Recombinant Lassa Virus Pre-Glycoprotein Polyprotein Gp Complex (GPC) Protein (His&Myc)

Name: Recombinant Lassa Virus Pre-Glycoprotein Polyprotein Gp Complex (GPC) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-03433P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Lassa Virus Pre-Glycoprotein Polyprotein Gp Complex (GPC) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P08669
Target Symbol	GPC
Synonyms	GPC; GP-C; Pre-glycoprotein polyprotein GP complex; Pre-GP-C
Species	Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	TSLYKGVYELQTLELNMETLNMTMPLSCTKNNSHHYIMVGNETGLELTLTNTSIINHKFCNLSDAHKKNLYDHALMSIISTFHLSIPNFNQYEAMSCDFNGGKISVQYNLSHSYAGDAANHCGTVANGVLQTFMRMAWGGSYIALDSGRGNWDCIMTSYQYLIIQNTTWEDHCQFSRPSPIGYLGLLSQRTRDIYISRRLL
Expression Range	59-259aa
Protein Length	Partial
Mol. Weight	27.8 kDa
Research Area	Signal Transduction
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	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.; 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.
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:956585

Gene Functions References

The data suggest that the alpha-dystroglycan binding site on Lassa virus GP1 is found at the top central core of the GP trimer. PMID: 28679759
A unique triad of histidines of Lassa Virus GP1 forms a binding site for host LAMP1. PMID: 25972533
implicate GP1 as a chaperone for the correct processing and shuttling of GP2 to the cell surface, and suggest that native GPC SP plays a role in this process PMID: 19105844

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.