

| Catalog No. | JN859033 | ||||
|---|---|---|---|---|---|
| Description |
Anti-Bacillus anthracis lef/LF/Lethal factor Antibody (F3-6) [F3-6] (JN859033) is a mouse monoclonal antibody detecting Bacillus anthracis in ELISA, IP, SPR. Suitable for Bacillus anthracis.
Highlights
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| Species reactivity | Bacillus anthracis | ||||
| Applications | ELISA, IP, SPR | ||||
| Host species | Mouse | ||||
| Isotype | IgG2a | ||||
| Clone ID | F3-6 | ||||
| Clonality | Monoclonal | ||||
| Target | lef, LF, Lethal factor, Anthrax lethal toxin endopeptidase component, Bacillus anthracis | ||||
| Endotoxin level | Please contact with the lab for this information. | ||||
| Purity | >95% as determined by SDS-PAGE. | ||||
| Purification | Protein A/G purified from cell culture supernatant. | ||||
| Accession | P15917 | ||||
| RRID | Anti-Bacillus anthracis lef/LF/Lethal factor Antibody (F3-6) (abinScience Cat# JN859033, RRID:AB_3729006) |
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| Form | Liquid | ||||
| Storage buffer | 0.01M PBS, pH 7.4. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4°C short term (1-2 weeks). Store at -20°C 12 months. Store at -80°C long term. | ||||
| Background | Lethal factor (lef/LF) is a ~93 kDa protein. Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. 1. Duesbery, NS. et al. (1999) Journal of applied microbiology 87, 289-93. PMID: 10475971 2. Vitale, G. et al. (2000) The Biochemical journal 352 Pt 3, 739-45. PMID: 11104681 3. Friedlander, AM. (1986) The Journal of biological chemistry 261, 7123-6. PMID: 3711080 4. Friedlander, AM. et al. (1993) Infection and immunity 61, 245-52. PMID: 8380282 5. Duesbery, NS. et al. (1998) Science (New York, N.Y.) 280, 734-7. PMID: 9563949 6. Vitale, G. et al. (1998) Biochemical and biophysical research communications 248, 706-11. PMID: 9703991 7. Panchal, RG. et al. (2004) Nature structural & molecular biology 11, 67-72. PMID: 14718925 | ||||
| Note | For research use only. |

SDS-PAGE for Anti-Bacillus anthracis lef/LF/Lethal factor Antibody (F3-6)


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