Recombinant Human ANGPTL7 protein, Mouse IgG2a Fc-tagged
|Product Overview :||Recombinant Human ANGPTL7 protein (Gln27-Pro346), fused to Mouse IgG2a Fc tag at C-terminus, was expressed in human 293 cells (HEK293).|
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|Description :||Angiopoietin-like 7 (ANGPTL7) is also known as Corneal-Derived Transcript 6 (CDT6), and is a secreted glycoprotein that is structurally related to the angiopoietins. It is expressed in the corneal stroma, trabecular meshwork, and sclera and is elevated in glaucoma aqueous humor. Recently, ANGPTL proteins, including ANGPTL-2, -3, -4, -5 and -7, are identified as growth factors in combination with SCF, Thrombopoietin, IGF-II and FGF acidic that enhance the expansion and engraftment of human and mouse hematopoietic stem cells.|
|Tag :||Mouse IgG2a Fc|
|Form :||Lyophilized from 0.22 um filtered solution in Tris with Glycine, Arginine and NaCl, pH7.5, 10% trehalose.|
|Molecular Mass :||The protein has a calculated MW of 64.1 kDa. The protein migrates as 60 kDa and 76 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.|
|Protein length :||320|
|Endotoxin :||Less than 1.0 EU per ug by the LAL method.|
|Purity :||>90% as determined by SDS-PAGE.|
|Storage :||For long term storage, the product should be stored at lyophilized state at -20 centigrade or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
-20 centigrade to -70 centigrade for 12 months in lyophilized state;
-70 centigrade for 3 months under sterile conditions after reconstitution.
|Reconstitution :||It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4ºC before opening to recover the entire contents.|
|Gene Name :||ANGPTL7|
|Official Symbol :||ANGPTL7|
|Synonyms :||ANGPTL7; angiopoietin-like 7; angiopoietin-related protein 7; AngX; CDT6; angiopoietin-like protein 7; angiopoietin-like factor (CDT6); cornea-derived transcript 6 protein; dJ647M16.1; RP4-647M16.2|
|Gene ID :||10218|
|mRNA Refseq :||NM_021146|
|Protein Refseq :||NP_066969|
|UniProt ID :||O43827|
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
Q&As (13)Ask a question
ANGPTL7 has been shown to interact with several proteins and molecules. For example, it can interact with integrins, which are cell adhesion receptors involved in angiogenesis. ANGPTL7 has also been found to interact with heparan sulfate proteoglycans, which are molecules that help regulate cell adhesion and signaling during angiogenesis. Additionally, ANGPTL7 has been reported to interact with certain extracellular matrix proteins, such as fibronectin and collagen. These interactions suggest that ANGPTL7 may have a role in modulating cell-matrix interactions during angiogenesis.
ANGPTL7 can have both pro-angiogenic and anti-angiogenic effects, depending on the context and cellular environment. In general, ANGPTL7 promotes blood vessel formation by stimulating endothelial cell migration, proliferation, and tube formation. It can also enhance angiogenic sprouting by promoting the proliferation and migration of endothelial tip cells. However, ANGPTL7 can also negatively regulate angiogenesis by inhibiting the activity of certain pro-angiogenic factors, such as VEGF. The precise mechanisms through which ANGPTL7 regulates blood vessel formation are still being investigated.
The expression of ANGPTL7 can be regulated by various factors and signaling pathways. It has been found that certain growth factors, such as vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-β), can stimulate ANGPTL7 expression. Additionally, transcription factors like hypoxia-inducible factor-1 alpha (HIF-1α) and forkhead box protein C1 (FOXC1) have been shown to regulate the expression of ANGPTL7.
At present, there are no approved drugs specifically targeting ANGPTL7. However, research is underway to develop therapeutic strategies that modulate ANGPTL7 activity. This includes exploring small molecules, antibodies, or RNA-based approaches to inhibit or modify ANGPTL7 function. These potential therapies may have future applications in the treatment of angiogenesis-related disorders.
