This product is a recombinant Mouse antibody that can recognize HCV E2. DAO5 specifically recognizes a linear epitope comprising part of the CD81 binding loop and the E strand of the central β-sandwich within HCV E2.
Figure 1 Mouse Anti-HCV E2 Antibody (DAO5) in SDS-PAGE.
Cross-competition profile of DAO5. (A) Cross-competition and biochemical analysis of the sE2412-715-DAO5 complex. (Left) sE2412-715 and an sE2412-715-DAO5 scFv complex were affinity loaded onto a StrepTactin column, a CBH-4D Fab fragment was added, and the eluted complex was analyzed by SDS-PAGE under nonreducing conditions. (Right) CD81-LEL was incubated overnight at RT with the full-length HCV ectodomain (comprising residues 384 to 715; sE2) and the sE2-DAO5 Fab complex, followed by SEC and analysis of the peak fractions by SDS-PAGE under reducing conditions. DAO5 heavy and light chains form an apparent single band in the reducing gel due to an almost identical molecular mass of ~24 kDa.
Vasiliauskaite I, Owsianka A, England P, et al. Conformational flexibility in the immunoglobulin-like domain of the hepatitis C virus glycoprotein E2[J]. MBio, 2017, 8(3): e00382-17.
Figure 2 Mouse Anti-HCV E2 Antibody (DAO5) in SEC-HPLC.
A preformed sE2412-715-DAO5 Fab complex was incubated in the absence or presence of a Fab fragment targeting a non-overlapping (AP33) or overlapping (e137) region of cE2 and analyzed by SEC. After preincubation with AP33 (green), appearance of a peak at a higher molecular mass indicated ternary complex formation; after preincubation with e137 Fab (blue), the presence of peaks corresponding to the binary complex (at ~13 ml) and an isolated Fab fragment (at ~16 ml) showed that no ternary complex was formed.
Vasiliauskaite I, Owsianka A, England P, et al. Conformational flexibility in the immunoglobulin-like domain of the hepatitis C virus glycoprotein E2[J]. MBio, 2017, 8(3): e00382-17.
Figure 3 Mouse Anti-HCV E2 Antibody (DAO5) in SDS-PAGE.
sE2412-715 or sE2 was immobilized on a StrepTactin column and incubated first with a molar excess of DAO5 scFv and subsequently with e137.
Vasiliauskaite I, Owsianka A, England P, et al. Conformational flexibility in the immunoglobulin-like domain of the hepatitis C virus glycoprotein E2[J]. MBio, 2017, 8(3): e00382-17.
Figure 4 Mouse Anti-HCV E2 Antibody (DAO5) in SPR.
Real-time SPR analysis of Fab binding to immobilized sE2 recorded the binding response (in resonance units [RU]) as a function of time. Fab fragments of e137 and DAO5 were injected over a surface with immobilized HCV sE2.
Vasiliauskaite I, Owsianka A, England P, et al. Conformational flexibility in the immunoglobulin-like domain of the hepatitis C virus glycoprotein E2[J]. MBio, 2017, 8(3): e00382-17.
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
See more details about Hi-Affi™ recombinant antibody benefits.
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CAT | Product Name | Application | Type |
---|---|---|---|
PABL-495 | Mouse Anti-HCV E2 Protein Recombinant Antibody (PABL-495) | ELISA, Neut | Mouse IgG |
PABL-496 | Recombinant Mouse Anti-HCV E2 Antibody (AP33) | FC, Neut, FuncS | IgG |
PABL-497 | Recombinant Human Anti-HCV E2 Antibody (AR3C) | Neut | IgG |
PABL-498 | Recombinant Human Anti-HCV E2 Antibody (C2) | Neut | IgG |
PABL-499 | Recombinant Human Anti-HCV E2 Antibody (HC33.8) | Neut | IgG |
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For Research Use Only. Not For Clinical Use.
For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.
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