ATR1-3
Home Up Anti A HNE-MDA-8OHG ACC1 & ACC2 ASIC1-ASIC2-ASIC3 Acrp30 ,APM1, Adiponectin Adenosine deaminase Adenosine Receptor Adiponectin Receptor, Adipsin AdipoQ/Acrp30 /APM1 Poly ADP ribose Adipsin/Complement Factor D Presursor Adrenomedullin AGRP AKT /PKB & CTMP TACE 5'-AMP-activated protein kinase Amyloids-beta Amylin Androgen Receptor Angiogenin Angiopoietin-1/Human Ang-2 Angiotensin I, II, III ACE1 and ACE2 Anion Exchanger ATR1-3 APE ACF / CUGBP2 AIF & APAF-1 APP AQP0, AQP1-9, AQPAP Arginine vasopressin ASIC4 Asp1/Asp2 & Asp2/Asp1 ATP (ABCG) Aven aviva

 

 

Antibodies to Anthrax Toxins (Protective Antigen, Lethal Factor, Edema Factor) Spore Antigens, and Toxin Receptors (ATR1-3)

 

After inhalation by mammals, Bacillus anthracis spores germinate in alveolar macrophages then migrate to lymph nodes where they multiply. The vegetative bacteria excrete the tripartite exotoxin, which consists of three polypeptides: protective antigen (PA, 83 kDa), lethal factor (LF, 90 kDa) and oedma factor (OF, 89 kDa). The two components (OF and LF) of the toxin enzymatically modify substrates within the cytosol of the mammalian cells: The OF is an adenylate cyclase that impairs the host defenses through a variety of mechanisms inhibiting phagocytosis. The LF is a zinc dependent protease that cleaves several mitogen activated protein kinase kinases (MAPKK) and causes lysis of macrophages. To intoxicate mammalian cells, the third component of the toxin PA, binds to a ubiquitously expressed cellular receptor, Tumor Endothelium Marker-8 (TEM8). Upon binding to TEM8, PA is cleaved into 20 and 63kDa fragments (PA20 and PA63) by furin or furin-like proteases. PA20 dissociates into medium and allows the PA63 fragment to heptamerize and bind LF and OF of the toxin. The resulting complex of PA63 fragment with EF and/or OF binds to PA-receptor TEM8/ATR and internalized into endosomes followed by translocation of LF and OF into cytosol of the cells. PA receptor TEM8 (also known as Anthrax Toxin receptor, ATR1) (human 564aa, mouse 562aa) is a glycoprotein with a extracellular (1-321aa), cytosolic (343-564aa) and TM (322-342) domains. The cytosolic domain is not required for translocation of LF into cytosol. The ATR/TEM8 gene is mapped at chromosome 4. Three splice variants (ATR1, ATR2 and ATR3) of TEM8/ATR have been reported. ATR1 (564aa) is the largest isoform whereas ATR2 (368aa) and ATR3 (333aa) are proteins truncated after the TM domain. The seqs (1-364aa) of ATR2 and ATR1 are identical whereas ATR3 has a unique 15aa seq at its C-terminal. ATR/TEM8 protein is expressed in a variety of cell lines and in heart, lung, lymphocytes and in central nervous system. The Von Willebrand Factor Type A domain (VWA) (44-216aa) present in ATR -1, -2 and -3 by itself is able to interact inactivate anthrax toxin. ATR antibodies might help in developing new approaches for PA-receptor study and treatment of anthrax.

 

 Items Antigen peptide location   Antibody Host  *Expected Ab Crossreactivity Aff. Pure IgG/Mab
Cat #
(100 ug)		  * Control Peptide Cat#
(100 ug)
ATR-1
(Ab # 1)		 h, 14 aa ~CT (cytoplasmic) Rb, poly h, m, r? ATR11-A ATR11-P
ATR1-3
(Ab #2)		 h, 15 aa ~NT (extracellular) Rb, poly h, m, r? ATR12-A ATR12-P
ATR-3
(Ab#3)		 h, 14 aa ~Internal Rb, poly h, m, r? ATR31-A ATR31-P

Spore antigen

Antibody

spore extract antigens (~90 kda)

Rb, poly

B anthracis spores

SA11-A

-

Spore antigen

Antibodies

spore antigens (~92-94 kDa)

Mouse, mono

B anthracis spores

SA12-M, SA13-M

-
PA Antibodies spore extract Mouse, mono B anthracis spores, PA PA11-M, PA12-M, PA-13-M, PA14-M, PA15-M -
 PA63 Protein PA 63 Kda B. anthracis Anthrax Protective Antigen (63 kda) Recombinant purified protein,
Cat # PA63-R (100 ug)
 PA83 Protein  PA 83 Kda B. anthracis Protective antigen (83 kda) Recombinant purified protein,
Cat # PA83-R (100 ug)
 LF Antibodies spore extract Mouse, mono B anthracis spore LF11-M & LF12-M  -
 Lethal Factor Protease Substrate 1, Fluorogenic  A 19-aa internally quenched Coumarin peptide substrate for monitoring LF protease activity; Cat # LFPS-1 (500 ug)
 Lethal Factor Protease Substrate 2, Colorimetric   A 14-aa pNA derivative MEK2 peptide substrate for high-throughput screening of LF inhibitors; Cat # LFPS-2 (1 mg)
 Lethal Factor Protease Substrate 3, Fluorogenic A 14-aa AMC derivative MEK2 peptide substrate for high-throughput screening of LF inhibitors; Cat # LFPS-3 (1 mg)
 Lethal Factor Protease Inhibitor-1  Cell permeable, 14-aa MEK2 analog, competitive inhibitor of LF
Cat # LFPI-4 (1 mg)
 Control Rabbit IgG  For use in ELISA, Western, Immunohisto. 20009-1 (1 mg)  



Rb=rabbit; m=mouse; r=rat; h=human; s=sheep; b=bovine; c=chicken; d=dog; ~CT or ~NT=near C or N-terminus. EC=Extracellular; CL=Cytoplasmic loop;

* Expected antibody crossreactivity information is mostly based upon high (>70%) sequence conservation of antigenic/control peptides in various species. When antibody crossreactivity has actually been experimentally confirmed in various species, it will be mentioned in the appropriate data sheets.

"Neat Antisera or antisera" are the unpurified antiserum and it is suitable for ELISA and Western.
"Affinity pure" IgG may be more suitable for immunohistochemical (IHC) applications and to reduce background in most immunological applications including ELISA and Western.
"Control peptides" can not be used for Western as they are very short peptides. They are intended for ELISA or antibody blocking studies to establish antibody specificity.
Western blot +ve protein controls, where available, are semi-pure, pure or recombinant proteins that are formulated in SDS-PAGE sample buffer. They are recommended to be used for Western (load 10 ul/lane) for visualization with antibodies.