Future research on ANGPTL7 is likely to focus on further understanding its role in angiogenesis, as well as its implications in disease pathology. This may involve studying the molecular mechanisms by which ANGPTL7 regulates blood vessel formation and exploring its interactions with other angiogenic factors. Additionally, clinical studies may evaluate the potential of targeting ANGPTL7 for therapeutic purposes.
Yes, ANGPTL7 has been implicated in various diseases and conditions. For instance, it has been found to play a role in the development of certain eye disorders like glaucoma and increased intraocular pressure. Additionally, altered expression of ANGPTL7 has been observed in different types of cancer, suggesting its involvement in tumor angiogenesis and progression.
Research on ANGPTL7 is ongoing, and it is being studied as a potential therapeutic target. Modulating the activity of ANGPTL7 may have therapeutic benefits in diseases characterized by abnormal angiogenesis, such as cancer and certain eye disorders. However, more research is needed to fully understand its potential therapeutic applications.
As of now, there are no approved drugs or therapies specifically targeting ANGPTL7. However, due to its involvement in angiogenesis and potential implications in various diseases, including cancer and ocular disorders, researchers are actively exploring the therapeutic potential of ANGPTL7. Studies have investigated the use of ANGPTL7 inhibitors or antibodies to block its pro-angiogenic effects in preclinical models. These efforts may lead to the development of targeted therapies aimed at inhibiting ANGPTL7's activity in specific disease contexts.
Genetic mutations or polymorphisms in the ANGPTL7 gene have not been extensively studied for disease susceptibility. However, a few studies have identified specific ANGPTL7 gene variants that may be associated with ocular disorders, such as primary open-angle glaucoma. These findings suggest that genetic variations in ANGPTL7 could potentially influence disease susceptibility or progression. More research is needed to fully characterize the genetic variations of ANGPTL7 and their impact on disease susceptibility.
While ANGPTL7 is primarily known for its role in angiogenesis, emerging evidence suggests that it may be involved in other biological processes as well. For example, studies have suggested a potential role for ANGPTL7 in wound healing and tissue repair. ANGPTL7 has also been implicated in the regulation of extracellular matrix remodeling and fibrosis. Furthermore, recent studies have linked ANGPTL7 to the regulation of lipid metabolism, indicating its involvement in metabolic processes beyond angiogenesis.
ANGPTL7 has shown some potential as a biomarker for certain diseases. For example, increased expression of ANGPTL7 has been observed in the aqueous humor of glaucoma patients compared to healthy individuals, suggesting its potential as a diagnostic biomarker for this condition. Additionally, ANGPTL7 expression levels have been associated with poor prognosis in certain types of cancer, such as breast cancer and hepatocellular carcinoma. However, more research is needed to validate ANGPTL7 as a reliable biomarker and determine its clinical utility in disease diagnosis and prognosis.
While ANGPTL7 shows altered expression in certain cancers and eye disorders, it is not currently used as a diagnostic marker. Diagnostic markers for such conditions are typically specific proteins or genetic mutations that are more reliable and validated. However, ongoing research may explore the potential utility of ANGPTL7 as a diagnostic or prognostic marker in these diseases.
ANGPTL7 has shown promise as a potential target for anti-angiogenic therapies. Its ability to modulate various aspects of angiogenesis makes it an attractive candidate for interventions aimed at controlling abnormal blood vessel growth in diseases such as cancer and ocular disorders. However, further research is necessary to fully understand the complexities of ANGPTL7's functions and interactions before developing therapeutic strategies targeting this protein.
Customer Reviews (4)Write a review
This stability is particularly advantageous for long-term studies or experiments involving extended incubation periods. -
ts high level of consistency allows for precise measurements and accurate data interpretation, enhancing the reliability of my findings. -
It minimizes the risk of protein degradation and maximizes the effectiveness of the protein in various applications, such as cell signaling pathways or metabolic studies. -
The manufacturer's deep understanding of the protein and its applications enables them to promptly and effectively address any issues that may arise during my trials. -
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