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Anti-Bacillus anthracis lef/LF/Lethal factor Recombinant Antibody (2LF) (JN859013)

Anti-Bacillus anthracis lef/LF/Lethal factor Recombinant Antibody (2LF)
Anti-Bacillus anthracis lef/LF/Lethal factor Recombinant Antibody (2LF)
Precio(USD):
Especificación:
  • 50ug
  • 100ug
  • 1mg
Número:
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Vista general
Número de catálogoJN859013
Reactividad de especiesBacillus anthracis
AplicacionesELISA, SPR
Especie huéspedMouse
ClonalidadMonoclonal
IsotipoIgG2a
ID de clon2LF
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 (2LF) (abinScience Cat# JN859013, RRID:AB_3729004)
_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 (2LF)

    SDS-PAGE

    SDS-PAGE for Anti-Bacillus anthracis lef/LF/Lethal factor Antibody (2LF)

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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