Recombinant Human Anti-F8 Antibody (BO2C11)
CAT#: PABX-058
Anti-F8 antibody is a Human antibody of IgG4 κ class that binds to an F8. It developed From patient memory B-lymphocyte cell line.
Published Data
Tested Data
Gene Expression
Inhib
Figure 1 Inhibition of fVIII functional activity in coagulation assays.
Equal volumes of BO2C11 and of a pool of normal plasma were incubated for 2 hours at 37°C. BO2C11 concentrations before mixing with plasma were as indicated. The residual fVIII activity was measured in an one-stage coagulation assay and was expressed as the percentage of the activity obtained in the absence of antibody.
Jacquemin, M. G., Desqueper, B. G., Benhida, A., Vander Elst, L., Hoylaerts, M. F., Bakkus, M., ... & Vermylen, J. (1998). Mechanism and kinetics of factor VIII inactivation: study with an IgG4 monoclonal antibody derived from a hemophilia A patient with inhibitor. Blood, 92(2), 496-506.
FuncS
Figure 2 Time-dependent effect of vWF on fVIII inactivation by BO2C11.
rfVIII alone (solid symbols) or rfVIII complexed with purified vWF (open symbols) was mixed with BO2C11 at either one of two concentrations (see below). The mixture was then incubated at 37°C for various periods of time, from 2 to 60 minutes, after which the residual fVIII activity was evaluated in a chromogenic assay. Results are expressed as the percentage of the activity observed in the absence of antibody. All values are given as final concentrations in the assay system. (•) rfVIII at 60 ng/mL (0.22 nmol/L); (○) rfVIII with vWF at 3 μg/mL (12 nmol/L); (▴) rfVIII + BO2C11 at 85 ng/mL (0.57 nmol/L); (▵) rfVIII-vWF + BO2C11 at 85 ng/mL (0.57 nmol/L); (▪) rfVIII + BO2C11 at 85 μg/mL (570 nmol/L); and (□) rfVIII-vWF + BO2C11 at 85 μg/mL (570 nmol/L).
Jacquemin, M. G., Desqueper, B. G., Benhida, A., Vander Elst, L., Hoylaerts, M. F., Bakkus, M., ... & Vermylen, J. (1998). Mechanism and kinetics of factor VIII inactivation: study with an IgG4 monoclonal antibody derived from a hemophilia A patient with inhibitor. Blood, 92(2), 496-506.
PK
Figure 3 Kinetics of fVIII/BO2C11 association.
BO2C11 was bound to the sensor chip surface by covalent coupling. Real-time binding was measured for rfVIII at the concentrations indicated. Between each experiment, surface-bound rfVIII was washed off by incubation with HCl, pH 2.0, for 36 seconds. The SPR response gives the amount of surface-bound component at each stage of the reaction, namely (A and B) baseline resonance signal; (B and C) association phase; and (C and D) dissociation phase.
Jacquemin, M. G., Desqueper, B. G., Benhida, A., Vander Elst, L., Hoylaerts, M. F., Bakkus, M., ... & Vermylen, J. (1998). Mechanism and kinetics of factor VIII inactivation: study with an IgG4 monoclonal antibody derived from a hemophilia A patient with inhibitor. Blood, 92(2), 496-506.
SPR
Figure 4 Time-dependent effect of vWF on fVIII inactivation by BO2C11.
rfVIII alone (solid symbols) or rfVIII complexed with purified vWF (open symbols) was mixed with BO2C11 at either one of two concentrations (see below). The mixture was then incubated at 37°C for various periods of time, from 2 to 60 minutes, after which the residual fVIII activity was evaluated in a chromogenic assay. Results are expressed as the percentage of the activity observed in the absence of antibody. All values are given as final concentrations in the assay system. (•) rfVIII at 60 ng/mL (0.22 nmol/L); (○) rfVIII with vWF at 3 μg/mL (12 nmol/L); (▴) rfVIII + BO2C11 at 85 ng/mL (0.57 nmol/L); (▵) rfVIII-vWF + BO2C11 at 85 ng/mL (0.57 nmol/L); (▪) rfVIII + BO2C11 at 85 μg/mL (570 nmol/L); and (□) rfVIII-vWF + BO2C11 at 85 μg/mL (570 nmol/L).
