Recombinant Lymphocytic Choriomeningitis Virus Pre-Glycoprotein Polyprotein Gp Complex (GPC) Protein (His/Tag-Free)

Name: Recombinant Lymphocytic Choriomeningitis Virus Pre-Glycoprotein Polyprotein Gp Complex (GPC) Protein (His/Tag-Free)
Brand: Beta LifeScience
SKU: BLC-11298P
Availability: InStock

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

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Product Overview

Description	Recombinant Lymphocytic Choriomeningitis Virus Pre-Glycoprotein Polyprotein Gp Complex (GPC) Protein (His/Tag-Free) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P09991
Target Symbol	GPC
Synonyms	GPC; GP-C; Segment; S; Pre-glycoprotein polyprotein GP complex; Pre-GP-C
Species	Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV)
Expression System	Yeast
Tag	N-His/Tag-Free
Protein Length	full length protein
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.
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	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.
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 References	KEGG: vg:956591

Gene Functions References

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

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.