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MABF2668-25UG
Sigma-AldrichAnti-fHbp Antibody, clone JAR 11
Anti-fHbp, clone JAR 11, Cat. No. MABF2668, is a mouse monoclonal antibody that detects Factor H binding protein (fHbp) in Neisseria meningitidis and is tested for use in Dot Blot, ELISA, and Western Blotting.
More>>Anti-fHbp, clone JAR 11, Cat. No. MABF2668, is a mouse monoclonal antibody that detects Factor H binding protein (fHbp) in Neisseria meningitidis and is tested for use in Dot Blot, ELISA, and Western Blotting. Less<<
NovAseptic® Drive Unit,GMP5000DU 1.1kW 7:1 E0 II 1/2 G Ex h
Übersicht
Replacement Information
Description
Catalogue Number
MABF2668-25UG
Description
Anti-fHbp Antibody, clone JAR 11
Alternate Names
Factor H-binding protein
Lipoprotein
Lipoprotein GNA1870
Background Information
Factor H-binding protein (UniProt: Q6QCC2; also known as Lipoprotein, Lipoprotein GNA1870. fHbp) is encoded by the gna1870 (also known as fhbp) gene in Neisseria meningitidis. Neisseria meningitidis, an encapsulated Gram-negative bacterium, is an important cause of bacterial sepsis and meningitis. fHbp, a surface exposed lipoprotein, is present in all strains of Neisseria meningitidis but is usually sparsely expressed. It is reported to be the only receptor for Factor H (fH), a down-regulatory protein of the alternate complement pathway. Recruitment of fH is the major contributory factor to the ability of this bacteria to avoid innate immune response via inhibition of complement-mediated lysis. High affinity between fH and fHbp is reported to be responsible for sequestering fH in the plasma and deplete and de-regulate complement system, which can cause complement-mediated damage in host cells. fHbp exists in two antigenic sub-families known as A and B that do not exhibit any cross-protective activity. fHbp has been divided into three variant groups based on its amino acid sequence. Variant group 1 belongs to subfamily B and accounts for about 60% of disease-causing group B isolates. Subfamily A includes variant groups 2 and 3. Antibodies generated against variant 1 are reported to be bactericidal only against bacterial strains expressing fHbp in the variant 1 group but not against strains that express variants 2 and 3 and vice versa. Clone JAR 11 that displays partial inhibitory activity against binding of fH to fHbp is shown to be specific for fHbp variant group 2 and does not react with variant groups 1 and 3. (Ref.: Beernink, PT et al., (2008). Infect. Immun.76(9); 4232 4240; Welsch, JA., et al. (2004). J. Immunol. 172(9); 5606-5615; Vu, DM., et al., (2012). Sci. Rep. 2: 341).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG2a in PBS without azide.
Anti-fHbp, clone JAR 11, Cat. No. MABF2668, is a mouse monoclonal antibody that detects Factor H binding protein (fHbp) in Neisseria meningitidis and is tested for use in Dot Blot, ELISA, and Western Blotting.
Key Applications
Dot Blot
ELISA
Western Blotting
Application Notes
Western Blotting Analysis: A representative lot detected fHbp in Western Blotting applications (Beernink, P.T., et. al. (2008). Infect Immun. 76(9):4232-40).
ELISA Analysis: A representative lot detected fHbp in ELISA applications (Vu, D.M., et. al. (2012). Sci Rep. 2:341).
Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user
Biological Information
Immunogen
His-tagged recombinant Factor H-binding protein (fHbp) from variant group 2 strain 2996 expressed in E. coli.
Epitope
C-terminal half
Clone
JAR 11
Concentration
1.0 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.
Host
Mouse
Specificity
Clone JAR 11 is a mouse monoclonal antibody that specifically detects Factor H-binding factor variant 2 in Neisseria meningitidis. It targets an epitope within 43 amino acids from the C-terminal half.
Evaluated by Dot Blotting with rfHbp 1D1 (variant 1), rfHbp 1D77 (variant 2), and rfHbp 1D28 (variant 3).
Dot Blotting Analysis: A 1:500 dilution of this antibody detected fHbp 1D77 (variant 2), but not rHbp 1D1(variant 1) or fHbp 1D28 (variant 3).
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
A broadly cross-reactive monoclonal antibody against an epitope on the n-terminus of meningococcal fHbp David M Vu 1 , Rolando Pajon, Donald C Reason, Dan M Granoff Sci Rep
2
341
2011
Meningococcal factor H binding protein (fHbp) is an important vaccine antigen for prevention of disease caused by capsular group B strains. The protein has been sub-classified into three variant groups. Most anti-fHbp antibodies are variant group-specific and recognize epitopes on the C-terminal domain. We report a murine IgG1 mAb, JAR 41, which broadly cross-reacted with fHbp sequence variants from all variant groups. The mAb bound to the surface of live meningococci with fHbp from each of the three variant groups. In combination with second non-bactericidal anti-fHbp mAbs, JAR 41 elicited complement-mediated bactericidal activity in vitro, and augmented passive protection against meningococcal bacteremia in human fH transgenic rats. The epitope was located on a conserved region of the N-terminal portion of the fHbp molecule opposite that of fH contact residues. The data underscore the importance of broadly cross-reactive, surface-exposed epitopes on the N-terminal domain in the design of protective fHbp vaccines.
Fine antigenic specificity and cooperative bactericidal activity of monoclonal antibodies directed at the meningococcal vaccine candidate factor h-binding protein. Beernink PT, Welsch JA, Bar-Lev M, Koeberling O, Comanducci M, Granoff DM. Infect Immun
76(9)
4232-40
2008
No broadly protective vaccine is available for the prevention of group B meningococcal disease. One promising candidate is factor H-binding protein (fHbp), which is present in all strains but often sparsely expressed. We prepared seven murine immunoglobulin G monoclonal antibodies (MAbs) against fHbp from antigenic variant group 2 (v.2) or v.3 ( approximately 40% of group B strains). Although none of the MAbs individually elicited bactericidal activity with human complement, all had activity in different combinations. We used MAb reactivity with strains expressing fHbp polymorphisms and site-specific mutagenesis to identify residues that are important for epitopes recognized by six of the v.2 or v.3 MAbs and by two v.1 MAbs that were previously characterized. Residues affecting v.2 or v.3 epitopes resided between amino acids 174 and 216, which formed an eight-stranded beta-barrel in the C domain, while residues affecting the v.1 epitopes included amino acids 121 and 122 of the B domain. Pairs of MAbs were bactericidal when their respective epitopes involved residues separated by 16 to 20 A and when at least one of the MAbs inhibited the binding of fH, a downregulatory complement protein. In contrast, there was no cooperative bactericidal activity when the distance between residues was >or=27 A or <or=14 A, which correlated with the inhibition of the binding of one MAb by the other MAb. Thus, a model for anti-fH MAb bactericidal activity against strains expressing low levels of fHbp requires the binding of two MAbs directed at nonoverlapping epitopes, which activates the classical complement pathway as well as inhibits fH binding. The latter increases the susceptibility of the organism to complement-mediated bacteriolysis.