Jacquemin, M. G., Desqueper, B. G., Benhida, A., Vander Elst, L., Hoylaerts, M. F., Bakkus, M., ... & Vermylen, J. (1998). Mechanism and kinetics of factor VIII inactivation: study with an IgG4 monoclonal antibody derived from a hemophilia A patient with inhibitor. Blood, 92(2), 496-506.
IP
Figure 5 Immunoprecipitation of wild-type and mutated rfVIII light chain.
Recombinant fVIII fragments labeled with [35S]methionine and expressed in reticulocyte lysates were incubated for 2 hours at 4°C with LE2E9 (LE) bound to Protein A Sepharose. After washing, bound material was eluted by SDS-buffer and analyzed by SDS-PAGE, followed by autoradiography. Controls included a human monoclonal antibody, BO2C11 (BO), directed toward the fVIII C2 domain,19 a rabbit polyclonal IgG antibody (aA3), directed toward amino acid residues 1797-1815 of the fVIII A3 domain and normal donor polyclonal IgG antibodies (Wi). The experiments were repeated 3 times with similar results.
Jacquemin, M., Benhida, A., Peerlinck, K., Desqueper, B., Vander Elst, L., Lavend'homme, R., ... & Gilles, J. G. (2000). A human antibody directed to the factor VIII C1 domain inhibits factor VIII cofactor activity and binding to von Willebrand factor. Blood, 95(1), 156-163.
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SDS-PAGE
Figure 1 Anti-Human F8 Antibody in SDS-PAGE
SDS-PAGE analysis of PABX-058 In non-reduced (lane 1) and β-mercaptoethanol-reduced (lane 2) conditions.
HPLC
Figure 2 Anti-Human F8 Antibody in HPLC
HPLC analysis of PABX-058 shows that the purity is more than 95%.
Column: 3 µm, 7.8 x 300 nm
Mobile phase: 150 mM Sodium Phosphate Buffer, pH 7.0
Detection: UV 280 nm
Injection: 10 µl
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Normal Tissue
Figure 1 Colon
Endothelial cells
Staining:Medium
Intensity: Moderate
Quantity:>75%
Location: Cytoplasmic/membranous
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/18777/41664_A_7_3.jpg
Normal Tissue
Figure 2 Kidney
Cells in glomeruli
Staining:Medium
Intensity: Moderate
Quantity: 75%-25%
Location: Cytoplasmic/membranous
Cells in tubules
Staining:High
Intensity: Strong
Quantity:>75%
Location: Cytoplasmic/membranous
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/18777/41664_A_7_5.jpg
Normal Tissue
Figure 3 Testis
Leydig cells
Staining:Medium
Intensity: Moderate
Quantity: 75%-25%
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/18777/41664_A_4_6.jpg
RNA Expression
Figure 4 RNA cell line category:Cell line enhanced (U-2197)
Cell lines ordered by descending RNA expression order.
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/ENSG00000185010-F8
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Specifications
- Immunogen
- The details of the immunogen for this antibody are not available.
- Host Species
- Human
- Derivation
- Human
- Type
- IgG
- Specificity
- Tested positive against native Human F8
- Species Reactivity
- Human
- Clone
- BO2C11
- Applications
- WB, ELISA, FuncS, Inhib, PK, IP, SPR
Product Property
- Purity
- >95% by SDS-PAGE and HPLC analysis
- Storage
- Store the antibody (in aliquots) at -20°C. Avoid repeated freezing and thawing of samples.
