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Mouse Monoclonal Anti-Anthrax Protective Antigen antibody (STJ99283)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-2000; ELISA 1:10000-20000
Recommended protocols: check protocols
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SCBT cat No:
Anti-Anthrax Protective Antigen antibody
|Catalogue No.|| |
Anti-Anthrax Protective Antigen antibody detects Anthrax Protective Antigen.
|Recommended dilution|| |
WB 1:500-2000; ELISA 1:10000-20000
|Molecular weight|| |
Anti-Anthrax Protective Antigen antibody was tube-contained in liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Anti-Anthrax Protective Antigen antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Database links|| |
|Protein function|| |
One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax.
|Protein sequence and domain|| |
Belongs to the bacterial binary toxin family. ; Contains 1 PA14 domain. The molecule is folded into four functional domains. Each domain is required for a particular step in the toxicity process. Domain 1 contains two calcium ions and the proteolytic activation site. Cleavage of the PA monomer releases the subdomain 1a, which is the N-terminal fragment of 20-kDa (PA20). The subdomain 1b is part of the remaining 63-kDa fragment (PA63) and contains the binding sites for LP and EF. Domain 2 is a beta-barrel core containing a large flexible loop that has been implicated in membrane insertion and pore formation. There is a chymotrypsin cleavage site in this loop that is required for toxicity. Domain 3 has a hydrophobic patch thought to be involved in protein-protein interactions. Domain 4 appears to be a separate domain and shows limited contact with the other three domains: it would swing out of the way during membrane insertion. It is required for binding to the receptor; the small loop is involved in receptor recognition.
|Protein post-translational modifications|| |
Proteolytic activation by furin or a furin-like protease cleaves the protein in two parts, PA-20 and PA-63; the latter is the mature protein. The cleavage occurs at the cell surface and probably in the serum of infected animals as well; both native and cleaved PA are able to bind to the cell receptor. The release of PA20 from the remaining receptor-bound PA63 exposes the binding site for EF and LF, and promotes oligomerization and internalization of the protein.
|Protein cellular localization|| |
Secreted, extracellular space. Note=Secreted through the Sec-dependent secretion pathway. Therefore, PA is translocated across the membrane in an unfolded state and then it is folded into its native configuration on the trans side of the membrane, prior to its release to the environment. PA requires the extracellular chaperone PrsA for efficient folding.
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St John’s Laboratory Ltd.
|Product type|| |
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