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Product Name Anthrax lethal factor Chinese Name 炭疽杆菌致死因子LF抗体 Alias Anthrax lethal toxin endopeptidase component; Anthrax LF; bacillus anthracis lethal factor; Lef; LF; LEF_BACAN. Research Area immunology Bacteria and viruses Immunogen Species Rabbit Clonality Polyclonal Applications WB=1:500-2000 ELISA=1:5000-10000 IHC-P=1:100-500 IHC-F=1:100-500 ICC=1:100-500 IF=1:100-500 (Paraffin sections need antigen repair)
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.Theoretical molecular weight 90kDa Cellular localization Secretory protein Form Liquid Concentration 1mg/ml immunogen KLH conjugated synthetic peptide derived from Bacillus anthracis lethal factor: 501-600/809 Lsotype IgG Purification affinity purified by Protein A Buffer Solution 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Storage Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. Attention This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. PubMed PubMed Product Detail The protease enzyme Lethal Factor (LF) is one of the three proteins (LF, EF & PA) composing the anthrax toxin produced by Bacillus anthracis, a bacteria which can infect many mammalian species and that may be fatal. LF is not toxic by itself, but when associated with Protective Antigen (PA), can then gain entry to cells. Once inside the cell, LF then 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 LF intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates.
Function:
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.
Subunit:
Anthrax toxins are composed of three distinct proteins, a protective antigen (PA), a lethal factor (LF) and an edema factor (EF). None of these is toxic by itself. PA+LF forms the lethal toxin (LeTx); PA+EF forms the edema toxin (EdTx).
Subcellular Location:
secreted
Similarity:
Belongs to the peptidase M34 family.
SWISS:
P15917
Gene ID:
45025515
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