Applications
- Application Notes
- The F8 antibody has been reported in applications of Western Blot, Enzyme-linked Immunosorbent Assay, Functional Assay, Inhibition, Pharmacokinetic, Immunoprecipitation, Surface Plasmon Resonance.
Target
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Customer Review
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Jessica Hill22.Feb,23
Great for F8 Detection
The Anti-F8 Antibody (BO2C11) has been excellent for our factor VIII detection assays. Its specificity and sensitivity are top-notch, providing clear and reliable results. This antibody has significantly improved the accuracy of our experiments and saved us a lot of troubleshooting time.
David Adams29.May,22
Reliable in Immunoassays
We incorporated this antibody into our immunoassays, and it has been a great asset. The specificity for factor VIII is precise, allowing for accurate detection and analysis. The reliable performance has made it an invaluable tool in our lab.
Megan Martinez13.Aug,21
Consistent High-Quality Results
This antibody has proven to be consistent and reliable in our assays. The high-quality, reproducible results have significantly improved our experiments, making it a crucial part of our research toolkit. The strong affinity and specificity for factor VIII have been particularly beneficial.
Q&As
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Is the anti-F8 antibody BO2C11 suitable for use in Western blotting?
A: Yes, the anti-F8 antibody BO2C11 (PABX-058) is suitable for use in Western blotting. It provides specific binding to F8, allowing for reliable detection in Western blot assays.
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What are the storage recommendations for the anti-F8 antibody BO2C11?
A: The recommended storage condition for the anti-F8 antibody BO2C11 (PABX-058) is at -20°C or lower. For short-term storage, it can be kept at 2-8°C. To ensure stability, avoid repeated freeze-thaw cycles.
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Can the anti-F8 antibody BO2C11 be used in immunoprecipitation assays?
A: Yes, the anti-F8 antibody BO2C11 (PABX-058) can be used in immunoprecipitation assays. It provides specific binding to F8, enabling the successful precipitation of the target protein from complex mixtures.
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Is the anti-F8 antibody BO2C11 effective in ELISA applications?
A: Yes, the anti-F8 antibody BO2C11 (PABX-058) is effective in ELISA applications. It has been validated for use in such assays and provides reliable detection of F8.
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What is the optimal dilution for using the anti-F8 antibody BO2C11 in immunofluorescence?
A: The optimal dilution for using the anti-F8 antibody BO2C11 (PABX-058) in immunofluorescence is typically 1:100 to 1:500. It is advisable to perform a dilution series to determine the best working concentration for your specific experimental conditions.
View the frequently asked questions answered by Creative Biolabs Support.
Citations
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Ketteler, Carolin, et al. "Impact of different factor VIII inhibitor kinetic profiles on the inhibitor titer quantification using the modified Nijmegen-Bethesda assay." Research and Practice in Thrombosis and Haemostasis 6.8 (2022): e12799. https://doi.org/10.1002/rth2.12799This study evaluates the impact of different kinetic profiles of four FVIII monoclonal antibodies on the inhibitor titer quantification using the modified Nijmegen-Bethesda assay. The research was conducted to understand how variations in antibody kinetics can influence the accuracy of FVIII inhibitor titers, which are crucial for managing hemophilia A. The study found that different FVIII monoclonal antibodies exhibit distinct kinetic profiles, affecting the calculation of inhibitor titers. The results suggest that a more accurate titer calculation method, such as using sigmoidal regression, should be employed to account for these kinetic differences.
Creative Biolabs contributed significantly to this research by providing the human anti-FVIII monoclonal antibody BO2C11 (Cat# PABX-058). This antibody was essential for analyzing its specific kinetic profile and its effect on FVIII inhibitor titer quantification. The data derived from the use of BO2C11 helped to highlight the need for improved titer calculation methods, thus supporting the study's goal of enhancing the accuracy of FVIII inhibitor quantification in clinical settings.
Cite This Product
To accurately reference this product in your publication, please use the following citation information:
(Creative Biolabs Cat# PABX-058, RRID: AB_3111697)
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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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