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Anti-Bacillus anthracis lef/LF/Lethal factor Recombinant Antibody (F5-1) (JN859023)

Anti-Bacillus anthracis lef/LF/Lethal factor Recombinant Antibody (F5-1)
Anti-Bacillus anthracis lef/LF/Lethal factor Recombinant Antibody (F5-1)
Precio(USD):
Especificación:
  • 50ug
  • 100ug
  • 1mg
Número:
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  • Datasheet

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Vista general
Número de catálogoJN859023
Reactividad de especiesBacillus anthracis
AplicacionesELISA, IP, SPR
Especie huéspedMouse
ClonalidadMonoclonal
IsotipoIgG2a
ID de clonF5-1
Objetivo lef, LF, Lethal factor, Anthrax lethal toxin endopeptidase component, Bacillus anthracis
Nivel de endotoxinas Please contact with the lab for this information.
Pureza >95% as determined by SDS-PAGE.
Purificación Protein A/G purified from cell culture supernatant.
Número de acceso P15917
RRID

Anti-Bacillus anthracis lef/LF/Lethal factor Antibody (F5-1) (abinScience Cat# JN859023, RRID:AB_3729005)
_x005F_x005F_x000D_

Forma Liquid
Buffer de almacenamiento 0.01M PBS pH 7.4

Consulte la información específica del buffer en la copia impresa del datasheet o en el COA específico del lote.

Información de uso del producto
Aplicación Dilución
ELISA 1:2000-1:20000
Estabilidad y almacenamiento 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.
Fondo

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
Nota For research use only.
Imágenes
  • Anti-Bacillus anthracis lef/LF/Lethal factor Recombinant Antibody (F5-1)

    SDS-PAGE

    SDS-PAGE for Anti-Bacillus anthracis lef/LF/Lethal factor Antibody (F5-1)

Referencias
Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
Enter any 2 of Mass, Concentration, Volume + Molecular Weight to solve for the unknown.
Mass
=
Concentration
×
Volume
Molecular Weight *
g/mol
Formula
C₁ × V₁ = C₂ × V₂
Enter any 3 of the 4 values to solve for the unknown.
Stock Solution
C₁ (Stock Conc.)
×
V₁ (Stock Vol.)
=
Working Solution
C₂ (Working Conc.)
×
V₂ (Working Vol.)
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