Recombinant Human Anthrax Toxin Receptor 1 (ANTXR1) Protein (His/Tag-Free)

Beta LifeScience SKU/CAT #: BLC-10467P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Anthrax Toxin Receptor 1 (ANTXR1) Protein (His/Tag-Free)

Beta LifeScience SKU/CAT #: BLC-10467P
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Product Overview

Description Recombinant Human Anthrax Toxin Receptor 1 (ANTXR1) Protein (His/Tag-Free) is produced by our Yeast expression system. This is a extracellular protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q9H6X2
Target Symbol ANTXR1
Synonyms Anthrax toxin receptor 1; ANTR1_HUMAN; Antxr1; ATR; Tumor endothelial marker 8
Species Homo sapiens (Human)
Expression System Yeast
Tag N-His/Tag-Free
Protein Length Extracellular Domain
Mol. Weight 34.4kDa
Research Area Tags & Cell Markers
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells.; (Microbial infection) Acts as a receptor for protective antigen (PA) of B.anthracis.
Subcellular Location Cell membrane; Single-pass type I membrane protein. Cell projection, lamellipodium membrane; Single-pass type I membrane protein. Cell projection, filopodium membrane; Single-pass type I membrane protein.
Protein Families ATR family
Database References

HGNC: 21014

OMIM: 230740

KEGG: hsa:84168

STRING: 9606.ENSP00000301945

UniGene: PMID: 29115620

  • Novel targets ANTXR1 and RSPO2 were confirmed to be suppressed by miR-493 directly. PMID: 28651234
  • 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. PMID: 28650343
  • expression does not affect cytotoxicity to anthrax toxin PMID: 27170489
  • Findings suggest that down-regulation of tumor endothelial marker 8 play an important role in the inhibition of tumorigenesis and development of osteosarcoma. PMID: 26996335
  • 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. PMID: 26677171
  • In the absence of any N-linked glycans, TEM8 fails to fold correctly and is recognized by the ER quality control machinery. PMID: 25781883
  • 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. PMID: 25045128
  • TEM8-targeted siRNAs also offered significant protection against lethal toxin in human macrophage-like cells. PMID: 24742682
  • ANTXR2 is expressed by human uterine smooth muscle cell and appears important for normal human uterine smooth muscle cell viability, migration and contractility. PMID: 24060446
  • High ANTXR1 accelerates breast tumor growth and lung metastasis. PMID: 23832666
  • There is an attenuation of ANTXR1 expression post-infection which may be a protective mechanism that has evolved to prevent reinfection. PMID: 23607659
  • Mutations affecting ANTXR1 function are responsible for GAPO syndrome's characteristic generalized defect in extracellular-matrix homeostasis. PMID: 23602711
  • Two new splice variants, one encoding a membrane-bound form of the receptor and the other secreted, which we have designated V4 and V5 (the latter being the only variant expressed in the prostate). PMID: 22912819
  • 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. PMID: 22303962
  • Disruption of Tem8 results in impaired growth of human tumor xenografts of diverse origin including melanoma, breast, colon, and lung cancer. PMID: 22340594
  • The copy number of CEA and TEM-8 mRNA, as detected by a real-time quantitative PCR, appears to be a promising marker for evaluating the risk of tumor spread. PMID: 21573768
  • postulate that the developmentally controlled expression of TEM8 modulates endothelial cell response to canonical Wnt signaling to regulate vessel patterning and density PMID: 21829615
  • TEM8.1 expression in breast cancer cells confers a more aggressive, proangiogenic phenotype. PMID: 22085271
  • TEM8 was expressed at a higher level in the stroma adjacent to the triple-negative breast cancer in all cases, with focal immunoreactive areas within the tumor. PMID: 21965755
  • studies reveal that TEM8 exists in different forms at the cell surface, a structure dependent on interactions with components of the actin cytoskeleton PMID: 21129411
  • Data show that the two different PA oligomers are equally stabilized by ANTXR interactions. PMID: 21079738
  • Results describe the expression, purification and crystallization of human anthrax toxin receptor 1 vWA domain to 1.8 A resolution from a single crystal. PMID: 21206026
  • the crystal structure of the TEM8 extracellular vWA domain at 1.7 A resolution. PMID: 20585457
  • actin was also found to be essential for efficient heptamerization of anthrax toxin PA, but only when bound to one of its 2 receptors, TEM8 PMID: 20221438
  • Here we describe the cloning of the human PA receptor using a genetic complementation approach PMID: 11700562
  • 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. PMID: 15689409
  • results indicate that TEM8 plays a positive role in endothelial cell activities related to angiogenesis PMID: 15777794
  • These results suggest that the TEM-8 vW and transmembrane domains may play an important biological role in TEM-8 related tubule formation. PMID: 15993844
  • because protective antigen binds to CMG2 with much higher affinity than it does to TEM8, a lower pH is needed to attenuate CMG2 binding to allow pore formation; toxin can form pores at different points in the endocytic pathway PMID: 16141341
  • Data show that cells expressing palmitoylation-defective mutant receptors are less sensitive to anthrax toxin due to a lower number of surface receptors as well as premature internalization of protective antigen without a requirement for heptamerization. PMID: 16401723
  • TEM8 is a new adhesion molecule linking collagen I or PA to the actin cytoskeleton PMID: 16762926
  • TEM8 expression levels in DC-based therapeutic vaccines would allow the selection of a subgroup of patients who are most likely to benefit from therapeutic vaccination. PMID: 19440709
  • ANTXR1 does not use an adaptor to bind the cytoskeleton. This peptide orders actin filaments into arrays, demonstrating an actin bundling activity that is novel for a membrane protein PMID: 19817382
  • ATR/TEM8 protein is highly expressed in epithelial cells, which represent the primary location for bacterial invasion. PMID: 15689409
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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