ANTXR2A
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Zebrafish | ANTXR2A-3894Z | Recombinant Zebrafish ANTXR2A | Mammalian Cell | His |
- Involved Pathway
- Protein Function
- Interacting Protein
ANTXR2A involved in several pathways and played different roles in them. We selected most pathways ANTXR2A participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ANTXR2A were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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ANTXR2A has several biochemical functions, for example, Rho GTPase binding, actin binding, metal ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ANTXR2A itself. We selected most functions ANTXR2A had, and list some proteins which have the same functions with ANTXR2A. You can find most of the proteins on our site.
Function | Related Protein |
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Rho GTPase binding | DAAM1;DIAPH1;ARHGEF2;RHOH;DAPK3;DOCK11;PARD6A;LRRK2;DOCK9 |
actin binding | VILL;ACTN4;FMN1;DIXDC1;BAIAP2L1;MTSS1L;WDR1;CXCR4;MICAL2 |
metal ion binding | PPP4CB;LNX2B;RC3H1;HIVEP2A;ZNF436;CYP2D26;HDAC7A;ZNRF2A;ZFP652 |
receptor activity | NR2C2;CD40;CADM2A;CNTNAP1;TNPO3;ICAM1;ITGB1B;NRXN1;CRTAM |
ANTXR2A has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ANTXR2A here. Most of them are supplied by our site. Hope this information will be useful for your research of ANTXR2A.
- Q&As
- Reviews
Q&As (16)
Ask a questionCurrently, there are no specific drugs or treatments that directly target ANTXR2A. However, research is ongoing to explore the potential of blocking ANTXR2A's interaction with anthrax toxin as a therapeutic strategy for anthrax infection. Additionally, understanding the role of ANTXR2A in other diseases may lead to the development of targeted therapies in the future.
There have been reports of genetic variations and mutations in ANTXR2A in certain diseases. For example, mutations in ANTXR2A have been associated with juvenile hyaline fibromatosis, a rare genetic disorder characterized by the accumulation of hyaline material in various tissues. However, further research is needed to fully understand the extent and significance of genetic variations in ANTXR2A.
Targeting ANTXR2A may have potential therapeutic applications in the context of anthrax infection. By blocking the interaction between ANTXR2A and anthrax toxin, it may be possible to prevent or reduce the harmful effects of the toxin. However, it is important to note that this area of research is still being explored, and more studies are needed to evaluate the feasibility and effectiveness of such therapeutic approaches.
ANTXR2A is not widely used as a diagnostic marker for diseases. However, in certain cases, elevated levels of ANTXR2A expression have been observed in tumors, such as breast cancer and ovarian cancer. This suggests that ANTXR2A levels could potentially be explored as a biomarker for these cancers. Further research is needed to determine the diagnostic utility of ANTXR2A in various diseases.
ANTXR2A serves as a receptor for anthrax protective antigen (PA), a component of anthrax toxin. When PA binds to ANTXR2A on the cell surface, it undergoes proteolytic cleavage, allowing the binding and internalization of the other components of anthrax toxin. This leads to the disruption of cellular processes and contributes to the pathogenic effects of anthrax infection.
In addition to its involvement in anthrax infection, mutations or dysregulation of ANTXR2A have been associated with several human diseases. These include juvenile hyaline fibromatosis, which leads to the formation of fibrous tumors in various tissues, and infantile systemic hyalinosis, a rare disorder characterized by widespread deposition of hyaline material in multiple organs.
Yes, ANTXR2A has been found to have additional functions beyond its role as an anthrax toxin receptor. It has been implicated in cell adhesion, cell migration, and extracellular matrix organization. It is also involved in embryonic development, as its expression is detected in various fetal tissues.
Although there are no specific therapies targeting ANTXR2A currently available, its involvement in anthrax infection and other diseases makes it a potential target for future therapeutic development. In the case of anthrax, blocking the interaction of ANTXR2A with anthrax toxin could be a viable strategy for preventing or treating infection. Additionally, understanding the role of ANTXR2A in other diseases may reveal opportunities for therapeutic interventions in the future.
The potential of targeting ANTXR2A for therapeutic purposes is still being investigated. As ANTXR2A is involved in angiogenesis and tumor progression, inhibiting its function could be a strategy to suppress tumor growth and metastasis. One approach being explored is the use of monoclonal antibodies or small-molecule inhibitors to block ANTXR2A activity. Preliminary studies have shown promising results in inhibiting tumor growth in animal models.
ANTXR2A is expressed in a wide range of cell types, including epithelial cells, fibroblasts, endothelial cells, and certain immune cells. Its expression levels may vary depending on the cell and tissue type.
Yes, mutations in ANTXR2A have been associated with a rare genetic disorder called hyaline fibromatosis syndrome (HFS). HFS is characterized by the abnormal accumulation of hyaline material in the skin, joints, and internal organs, resulting in a range of symptoms including joint contractures, skin nodules, and organ dysfunction. These mutations impair the function of ANTXR2A, leading to abnormal tissue deposition and fibrosis. HFS is inherited in an autosomal recessive manner, meaning that both copies of the ANTXR2A gene must have mutations for the disorder to manifest. Genetic counseling and supportive management are typically provided for individuals with HFS.
Yes, ANTXR2A has been found to interact with various proteins. Apart from its interaction with anthrax protective antigen, it has been shown to interact with extracellular matrix proteins like collagen IV, laminin, and fibronectin. It also interacts with proteins involved in cell signaling and adhesion, such as integrins and focal adhesion kinase (FAK).
ANTXR2A does have some involvement in immune response as it is expressed in immune cells like macrophages and dendritic cells. However, its exact role in the immune system is not well-defined. It may play a part in immune cell adhesion, migration, or communication, but further research is needed to fully understand its immune-related functions.
ANTXR2A has been linked to several signaling pathways involved in cell adhesion, migration, and angiogenesis. It interacts with integrins, a family of cell surface receptors, and modulates their signaling, including the activation of small GTPases such as RhoA and Rac1. ANTXR2A has also been found to regulate the expression and activity of matrix metalloproteinases (MMPs), which are involved in extracellular matrix remodeling and tumor invasion. Additionally, ANTXR2A may interact with growth factor receptors and affect downstream signaling cascades. However, more research is needed to fully understand the signaling pathways associated with ANTXR2A.
Yes, genetic variants and polymorphisms in ANTXR2A have been identified. These variations can occur within the coding regions of the gene, potentially leading to changes in the structure or function of the protein. Research on these genetic variants is ongoing to determine their impact on disease susceptibility or other biological processes.
Yes, ANTXR2A protein is expressed in various normal tissues, including the liver, kidney, heart, lung, and intestines. It is also present in certain immune cells, such as macrophages and dendritic cells.
Customer Reviews (4)
Write a reviewthe manufacturer's commitment to quality control and product development is admirable.
This quality control instills trust in the product, eliminating any worries about variability and ensuring the integrity of my research outcomes.
the ANTXR2A protein offers exceptional advantages in my trials, facilitating my exploration of important cellular mechanisms.
Their rigorous testing procedures and attention to detail guarantee the consistency and reliability of the ANTXR2A protein across different batches.
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