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Product Details
| Application |
ICC, IP, WB |
|---|---|
| Clone |
MON-148 |
| Formulation |
Liquid. Ascites fluid. Contains no preservatives. |
| Host |
Mouse |
| Immunogen |
Recombinant human furin. |
| Isotype |
IgG2a |
| Recommendation 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. |
| 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). |
| Species Reactivity |
Human, Mouse |
| Specificity |
Recognizes epitope region 2 (R2) in the catalytic domain of furin convertase. |
| UniProt ID |
P09958 |
| Worry-free Guarantee |
This antibody is covered by our Worry-Free Guarantee. |
Handling & Storage
| Use/Stability |
Stable for at least 3 months when stored at +4°C. |
|---|---|
| Handling |
Avoid freeze/thaw cycles. |
| Short Term Storage |
+4°C |
| Long Term Storage |
-20°C |
| Shipping |
Blue Ice |
| Regulatory Status |
RUO – Research Use Only |
|---|
- Polyphenols with indirect proprotein convertase inhibitory activity: J. Zhu, et al.; Int. J. Oncol. 43, 947 (2013), Application(s): IP, Abstract
- Enhanced UV-induced skin carcinogenesis in transgenic mice overexpressing proprotein convertases.: Fu, J., Bassi, D. E., et al.; Neoplasia 15, 169 (2013), Application(s): IHC / Reactant(s): Mouse, 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
- Transgenic overexpression of the proprotein convertase furin enhances skin tumor growth.: Bassi, D. E., Fu, J., et al.; Neoplasia 14, 271 (2012), Reactant(s): Mouse, Abstract
- 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
- Analysis of furin ectodomain shedding in epididymal fluid of mammals: demonstration that shedding of furin occurs in vivo: Thimon, V., Belghazi, M., et al.; Reproduction 132, 899 (2006), Abstract
- 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
- Inhibition of furin by serpin Spn4A from Drosophila melanogaster: Oley, M., Letzel, M. C., et al.; FEBS Lett. 577, 165 (2004), 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
- 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
- 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
- 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
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