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Recombinant Epstein-Barr virus Envelope glycoprotein GP350 (BLLF1), partial

Recombinant Epstein-Barr virus Envelope glycoprotein GP350 (BLLF1), partial

CSB-EP360986EFA

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Size:

20ug100ug1mg(1mg*1 or 500ug*2)

US$388

Quantity:

Express system: E.coli

Species: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)

Tag Info: N-terminal 6xHis-SUMO-tagged

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Product Details
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Target Background

Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

BLLF1

Uniprot NO.

P03200

Research Area

Others

Alternative Names

Membrane antigen Short name: MA

Species

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)

Source

E.coli

Expression Region

1-493aa

Target Protein Sequence

MEAALLVCQYTIQSLIHLTGEDPGFFNVEIPEFPFYPTCNVCTADVNVTINFDVGGKKHQLDLDFGQLTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINVTTGEEQQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPYIKWDNCNSTNITAVVRAQGLDVTLPLSLPTSAQDSNFSVKTEMLGNEIDIECIMEDGEISQVLPGDNKFNITCSGYESHVPSGGILTSTSPVATPIPGTGYAYSLRLTPRPVSRFLGNNSILYVFYSGNGPKASGGDYCIQSNIVFSDEIPASQDMPTNTTDITYVGDNATYSVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPSGCENISGAFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFADPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPS

Mol. Weight

68.5kDa

Protein Length

Partial

Tag Info

N-terminal 6xHis-SUMO-tagged

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.

Storage

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.

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.

Troubleshooting and FAQs

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Datasheet & COA

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Images

(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-EP360986EFA could indicate that this peptide derived from E.coli-expressed Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) BLLF1.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP360986EFA could indicate that this peptide derived from E.coli-expressed Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) BLLF1.

Description

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Target Background

Function

Initiates virion attachment to host B-lymphocyte cell, leading to virus entry. Acts by binding to host CR2 at the surface of B-lymphocytes, facilitating the binding of viral glycoprotein gp42 to HLA class II molecules. Attachment triggers virion-host membrane fusion and invasion of the host cell.

Gene References into Functions

The similar distribution of gp350/220 variants in nasopharyngeal carcinoma, EBV-associated gastric carcinoma and healthy donors suggest that gp350/220 variations are geographically restricted rather than tumor-specific polymorphisms. PMID:22038027
gp350 mainly exerts its functions after the internalization step, presumably during release of the viral capsid from the endosomal compartment, and that CD21-dependent but also CD21-independent molecular mechanisms are involved in this process. PMID:19889766
X-ray structure of the highly glycosylated gp350; defined the CR2 binding site on gp350, deglycosylated gp350 bound CR2 similarly to the glycosylated form, suggesting that glycosylation is not important for receptor binding PMID:17072314
These site-directed mutations identified a novel negatively charged complement receptor type 2-binding surface described by residues Glu-21, Asp-22, Glu-155, Asp-208, Glu-210, and Asp-296. PMID:18786993