Recombinant Epstein-Barr Virus Envelope Glycoprotein L (GL) Protein (His-SUMO)

Name: Recombinant Epstein-Barr Virus Envelope Glycoprotein L (GL) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08983P
Availability: InStock

Greater than 90% 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 Epstein-Barr Virus Envelope Glycoprotein L (GL) 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	P03212
Target Symbol	GL
Synonyms	gL; BKRF2Envelope glycoprotein L; gL
Species	Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	NWAYPCCHVTQLRAQHLLALENISDIYLVSNQTCDGFSLASLNSPKNGSNQLVISRCANGLNVVSFFISILKRSSSALTGHLRELLTTLETLYGSFSVEDLFGANLNRYAWHRGG
Expression Range	23-137aa
Protein Length	Full Length of Mature Protein
Mol. Weight	28.7kDa
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	The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH. Fusion of EBV with B-lymphocytes requires the additional receptor-binding protein gp42, which forms a complex with gH/gL. The heterodimer gH/gL targets also host EPHA2 to promote viral entry.
Subcellular Location	Virion membrane; Peripheral membrane protein; Extracellular side. Host cell membrane; Peripheral membrane protein; Extracellular side. Host Golgi apparatus, host trans-Golgi network.
Protein Families	Herpesviridae glycoprotein L family
Database References	KEGG: vg:3783710

Gene Functions References

Here, the authors demonstrate that the BKRF2 gene behaves as a true-late lytic gene, whereas the BKRF3 and BKRF4 genes belong to the early lytic gene family. The results further reveal that both BKRF3 and BKRF4 promoters are new synergistic targets of Zta and Rta, two Epstein-Barr virus latent-to-lytic switch transactivators. PMID: 30096410
The critical regulator of EBV tropism is the gp42 N-terminal domain, which tethers the HLA-binding domain to gHgL by wrapping around the exterior of three gH domains. PMID: 27929061
Findings suggest that EBV gH/gL detection complements viral capsid antigen (VCA) detection in the diagnosis of nasopharyngeal carcinoma (NPC) and aids in the identification of patients with VCA-negative NPC. PMID: 27093005
The KGD motif of Epstein-Barr virus gH/gL directs EBV fusion of B cells and epithelial cells. PMID: 22215569
Data show that the gL subunit and N-terminal residues of gH form a globular domain at one end of the structure. PMID: 21149717

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.