Anthrax Protective Antigen Antibody (YA1060)(PBS only)
(Synonyms: Protective antigen)Anthrax Protective Antigen Antibody (YA1060) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to Anthrax Protective Antigen.
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Host:
Mouse
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Isotype:
IgG
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Application:
ELISA
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Reactivity :
Bacillusanthracis
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|
| Dilution Ratio | 1:10000 |
Product Details
Anthrax Protective Antigen Antibody (YA1060) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to Anthrax Protective Antigen.
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Host Mouse
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Species ReactivityBacillusanthracis
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Calculated Molecular Weight -
A synthesized peptide derived from Anthrax Protective gen
Affinity Purified
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Anthrax Protective Antigen is a Protective antigen constitutes one of the three proteins composing the anthrax toxin; it mediates attachment to host cells and translocation of edema factor (EF) and lethal factor (LF) into the host cytoplasm. PA associated with LF forms the lethal toxin (LeTx) and causes death when injected; PA associated with EF forms the edema toxin (EdTx) and produces edema. PA induces immunity to infection with anthrax; Mediates the attachment to host cells by binding host cell receptors ANTXR1 and ANTXR2. Following host cell surface attachment, PA is cleaved by FURIN to generate the PA-63 (Protective antigen PA-63) form, which constitutes the mature form of the protein that oligomerizes and forms a pore to translocate the enzymatic toxin components edema factor (EF) and lethal factor (LF) into the host cytosol; Mature form that oligomerizes and forms a pore to translocate the enzymatic toxin components edema factor (EF) and lethal factor (LF) into the host cytosol. Following attachment to host cell receptors and cleavage by FURIN, homooligomerizes to form ring-shaped oligomers that are in a pre-pore conformation, and associates with EF and LF. Toxin-leaded complexes are then endocytosed in a clathrin-dependent process, followed by a conformational change of oligomerized PA-63 from the pre-pore to pore state, which is triggered by the low pH in the endosome. Once active, the pore mediates unfolding of EF and LF, which pass through the pore and translocate into the host cytosol[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16].
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Subcellular Localization
Secreted; Host cell membrane; Host cell membrane; Multi-pass membrane protein; Host endosome membrane; Multi-pass membrane protein
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Subunit
Interacts with host ANTXR1 and ANTXR2
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SwissProt ID
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Synonyms
Protective antigen
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Research Field
Microbiology
Documentation
References
[1]. Bradley KA, et al. Identification of the cellular receptor for anthrax toxin. Nature. 2001 Nov 8;414(6860):225-9. [Content Brief]
[2]. Bradley KA, et al. Binding of anthrax toxin to its receptor is similar to alpha integrin-ligand interactions. J Biol Chem. 2003 Dec 5;278(49):49342-7. [Content Brief]
[3]. Santelli E, et al. Crystal structure of a complex between anthrax toxin and its host cell receptor. Nature. 2004 Aug 19;430(7002):905-8. [Content Brief]
[4]. Lacy DB, et al. Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13147-51. [Content Brief]
[5]. Singh Y, et al. The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity. J Biol Chem. 1991 Aug 15;266(23):15493-7. [Content Brief]
[6]. Mock M, et al. Anthrax. Annu Rev Microbiol. 2001;55:647-71. [Content Brief]
[7]. Singh Y, et al. Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytic uptake into mammalian cells. Infect Immun. 1999 Apr;67(4):1853-9. [Content Brief]
[8]. Chauhan V, et al. Identification of amino acid residues of anthrax protective antigen involved in binding with lethal factor. Infect Immun. 2002 Aug;70(8):4477-84. [Content Brief]
[9]. Pimental RA, et al. Anthrax toxin complexes: heptameric protective antigen can bind lethal factor and edema factor simultaneously. Biochem Biophys Res Commun. 2004 Sep 10;322(1):258-62. [Content Brief]
[10]. Abrami L, et al. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J Cell Biol. 2003 Feb 3;160(3):321-8. [Content Brief]
[11]. Abrami L, et al. Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. PLoS Pathog. 2010 Mar 5;6(3):e1000792. [Content Brief]
[12]. Krantz BA, et al. A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science. 2005 Jul 29;309(5735):777-81. [Content Brief]
[13]. Feld GK, et al. Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers. Nat Struct Mol Biol. 2010 Nov;17(11):1383-90. [Content Brief]
[14]. Hardenbrook NJ, et al. Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors. Nat Commun. 2020 Feb 11;11(1):840. [Content Brief]
[15]. Zhou K, et al. Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors. Structure. 2020 Aug 4;28(8):879-887.e3. [Content Brief]
[16]. Antoni C, et al. Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state. PLoS Pathog. 2020 Aug;16(8):e1008530. [Content Brief]
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