Difference between revisions of "Part:BBa K4586002"

Revision as of 15:17, 24 September 2023

ZF21.16

Part Description

Zinc finger proteins are considered one of the most unique and huge collections of proteins that are variable in their biological function and structure. In our condition this zinc finger protein recognizes a specific DNA sequence thus ZF21.16 can be combined with any other protein as transcription factor to direct its activity toward the target sequences that are located near the gene of interest.

Usage

We used this part in our design to form the internal domain of our syn notch receptor (BBa_K4586022). This internal domain is released after receptor activation and guided by the ZF21.16 to the target promoter that regulates the levels of expression of our therapeutic agent as shown in figure 1.

Figure 1: This figure illustrates the design of our biological circuit expressing our therapeutic agent under the control of the VP64 transcription module that regulates the activity of the ZF21.16minCMV promoter.

Literature Characterization

The study used ZF21 antibody for detection of ZF21 by Western blot at 1 µg/mL. For immunofluorescence, start at 20 µg/mL.

(A)western blot analysis of ZF21 in 3T3 cell tissue lysate with ZF 21 antibodies in abscence of blocking peptide while (B) the same western blot analysis in presence of blocking peptide

References

Nagano, M., Hoshino, D., Koshiba, S., Shuo, T., Koshikawa, N., Tomizawa, T., Hayashi, F., Tochio, N., Harada, T., Akizawa, T., Watanabe, S., Handa, N., Shirouzu, M., Kigawa, T., Yokoyama, S., & Seiki, M. (2011). ZF21 protein, a regulator of the disassembly of focal adhesions and cancer metastasis, contains a novel noncanonical pleckstrin homology domain. The Journal of biological chemistry, 286(36), 31598–31609. https://doi.org/10.1074/jbc.M110.199430 Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 25: / Line 25: @@
 <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%'>Figure 1: This figure illustrates the design of our biological circuit expressing our therapeutic agent under the control of the VP64 transcription module that regulates the activity of the ZF21.16minCMV promoter.   </span></p></div></html>
+==Literature Characterization==
+The study used ZF21 antibody for detection of ZF21 by Western blot at 1 µg/mL. For immunofluorescence, start at 20 µg/mL.
+<html><div align="center"style="border:solid #17252A; width:50%;float:center;"><img style="                              	max-width:850px;
+							width:75%;
+							height:auto;
+								position: relative;
+							top: 50%;
+							left: 35%;
+							transform: translate( -50%);
+							padding-bottom:25px;
+							padding-top:25px;
+							"src="https://static.igem.wiki/teams/4586/wiki/literature-characterisation-parts/zf21-16.png">
+<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%'> (A)western blot analysis of ZF21 in 3T3 cell tissue lysate with ZF 21 antibodies in abscence of blocking peptide while (B) the same western blot analysis in presence of blocking peptide </span></p></div></html>
+==References==
+Nagano, M., Hoshino, D., Koshiba, S., Shuo, T., Koshikawa, N., Tomizawa, T., Hayashi, F., Tochio, N., Harada, T., Akizawa, T., Watanabe, S., Handa, N., Shirouzu, M., Kigawa, T., Yokoyama, S., & Seiki, M. (2011). ZF21 protein, a regulator of the disassembly of focal adhesions and cancer metastasis, contains a novel noncanonical pleckstrin homology domain. The Journal of biological chemistry, 286(36), 31598–31609. https://doi.org/10.1074/jbc.M110.199430
 <!-- Add more about the biology of this part here
 ===Usage and Biology===