Anti-Human AQP4 Recombinant Antibody (D15107)
CAT#: TAB-0977CLV
The anti-aquaporin-4 antibody D15107 is an chimeric antibody targeting human aquaporin-4, and can be used for treating the neuromyelitis optica.
Published Data
Gene Expression
ELISA
Figure 1 Binding of the mAbs to hAQP4 M23 expressed on the envelope of budded baculovirus.
Time course of binding of 300 ng · mL−1 of C9401, D12092 and D15107 at room temperature. Bound antibodies were measured by ELISA and estimated as percent of maximal binding of D15107 at each temperature.
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
ELISA
Figure 2 Binding of the mAbs to hAQP4 M23 expressed on the envelope of budded baculovirus.
Time course of binding of 300 ng · mL−1 of C9401, D12092 and D15107(blue) at 4°C. Bound antibodies were measured by ELISA and estimated as percent of maximal binding of D15107 at each temperature.
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
ELISA
Figure 3 Binding of the mAbs to hAQP4 M23 expressed on the envelope of budded baculovirus.
Concentration–response binding of C9401, D12092 and D15107(blue) at 4°C overnight. Bound antibodies were measured by ELISA and estimated as percent of maximal binding of D15107.
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
Figure 4 Binding of the mAbs to AQP4 expressed in stable CHO cell lines.
Concentration-dependent binding of D15107 to fixed CHO cells expressing M23 alone (green) or M1 alone (blue) at 4°C overnight, or live hAQP4(red) M1 37°C for 1 h.
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
IF
Figure 5 Live imaging of binding of fluorescent-labelled mAbs to hAQP4‐M1 cells.
Cells were treated with 10µg/ml Alexa-Fluor-555-labelled C9401, D12092 or D15107, and fluorescence of eGFP expressed in hAQP4-M1 cells and mAbs was observed 24 h after incubation.
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
WB
Figure 6 Effect of mAbs on levels of AQP4 in hAQP4-M1 cells.
A typical blot is shown.
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
FuncS
Figure 7 Effect of mAbs on levels of AQP4 in hAQP4-M1 cells.
hAQP4-M1 cells were treated with 5 µg/mL of C9401 (lanes 3 and 4), D15107 (lanes 5 and 6) or mAQP4‐specific E5415B (lane 2) in the absence (lanes 2, 3 and 5) or presence (lanes 4 and 6) of 100 nM bafilomycin A1 at 37°C for 24 h. Amounts of eGFP and AQP4 were determined by Western blotting and estimated as fold relative to non‐treated cells (lane 1).
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
ELISA
Figure 8 Binding of chimeric mAbs to hAQP4 M23 expressed on the envelope of budded baculovirus.
Concentration-dependent binding of original and chimeric D15107 to hAQP4 M23 expressed on the envelope of BV were determined by ELISA at 4°C overnight and shown as percent of maximal binding of each antibody.
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
FuncS
Figure 9 Cytoprotective effect of chimeric D15107 against CDC induced by NMO-IgG.
hAQP4-M1/M23 cells were treated with either rabbit complement (RC), 2 or 10 µg/mL of chimeric D15107 (C-D15107), or 200–500 µg/mL of the purified IgG fractions from different patients and their combinations as indicated at 37°C for 2 h. Cell mortalities were determined by LDH assay and estimated as fold relative to non-treated cells (control).
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
FuncS
Figure 10 Injection (i.p. or intra-cerebral) of chimeric D15107 into mice.
Serum levels of chimeric D15107 in mice after i.p. injection (n = 3 for each time point) determined by ELISA. Concentrations of the antibody detected with secondary anti‐human IgG antibody were below the detectable level in mice injected with PBS (n = 4).
Miyazaki‐Komine, K., Takai, Y., Huang, P., Kusano‐Arai, O., Iwanari, H., Misu, T., ... & Fujihara, K. (2016). High avidity chimeric monoclonal antibodies against the extracellular domains of human aquaporin‐4 competing with the neuromyelitis optica autoantibody, NMO‐IgG. British journal of pharmacology, 173(1), 103-114.
FC
Figure 11 Binding properties of four established monoclonal antibodies using flow cytometry.
