Product Details
| Clone: | MON-148 |
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| Host: | Mouse |
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| Isotype: | IgG2a |
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| Immunogen: | Recombinant human furin. |
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| UniProt ID: | P09958 |
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| Source: | Ascites fluid from Balb/c mice obtained after ingection of MON-148 producing hybridoma cells and isolated using a physiological salt solution (0.9% NaCl). |
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| Species reactivity: | Human, Mouse
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| Specificity: | Recognizes epitope region 2 (R2) in the catalytic domain of furin convertase. |
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| Applications: | ICC, IP, WB
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| Recommended Dilutions/Conditions: | Immunocytochemistry (1:200-1:400)
Immunoprecipitation (1:200; 50mM TRIS/HCl, pH 7.4, 150mM NaCl, 1% Triton X-100; 1% sodium deoxycholate, 0.1% SDS)
Western Blot (1:1,000)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application. |
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| Formulation: | Liquid. Ascites fluid. Contains no preservatives. |
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| Use/Stability: | Stable for at least 3 months when stored at +4°C. |
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| Handling: | Avoid freeze/thaw cycles. |
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| Shipping: | Blue Ice |
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| Short Term Storage: | +4°C |
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| Long Term Storage: | -20°C |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Polyphenols with indirect proprotein convertase inhibitory activity: J. Zhu, et al.; Int. J. Oncol.
43, 947 (2013),
Application(s): IP,
Abstract;
Generation and characterization of non-competitive furin-inhibiting nanobodies: J. Zhu, et al.; Biochem. J.
448, 73 (2012),
Application(s): IP,
Abstract;
Full Text
A femtomol range FRET biosensor reports exceedingly low levels of cell surface furin: implications for the processing of anthrax protective antigen: K. Gawlik, et al.; PLoS One
5, e11305 (2010),
Application(s): WB and ICC,
Abstract;
Full Text
Membrane type-1 matrix metalloprotease-independent activation of pro-matrix metalloprotease-2 by proprotein convertases: B.H. Koo, et al.; FEBS J.
276, 6271 (2009),
Abstract;
Full Text
Consequences of C-terminal domains and N-terminal signal peptide deletions on LEKTI secretion, stability, and subcellular distribution: A. Jayakumar, et al.; Arch. Biochem. Biophys.
435, 89 (2005),
Application(s): WB and ICC,
Abstract;
'Shed' furin: mapping of the cleavage determinants and identification of its C-terminus: B. Plaimauer, et al.; Biochem. J.
354, 689 (2001),
Abstract;
Polyarginines are potent furin inhibitors: A. Cameron, et al.; J. Biol. Chem.
275, 36741 (2000),
Abstract;
Full Text
Modulation of furin-mediated proprotein processing activity by site-directed mutagenesis: J.W. Creemers, et al.; J. Biol. Chem.
268, 21826 (1993),
Abstract;
Full Text
Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases: W.J. Van de Ven, et al.; Crit. Rev. Oncog.
4, 115 (1993),
Abstract;
Development and characterization of a panel of monoclonal antibodies against the novel subtilisin-like proprotein processing enzyme furin: H.L. van Duijnhoven, et al.; Hybridoma
11, 71 (1992),
Abstract;
