Recombinant Suid herpesvirus 1 Envelope glycoprotein B(gB),partial CSB-EP362400SRH
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
(gB)
Species: (Organism)
Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1) (Pseudorabies virus (strain Indiana-Funkhauser / Becker))
Gene Names:
gB
Tag info:
C-terminal 6xHis-tagged
Target Protein AA Sequence:
RHISRLRRNPMKALYPVTTKTLKEDGVDEGDVDEAKLDQARDMIRYMSIVSALEQQEHKARKKNSGPALLASRVGAMATRRRHYQRLESEDPDAL
Expression Region:
819-913aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Partial
Pathway:
Mol. Weight:
11.8 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Others
Function:
Involvement in disease:
Relevance:
Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.
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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Reference:
"The export pathway of the pseudorabies virus gB homolog gII involves oligomer formation in the endoplasmic reticulum and protease processing in the Golgi apparatus." Whealy M.E., Robbins A.K., Enquist L.W. J. Virol. 64:1946-1955(1990)