Established anti-AQP4 extracellular domain antibodies, including C9401 (a–d), D12092 (e–h), D15107 (i–l), and D15129 (m–p), were added to CHO cells transiently transfected with either hAQP4 M1 (a, e, i, and m), hAQP4 M23 (b, f, j and n), mAQP4 M1 (c, g, k, and o), or mAQP4 M23 (d, h, l, and p) cDNA connected to EGFP cDNA with IRES, and bound antibodies were estimated with flow cytometry.
Miyazaki, K., Abe, Y., Iwanari, H., Suzuki, Y., Kikuchi, T., Ito, T., ... & Ikeshima-Kataoka, H. (2013). Establishment of monoclonal antibodies against the extracellular domain that block binding of NMO-IgG to AQP4. Journal of neuroimmunology, 260(1-2), 107-116.
FC
Figure 12 Effect of amino acid substitutions in the extracellular loops of hAQP4 on binding of monoclonal antibodies.
C9401 (a–d), D12092 (e–h), D15107 (i–l), and D15129 (m–p) were added to CHO cells transiently transfected with either wild-type hAQP4 M23 (a, e, i, and m), T62S/K64N-hAQP4 M23 (b, f, j and n), M149T-hAQP4 M23 (c, g, k, and o), or E228A-hAQP4 M23 (d, h, l, and p) cDNA connected to EGFP cDNA with IRES, and bound antibodies were estimated with flow cytometry.
Miyazaki, K., Abe, Y., Iwanari, H., Suzuki, Y., Kikuchi, T., Ito, T., ... & Ikeshima-Kataoka, H. (2013). Establishment of monoclonal antibodies against the extracellular domain that block binding of NMO-IgG to AQP4. Journal of neuroimmunology, 260(1-2), 107-116.
FuncS
Figure 13 The monoclonal antibodies have no effect on water permeability of AQP4.
The functional assay of hAQP4 incorporated into liposomes. Water permeability was estimated by the functional assay using liposomes incorporating His-tagged hAQP4 M23 in the presence or absence of the monoclonal antibodies D12092 and D15107.
Miyazaki, K., Abe, Y., Iwanari, H., Suzuki, Y., Kikuchi, T., Ito, T., ... & Ikeshima-Kataoka, H. (2013). Establishment of monoclonal antibodies against the extracellular domain that block binding of NMO-IgG to AQP4. Journal of neuroimmunology, 260(1-2), 107-116.
WB
Figure 14 The monoclonal antibodies have no effect on water permeability of AQP4.
Western blotting of monoclonal antibodies bound to liposomes. Lysate from liposomes with (lanes 2, 4, and 6) or without (lanes 1, 3, and 5) hAQP4 treated with vehicle (lanes 1, 2), D12092 (lanes 3, 4), or D15107 (lanes 5, 6) was subjected to Western blotting using an HRP-labeled anti-mouse IgG or anti-AQP4 C-terminal antibody followed by HRP-labeled anti-rabbit IgG. His-tagged hAQP4-M23 is indicated with an arrow.
Miyazaki, K., Abe, Y., Iwanari, H., Suzuki, Y., Kikuchi, T., Ito, T., ... & Ikeshima-Kataoka, H. (2013). Establishment of monoclonal antibodies against the extracellular domain that block binding of NMO-IgG to AQP4. Journal of neuroimmunology, 260(1-2), 107-116.
FC
Figure 15 Effect of treatment with monoclonal antibodies on the binding of NMO-IgG to cells expressing hAQP4.
NMO-IgGs (Pt1-5) were added to CHO cells stably transfected with hAQP4 M23-IRES-EGFP cDNA in the presence (black line histogram) or absence (gray zone histogram) of pretreatment with the monoclonal antibody D12092 and D15107, and bound NMO-IgGs were estimated with flow cytometry. The horizontal axis shows the antibodies binding and the vertical axis shows the cell counts.
Miyazaki, K., Abe, Y., Iwanari, H., Suzuki, Y., Kikuchi, T., Ito, T., ... & Ikeshima-Kataoka, H. (2013). Establishment of monoclonal antibodies against the extracellular domain that block binding of NMO-IgG to AQP4. Journal of neuroimmunology, 260(1-2), 107-116.
IF
Figure 16 Monoclonal antibodies replace the binding of NMO-IgG on the cell expressing AQP4.
