Custom antibodies against human neutrophil and inflammation targets
A set of epitope-mapped mouse monoclonal antibodies targeting human neutrophil receptors and inflammation-related proteins, including N-formyl peptide receptors, NADPH oxidase subunits (gp91phox, p22phox), and CAP-18. Available for non-exclusive licensing.
Description
Mouse monoclonal antibodies available for non-exclusive licensing from Montana State University are listed below:
Anti-N-formyl peptide receptor antibodies against human neutrophil N-formyl peptide receptor, NFPRa and NFPRb: NFPRa and NFPRb can be employed in the study of inflammation sites where the accumulation, activation and control of neutrophils is partly driven by the binding of N-formyl peptides to N-formyl peptide chemoattractant receptors (FPRs).
NFPRa
Anti-FPR1 (human neutrophil N-formyl peptide receptor 1) and anti-FPR2 (human neutrophil N-formyl peptide receptor 2); IgG1; used as hybridoma culture supernatant and purified protein; epitope mapped, recognizing cytoplasmic cterminal tail region containing residues of FPR1 (305-GQDFRERLI-313) and of FPR2 (306- GQDFRERLI-314); Walid S. Maaty, et al J. Biol. Chem. 2013, 288:27042-27058.
NFPRb
Anti-FPR1 (human neutrophil N-formyl peptide receptor 1); IgG1; used as hybridoma culture supernatant and purified protein; epitope mapped, recognizing a region of FPR1 containing the cytoplasmic c-terminal tail residues 338- STLPSAEVELQAK-350; sensitive to C-terminal tail phosphorylation; Walid S. Maaty, et al J. Biol. Chem. 2013, 288:27042-27058.
Anti-gp91phox (human neutrophil flavocytochrome b large subunit; aka beta subunit, Nox2, cytochrome b559 or cytochrome b558)
mAb 54.1
IgG1, used as hybridoma culture supernatant and purified protein; epitope mapped, cytoplasmic domain (ref.: Burritt et al J Biol Chem. 1995 270:16974-80). cross reacts with Nox1, Nox3, Nox4, GRP58 (ref.: Baniulis et al. BBA 2005 1752:186-96).
mAb NL7
IgG1, used as hybridoma culture supernatant and purified protein; epitope mapped, cytoplasmic domain. (ref.: Burritt et al J Immunol. 2003 170:6082-9).
mAb CL5
IgG1, used as hybridoma culture supernatant and purified protein; epitope mapped, extracellular domain. (ref.: Baniulis et al Eur J Haematol. 2005 74:337-47).
Anti-p22phox (human neutrophil flavocytochrome b small subunit; aka alpha subunit, cytochrome b559 or cytochrome b558)
mAb 44.1
IgG2, used as hybridoma supernatant only; does not survive low pH treatment w/o special care; epitope mapped, cytoplasmic domain (ref.: Burritt et al J Biol Chem. 1995 270:16974-80).
mAb CS9
IgG1, used as hybridoma culture supernatant and purified protein; epitope mapped, cytoplasmic domain (ref.: Taylor et al J Immunol. 2004 173:7349-57).
Anti-human neutrophil CAP-18
H7
IgG1, used as hybridoma supernatant and purified protein; epitope mapped, holoprotein (ref.: Stie et al J Leukoc Biol. 2007 82:161-72).
About Montana State University
Montana State University's substantial research enterprise growth has been accompanied by focused investments in innovation and research translation, creating new opportunities for companies to engage with MSU research and expertise. A particular strength is MSU’s network of specialized centers, institutes, and industry-accessible core facilities, which bring together multidisciplinary expertise, advanced research infrastructure, testing capabilities, and established pathways for working with industry partners. MSU is one of a select group of universities participating in the NSF's Accelerating Research Translation (ART) program, which is building the capacity and infrastructure needed to translate more research discoveries into solutions with real-world impact. The growing MSU Innovation Campus and expanding incubator infrastructure provide additional opportunities for university-industry interaction, startup development, and technology-focused companies. These efforts are complemented by MSU’s Technology Transfer Office, which works with researchers and companies to protect and license MSU inventions and facilitate industry-sponsored research collaborations.
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