Technical Data
A2296-97J
ANTXR1, Control Peptide (Anthrax Toxin Receptor 1, Tumor Endothelial Marker 8, ATR, TEM8)
100ug
Molecular Biology Storage: -20CShipping: Blue Ice
Control peptide for A2296-97H, polyclonal antibody to ANTXR1.

Anthrax toxin secreted by Bacillus anthracis, consists of three polypeptides: protective antigen (PA, 83kD) lethal factor (LF, 90kD) and oedma factor (OF, 89kD). 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 mitogen activated protein kinase kinase (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 63kD fragments (PA20 and PA63) by furin or furin-like proteases. PA63 fragment then forms a complex with LF and OF components of toxin leading to internalization and 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 an 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 fact that 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.

Source:
Synthetic peptide corresponding to 15aa of human ATR-1. N-terminus (extracellular). 100% conserved in mouse and rat ATR1 and alternatively spliced isoforms 1-4.

Molecular Weight:
~3kD

Applications:
Suitable for use in ELISA and Antibody Blocking. Not suitable for Western Blot. Other applications not tested.

Recommended Dilution:
ELISA: 1ug/ml coat ELISA plates and detected with antibodies.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
Lyophilized powder may be stored at -20C. Stable for 12 months at -20C. Reconstitute with sterile buffer or ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Molecular Weight:
~3kD
Source: Synthetic peptide
Purity: Purified
Concentration: ~1mg/ml
Form: Supplied as a lyophilized powder from PBS, pH7.5.

Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
1. Bradley KA et al (2001) Nature 414, 225-229. 2. liu S and Leppla SH (2002) JBC (in press). 3. Leppla, SH (1982) PNAS 79, 3182. 4. OBrien J et al (1985) Infect Immun 47, 306. 5. Duesbery, NS et al (1998) Science 280, 734.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.