Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
ANTXR1 encodes a type I transmembrane protein and is a tumor-specific endothelial marker that has been implicated in colorectal cancer. Additionally we are shipping anthrax Toxin Receptor 1 Proteins (14) and anthrax Toxin Receptor 1 Kits (4) and many more products for this protein.
Showing 10 out of 179 products:
Human Polyclonal ANTXR1 Primary Antibody for EIA, IF - ABIN499365
Molloy, Bresnahan, Leppla, Klimpel, Thomas: Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. in The Journal of biological chemistry 1992
Show all 5 references for ABIN499365
Human Polyclonal ANTXR1 Primary Antibody for EIA - ABIN358475
Wei, Lu, Chaudry, Leppla, Cohen: The LDL receptor-related protein LRP6 mediates internalization and lethality of anthrax toxin. in Cell 2006
Show all 3 references for ABIN358475
Human Polyclonal ANTXR1 Primary Antibody for IHC (p), WB - ABIN392154
Werner, Kowalczyk, Faundez: Anthrax toxin receptor 1/tumor endothelium marker 8 mediates cell spreading by coupling extracellular ligands to the actin cytoskeleton. in The Journal of biological chemistry 2006
Show all 3 references for ABIN392154
Human Polyclonal ANTXR1 Primary Antibody for DB - ABIN389986
Abrami, Leppla, van der Goot: Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis. in The Journal of cell biology 2006
Show all 3 references for ABIN389986
Human Polyclonal ANTXR1 Primary Antibody for EIA - ABIN358529
Bradley, Mogridge, Mourez, Collier, Young: Identification of the cellular receptor for anthrax toxin. in Nature 2001
Show all 3 references for ABIN358529
Human Polyclonal ANTXR1 Primary Antibody for DB - ABIN389930
Rainey, Wigelsworth, Ryan, Scobie, Collier, Young: Receptor-specific requirements for anthrax toxin delivery into cells. in Proceedings of the National Academy of Sciences of the United States of America 2005
Show all 3 references for ABIN389930
Human Polyclonal ANTXR1 Primary Antibody for WB - ABIN374464
Cross, Lindsey, Fantes, McKay, McGill, Cooke: The structure of a subterminal repeated sequence present on many human chromosomes. in Nucleic acids research 1991
Show all 2 references for ABIN374464
Chicken Polyclonal ANTXR1 Primary Antibody for WB - ABIN2784026
Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. in Cell 2006
Human Polyclonal ANTXR1 Primary Antibody for ELISA, WB - ABIN185280
Carson-Walter, Watkins, Nanda, Vogelstein, Kinzler, St Croix: Cell surface tumor endothelial markers are conserved in mice and humans. in Cancer research 2001
Findings suggest that down-regulation of tumor endothelial marker 8 play an important role in the inhibition of tumorigenesis and development of osteosarcoma.
TEM8 may be differentially expressed between wound types and loss of this molecule impacts HaCaT growth and migration, potentially implicating this molecule as a factor involved in successful progression of wound healing.
In the absence of any N-linked glycans, TEM8 fails to fold correctly and is recognized by the ER quality control machinery.
These studies expand the allelic spectrum in this rare condition and potentially provide insight into the role of ANTXR1 in the regulation of the extracellular matrix.
ANTXR2 (show ANTXR2 Antibodies) is expressed by human uterine smooth muscle cell and appears important for normal human uterine smooth muscle cell viability, migration and contractility.
High ANTXR1 accelerates breast tumor growth and lung metastasis.
There is an attenuation of ANTXR1 expression post-infection which may be a protective mechanism that has evolved to prevent reinfection.
Mutations affecting ANTXR1 function are responsible for GAPO syndrome's characteristic generalized defect in extracellular-matrix homeostasis.
An acidic region in the cytosolic tail of ANTXR1 decreases actin association, sending a signal that prevents binding of ANTXR1 to the protective antigen and providing evidence that cytoskeletal dynamics regulate ANTXR1 function.
Disruption of Tem8 results in impaired growth of human tumor xenografts of diverse origin including melanoma, breast, colon, and lung cancer.
An essential physiologic role for Antxr1 in arteriogenesis and peripheral artery disease.
Data demonstrate that TEM8 is an essential regulator of connective tissue homeostasis. it controls synthesis of major matrix components in both endothelial and fibroblastic cells and regulates signaling pathways and matrix degradation.
These results strongly suggest that TEM8 is the only minor anthrax toxin receptor mediating direct lethality in vivo and that other proteins implicated as receptors do not play this role.
This is the first demonstration that the ATR/TEM8 protein is highly expressed in epithelial cells, suggesting that the ATR/TEM8 expression pattern is highly relevant for understanding the pathogenesis of anthrax infection.
The mRNA transcripts of both receptors, ANTXR1 and ANTXR2 (show ANTXR2 Antibodies) were detected in J774A.1 cells and mouse tissues suggesting that anthrax edema toxin and B. anthracis Sterne spore are involved in the ANTXR mRNA regulation in host cells.
Data show that the lethality of anthrax toxin for mice is mostly mediated by CMG2 (show ANTXR2 Antibodies) and that TEM8 plays only a minor role.
Host-derived TEM8 promotes the growth of certain tumors.
This gene encodes a type I transmembrane protein and is a tumor-specific endothelial marker that has been implicated in colorectal cancer. The encoded protein has been shown to also be a docking protein or receptor for Bacillus anthracis toxin, the causative agent of the disease, anthrax. The binding of the protective antigen (PA) component, of the tripartite anthrax toxin, to this receptor protein mediates delivery of toxin components to the cytosol of cells. Once inside the cell, the other two components of anthrax toxin, edema factor (EF) and lethal factor (LF) disrupt normal cellular processes. Three alternatively spliced variants that encode different protein isoforms have been described.
anthrax toxin receptor 1
, tumor endothelial marker 8
, anthrax toxin receptor 1-like