Difference between revisions of "Part:BBa K5036006"
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==Part Description== | ==Part Description== | ||
It is vascular endothelial growth factor receptor which contain 3 members contain similar structures and their external parts are made up entirely of repeating segments that resemble parts of antibodies (immunoglobulin homology repeats) and they have a critical role in the formation of blood vessels and lymphatic vessels. | It is vascular endothelial growth factor receptor which contain 3 members contain similar structures and their external parts are made up entirely of repeating segments that resemble parts of antibodies (immunoglobulin homology repeats) and they have a critical role in the formation of blood vessels and lymphatic vessels. | ||
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==Usage== | ==Usage== | ||
| − | This is the extracellular domain of the second chain | + | This is the extracellular domain of the second chain dCas9-synRTK receptor which respond specifically to vascular endothelial growth factor (VEGF) which is a specific substance for wounds so when activated it transduce the signal causing dimerization of the two receptor chains and thus help in the control of transcription and prevent auto activation. |
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<html><div align="center"style="border:solid #17252A; width:100%;float:center;"><img style=" max-width:850px; | <html><div align="center"style="border:solid #17252A; width:100%;float:center;"><img style=" max-width:850px; | ||
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<p class=MsoNormal align=center style='text-align:left;border:none;width:98% ;justify-content:center;'><span | <p class=MsoNormal align=center style='text-align:left;border:none;width:98% ;justify-content:center;'><span | ||
| − | lang=EN style='font-size:11.0pt;line-height:115%'>this figure illustrates the structure of the extracellular domain of our receptor's | + | lang=EN style='font-size:11.0pt;line-height:115%'>this figure illustrates the structure of the extracellular domain of our receptor's second chain |
. </span></p></div></html> | . </span></p></div></html> | ||
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lang=EN style='font-size:11.0pt;line-height:115%'>The figure shows immunohistochemical staining of proteins associated with blood vessel growth in angiosarcoma scalp tissue. Panel A reveals strong positivity for VEGF-A in tumor cells. Panels B and C demonstrate consistent positivity for VEGFR-1 and VEGFR-3, respectively, in the lining of tumor cells. Panel D shows VEGF-C expression within the angiosarcoma, surrounded by lighter areas containing lymphocyte immune cells. | lang=EN style='font-size:11.0pt;line-height:115%'>The figure shows immunohistochemical staining of proteins associated with blood vessel growth in angiosarcoma scalp tissue. Panel A reveals strong positivity for VEGF-A in tumor cells. Panels B and C demonstrate consistent positivity for VEGFR-1 and VEGFR-3, respectively, in the lining of tumor cells. Panel D shows VEGF-C expression within the angiosarcoma, surrounded by lighter areas containing lymphocyte immune cells. | ||
</span></p></div></html> | </span></p></div></html> | ||
| + | ==Reference== | ||
| + | Itakura, E., Yamamoto, H., Oda, Y., & Tsuneyoshi, M. (2008). Detection and characterization of vascular endothelial growth factors and their receptors in a series of angiosarcomas. Journal of surgical oncology, 97(1), 74-81. | ||
Revision as of 17:54, 13 September 2024
Vascular Endothelial Growth Factor Receptor 2 (VEGF-R2)
Part Description
It is vascular endothelial growth factor receptor which contain 3 members contain similar structures and their external parts are made up entirely of repeating segments that resemble parts of antibodies (immunoglobulin homology repeats) and they have a critical role in the formation of blood vessels and lymphatic vessels.
Usage
This is the extracellular domain of the second chain dCas9-synRTK receptor which respond specifically to vascular endothelial growth factor (VEGF) which is a specific substance for wounds so when activated it transduce the signal causing dimerization of the two receptor chains and thus help in the control of transcription and prevent auto activation.
this figure illustrates the structure of the extracellular domain of our receptor's second chain .
Literature Characterization
In this study, a group of 34 angiosarcomas were examined using immunohistochemistry technique which allowed to assess the levels of proteins involved in blood vessel growth, including vascular endothelial growth factors (VEGF-A and VEGF-C) and their corresponding receptors (VEGFR-1, VEGFR-2, and VEGFR-3).
VEGF-A was expressed by 32/34 (94%), VEGF-C by 4/34 (12%), VEGFR-1 by 32/34 (94%), VEGFR-2 by 22/34 (65%), and VEGFR-3 by 27/34 (79%) .
The figure shows immunohistochemical staining of proteins associated with blood vessel growth in angiosarcoma scalp tissue. Panel A reveals strong positivity for VEGF-A in tumor cells. Panels B and C demonstrate consistent positivity for VEGFR-1 and VEGFR-3, respectively, in the lining of tumor cells. Panel D shows VEGF-C expression within the angiosarcoma, surrounded by lighter areas containing lymphocyte immune cells.
Reference
Itakura, E., Yamamoto, H., Oda, Y., & Tsuneyoshi, M. (2008). Detection and characterization of vascular endothelial growth factors and their receptors in a series of angiosarcomas. Journal of surgical oncology, 97(1), 74-81.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 364
Illegal BglII site found at 1723 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 1236
Illegal BsaI.rc site found at 46
Illegal BsaI.rc site found at 824
Illegal BsaI.rc site found at 2113