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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 176 products:
Human Monoclonal ANTXR1 Primary Antibody for ICC, IF - ABIN252539
Matsuda, Ohga, Hida, Muraki, Tsuchiya, Kurosu, Akino, Shih, Totsuka, Klagsbrun, Shindoh, Hida: Isolated tumor endothelial cells maintain specific character during long-term culture. in Biochemical and biophysical research communications 2010
Show all 4 Pubmed References
Human Polyclonal ANTXR1 Primary Antibody for ELISA, WB - ABIN250274
Carson-Walter, Watkins, Nanda, Vogelstein, Kinzler, St Croix: Cell surface tumor endothelial markers are conserved in mice and humans. in Cancer research 2001
These studies identify ANTXR1, a class of receptor that is shared by a mammalian virus and a bacterial toxin, as the cellular receptor for Seneca Valley virus.
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.
Anthrax Toxin Protective Antigen Variants That Selectively Utilize either the CMG2 (show ANTXR2 Antibodies) or TEM8 Receptors for Cellular Uptake and Tumor Targeting.
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