Anthrax Toxin Lethal Factor antibody
Quick Overview for Anthrax Toxin Lethal Factor antibody (ABIN1713345)
Target
Reactivity
Host
Clonality
Conjugate
Application
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Cross-Reactivity (Details)
- Anthrax LF (Lethal Factor) produced by Bacillus anthracis
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Purification
- Purified by Protein A.
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Immunogen
- KLH conjugated synthetic peptide derived from Bacillus anthracis lethal factor
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Isotype
- IgG
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anti-Anthrax Toxin Lethal Factor (Lef) (AA 779-792) antibody
Lef Reactivity: Bacillus anthracis WB Host: Mouse Monoclonal unconjugated
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Application Notes
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WB 1:100-1000
IHC-P 1:100-500
IF(IHC-P) 1:50-200 -
Restrictions
- For Research Use only
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Format
- Liquid
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Concentration
- 1 μg/μL
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Buffer
- 0.01M TBS( pH 7.4) with 1 % BSA, 0.02 % Proclin300 and 50 % Glycerol.
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Preservative
- Sodium azide
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Precaution of Use
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE, which should be handled by trained staff only.
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Storage
- 4 °C,-20 °C
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Storage Comment
- Shipped at 4°C. Store at -20°C for one year. Avoid repeated freeze/thaw cycles.
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Expiry Date
- 12 months
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- Anthrax Toxin Lethal Factor (Lef)
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Alternative Name
- Bacillus Anthracis Lethal Factor
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Background
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Synonyms: Lethal factor, LF, Anthrax lethal toxin endopeptidase component, lef, pXO1-107, BXA0172, GBAA_pXO1_0172, LEF_BACAN.
Background: One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is 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. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates. Also cleaves mouse Nlrp1b allele 1, leading to NLRP1 inflammasome activation, IL1B release and eventually host inflammatory response Miscellaneous LF binds to the heptamer formed by cleaved PA on the host cell membrane. This step is followed by internalization of the heterooligomeric complex by receptor-mediated endocytosis. LeTx requires passage through an acidic vesicle for activity, at acidic pH , as the pore is inserted into the membrane, LF is translocated and reaches its cytosolic targets. LF is probably directly involved in its routing, by interacting with the lipid membrane. This interaction could involve a conformational change of LF and/or an oligomerization of the protein. LF may have the capability of partially unfolding in order to cross the membrane. Catalytic activity Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases. Cofactor Zn2+ Binds 1 zinc ion per subunit.
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Gene ID
- 3361711, 39675599
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UniProt
- P15917
Target
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