This recombinant monoclonal antibody to Mycobacterium tuberculosis acyl-carrier protein (ACP) 2 is a Synthetic construct monoclonal antibody that can be used for applications: ELISA.
Figure 1 Ligand binding
Antibody affinity was first determined by yeast display titrations (●), and then improved through random mutagenesis and in vitro selection using FACS, yielding affinity improvement from an apparent Kd =
900-50 nM in 2acp12 (○).
Baran, D., Pszolla, M. G., Lapidoth, G. D., Norn, C., Dym, O., Unger, T., ... & Fleishman, S. J. (2017). Principles for computational design of binding antibodies. Proceedings of the National Academy of Sciences, 114(41), 10900-10905.
Figure 2 Surface plasmon resonance traces.
The antibodies were expressed as Fab- and aminecoupled to CM5 chips. The affinities determined from the kinetic fits were 100 nM for 2acp12.
Baran, D., Pszolla, M. G., Lapidoth, G. D., Norn, C., Dym, O., Unger, T., ... & Fleishman, S. J. (2017). Principles for computational design of binding antibodies. Proceedings of the National Academy of Sciences, 114(41), 10900-10905.
Figure 3 Mutation analysis of designed binding modes.
Relative binding signal of variants containing single-point mutations in ligand-binding sites (gray bars) or outside the ligand-binding sites (black bars). Additional manual mutations were introduced on the ligand ACP (cyan spheres) in the intended binding surface (gray bars) or outside the binding surface (black bars) and tested for binding of the affinitymatured antibodies. Finally, mutations were introduced in the designed antibodies also through random mutagenesis and in vitro selection of improved binders (blue spheres). Mutations at the binding surface reduced affinity, except for Val71Glu on ACP, which enhanced binding of the affinity-matured 2acp12_ev. Mutations away from the interface, including those isolated from in vitro selection, increased binding affinity. Binding signals were tested in yeast surface display with the antibodies expressed as scFv and the ligand at 50 nM concentration for 2acp12_ev and at 1 μM concentration for 2acp12, 5acp14_ev, and 5ins16.
Baran, D., Pszolla, M. G., Lapidoth, G. D., Norn, C., Dym, O., Unger, T., ... & Fleishman, S. J. (2017). Principles for computational design of binding antibodies. Proceedings of the National Academy of Sciences, 114(41), 10900-10905.
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 |
---|---|---|---|
PABS-0025 | Anti-Mycobacterium tuberculosis acyl-carrier protein (ACP) 2 Recombinant Antibody (Clone 5ins14) | ELISA, FuncS | IgG |
CAT | Product Name | Application | Type |
---|---|---|---|
PFBS-0012 | Anti-Mycobacterium tuberculosis acyl-carrier protein (ACP) 2 Recombinant Antibody (Clone 2acp12); Fab Fragment | ELISA, FuncS | Fab |
PFBS-0025 | Anti-Mycobacterium tuberculosis acyl-carrier protein (ACP) 2 Recombinant Antibody (Clone 5ins14); Fab Fragment | ELISA, FuncS | Fab |
CAT | Product Name | Application | Type |
---|---|---|---|
PSBS-0012 | Anti-Mycobacterium tuberculosis acyl-carrier protein (ACP) 2 Recombinant Antibody (Clone 2acp12); scFv Fragment | ELISA, FuncS | scFv |
PSBS-0025 | Anti-Mycobacterium tuberculosis acyl-carrier protein (ACP) 2 Recombinant Antibody (Clone 5ins14); scFv Fragment | ELISA, FuncS | scFv |
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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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