CHO cells stably transfected with AQP4 M23-IRES-EGFP were incubated with NMO-IgG from patient 2 for 2 h (a), then they were treated with D12092 (c and f) or D15107 (d and g) in the presence of NMO-IgG and further incubated for 24 h. Cells incubated with NMO-IgG for 26 h were also examined (b and e). Bound NMO-IgG and the monoclonal antibodies were detected by Alexa Fluor 568-cinjugated anti-human IgG (a–d) and Alexa Fluor 555-conjugated anti-mouse IgG (e–g), respectively.
Miyazaki, K., Abe, Y., Iwanari, H., Suzuki, Y., Kikuchi, T., Ito, T., ... & Ikeshima-Kataoka, H. (2013). Establishment of monoclonal antibodies against the extracellular domain that block binding of NMO-IgG to AQP4. Journal of neuroimmunology, 260(1-2), 107-116.
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Subcellular Location
Figure 1 IF staining of human cell line U-251 MG
Immunofluorescent staining of human cell line U-251 MG shows localization to plasma membrane.
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/14784/if_selected.jpg
Subcellular Location
Figure 2 IF staining of human cell line A-431
Immunofluorescent staining of human cell line A-431 shows localization to cell junctions.
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/5079/if_selected.jpg
Normal Tissue
Figure 3 Cerebral cortex
Glial cells
Staining: Medium
Intensity: Strong
Quantity: <25%
Location: Cytoplasmic/membranous
Neuropil
Staining: High
Intensity: Strong
Quantity: 75%-25%
Location: Cytoplasmic/membranous
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/14784/141530_B_7_5.jpg
Normal Tissue
Figure 4 Lung
Alveolar cells type I
Staining: High
Intensity: Strong
Quantity: 75%-25%
Alveolar cells type II
Staining: High
Intensity: Strong
Quantity:>75%
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/14784/141530_A_3_4.jpg
Normal Tissue
Figure 5 Kidney
Distal tubules
Staining: Medium
Intensity: Strong
Quantity: <25%
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/14784/141530_A_8_5.jpg
RNA Expression
Figure 6 RNA cell line category: Cell line enhanced (AF22, RPTEC TERT1)
Cell lines ordered by descending RNA expression order.
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/ENSG00000171885-AQP4
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Specifications
- Host Species
- Human
- Type
- Chimeric antibody
- Specificity
- Human
- Clone
- D15107
- Applications
- ELISA, FuncS, WB, IF, FC
- Related Disease
- Neuromyelitis optica
Applications
- Application Notes
- The antibody was validated for ELISA, Functional Assay, Western Blot, Immunofluorescence, Flow Cytometry. For details, refer to Published Data.
Target
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Customer Review
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Reliable AQP4
I have used the anti-AQP4 antibody in ELISA and Western blot, and its performance has been very dependable. The chimeric design offers specific recognition of human aquaporin-4, and the clear documentation on protocols has helped in achieving reproducible results in my water channel studies.
Consistent and Clear
The anti-AQP4 antibody provided consistent results in immunofluorescence and functional assays. I found the detailed application notes extremely helpful and the antibody's performance in detecting aquaporin-4 was reliable. Its chimeric design has notably enhanced the clarity of my experimental data.
Q&As
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What are the key assay formats confirmed for the AQP4 antibody?
A: Our anti-AQP4 antibody is validated for ELISA, functional assays, Western blot, immunofluorescence, and flow cytometry. These multiple validations ensure it reliably recognizes human aquaporin-4, making it a versatile tool for investigating water channel expression in various research settings.
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How does the chimeric design benefit performance in research assays?
A: The chimeric design of the anti-AQP4 antibody ensures effective and specific binding to its target. Its validated performance across ELISA, WB, IF, and FC experiments supports consistent data generation, enabling researchers to study aquaporin-4 expression with confidence and reliability.
View the frequently asked questions answered by Creative Biolabs Support.
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To accurately reference this product in your publication, please use the following citation information:
(Creative Biolabs Cat# TAB-0977CLV, RRID: AB_3714288)
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Downloadable Resources
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Product Notes
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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Protocol & Troubleshooting
We have outlined the assay protocols, covering reagents, solutions, procedures, and troubleshooting tips for common issues in order to better assist clients in conducting experiments with our products. View the full list of Protocol & Troubleshooting.
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