precursors by subtilisin kexin isozyme-1/site-1 protease", Journal of Virology, vol. 86, no. 9, p. 4935-4946, 2012. https://doi.org/10.1128/jvi.00024-12
[8] D. Burri, J. Palma, S. Kunz, & A. Pasquato, "Envelope glycoprotein of arenaviruses", Viruses, vol. 4, no. 10, p. 2162-2181, 2012. https://doi.org/10.3390/v4102162

Target Background

Function

class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.; Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.; interacts with the host receptor. Mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis.

Gene References into Functions

The viral glycoprotein precursor (GPC)was responsible for the induction of ATF6 regulated branch of the host cell's unfolded protein response. PMID: 21106748
N-linked glycan mutations at positions 87 and 97 on GP1 resulted in reduction of expression and absence of cleavage and were necessary for downstream functions, as confirmed by the loss of GP-mediated fusion activity with T87A and S97A mutants. PMID: 21056893
the LCMV GP is a trimer and must be considered a member of the class I viral fusion protein family PMID: 16731928
The stable signal peptide of the lymphocytic choriomeningitis virus surface glycoprotein precursor is involved in the glycoprotein (GP) precursor expression, processing, cell surface localization, particle formation and GP-mediated fusion. PMID: 17376927

Subcellular Location

[Glycoprotein G1]: Virion membrane; Peripheral membrane protein. Host endoplasmic reticulum membrane; Peripheral membrane protein. Host Golgi apparatus membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein.; [Glycoprotein G2]: Virion membrane; Single-pass membrane protein. Host endoplasmic reticulum membrane; Single-pass membrane protein. Host Golgi apparatus membrane; Single-pass membrane protein. Host cell membrane; Single-pass membrane protein.; [Stable signal peptide]: Virion membrane; Multi-pass membrane protein. Host endoplasmic reticulum membrane; Multi-pass membrane protein. Host Golgi apparatus membrane; Multi-pass membrane protein. Host cell membrane; Multi-pass membrane protein.

Protein Families

Arenaviridae GPC protein family

Database Links

KEGG: vg:956591

Code	CSB-EP357830LKW
Abbreviation	Recombinant Lymphocytic choriomeningitis virus GPC protein, partial
MSDS	MSDS Datasheet
Size	US$388
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel. Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP357830LKW could indicate that this peptide derived from E.coli-expressed Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV) GPC. Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP357830LKW could indicate that this peptide derived from E.coli-expressed Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV) GPC.
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Recombinant Lymphocytic choriomeningitis virus Pre-glycoprotein polyprotein GP complex (GPC), partial

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