Difference between revisions of "Team:Shanghai Metro Utd/Contribution"

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        <div class="sub-title">Contribution</div>
 +
        <div class="article-title">BBa_K4005000 </div>
 +
        <div class="article-content"><b>== Profile ==</b></div>
 +
        <div class="article-content">
 +
            Name: rANG<br />
 +
            Base Pairs: 375bp<br />
 +
            Origin: human，synthetic<br />
 +
            Properties: A coding sequence for Angiogenin.
 +
        </div>
 +
        <div class="article-content"><b>== Usage and Biology ==</b></div>
 +
        <div class="article-content">Angiogenin (Angiogenin, ANG) belongs to the secreted ribonuclease superfamily, and
 +
            was originally discovered to be an angiogenic factor derived from human tumors. Subsequent studies have
 +
            shown that ANG is also present in normal human tissues and body fluids. ANG increases the transcription of
 +
            ribosomal RNA (rRNA) in the nucleus, while vascular endothelial growth factor (VEGF) and fibroblast growth
 +
            factor-2 (FGF-2) activate mTOR and S6 kinase pathways to promote protein synthesis. Therefore, ANG can
 +
            cooperate with VEGF and FGF-2 to promote protein synthesis in endothelial cells. In addition, ANG is
 +
            necessary for endothelial cell proliferation. In addition to promoting angiogenesis, ANG is also involved in
 +
            many other physiological and pathological processes, such as neuroprotection, inflammation, and
 +
            tumorigenesis. Loss of function mutations in the ANG gene have been found in both amyotrophic lateral
 +
            sclerosis (ALS) and Parkinson's disease (PD). According to literature reports, heparan sulphate
 +
            proteoglycans (HSPGs) are required for ANG to enter cells. HSPGs are linear anionic glycosaminoglycan (GAG)
 +
            chains covalently linked to the core protein, composed of disaccharide repeating units of uronic acid and
 +
            glucosamine, and the glucosamine residues 3-OH, 6-OH and -NH And the 2-OH of uronic acid is replaced by a
 +
            sulfate group. HSPGs exist on the plasma membrane of all animals and are the main component of the
 +
            extracellular matrix. Factors such as size, location, degree of sulfation, and uronic acid in different
 +
            cells, tissues, and developmental stages contribute to the structural diversity of heparan sulphate (HS).
 +
            This structural diversity is the basis for HSPGs to perform multiple functions. In previous research, our
 +
            laboratory constructed a library of HS mutant mouse lung endothelial cells by knocking out key genes in the
 +
            HS biosynthesis process. In this study, we prokaryotic expression and purification of recombinant ANG
 +
            protein, using heparin and heparin derivatives and HS mutant mouse lung endothelial cell library to perform
 +
            enzyme-linked immunosorbent assay and flow cytometry experiments to explore the interaction between ANG and
 +
            HS The specificity and clarify its structure-activity relationship.</div>
 +
        <div class="article-title">BBa_K4005001 </div>
 +
        <div class="article-content"><b>== Profile ==</b></div>
 +
        <div class="article-content">
 +
            Name: P7 <br />
 +
            Base Pairs: 19bp<br />
 +
            Origin: T7 phage, genome<br />
 +
            Properties: A promoter for initiation of the transcription.
 +
        </div>
 +
        <div class="article-content"><b>== Construct design ==</b></div>
 +
        <div class="img-wrap no-margin">
 +
            <img src="https://static.igem.org/mediawiki/2021/d/de/T--Shanghai_Metro_Utd--contribution01.jpg" alt="">
 +
            <span>Figure 1. The rANG protein expression box.</span>
 +
        </div>
 +
        <div class="article-title">BBa_K4005004 </div>
 +
        <div class="article-content"><b>== Profile ==</b></div>
 +
        <div class="article-content">
 +
            Name: pro-rANG-His-ter<br />
 +
            Base Pairs: ~480bp<br />
 +
            Origin: human，synthetic<br />
 +
            Properties: A coding sequence for Angiogenin.
 +
        </div>
 +
        <div class="article-content"><b>== Usage and Biology ==</b></div>
 +
        <div class="article-content">Angiogenin (Angiogenin, ANG) belongs to the secreted ribonuclease superfamily,
 +
            and
 +
            was originally discovered to be an angiogenic factor derived from human tumors. Subsequent studies have
 +
            shown that ANG is also present in normal human tissues and body fluids. ANG increases the transcription
 +
            of
 +
            ribosomal RNA (rRNA) in the nucleus, while vascular endothelial growth factor (VEGF) and fibroblast
 +
            growth
 +
            factor-2 (FGF-2) activate mTOR and S6 kinase pathways to promote protein synthesis. Therefore, ANG can
 +
            cooperate with VEGF and FGF-2 to promote protein synthesis in endothelial cells. In addition, ANG is
 +
            necessary for endothelial cell proliferation. In addition to promoting angiogenesis, ANG is also
 +
            involved in
 +
            many other physiological and pathological processes, such as neuroprotection, inflammation, and
 +
            tumorigenesis. Loss of function mutations in the ANG gene have been found in both amyotrophic lateral
 +
            sclerosis (ALS) and Parkinson's disease (PD). According to literature reports, heparan sulphate
 +
            proteoglycans (HSPGs) are required for ANG to enter cells. HSPGs are linear anionic glycosaminoglycan
 +
            (GAG)
 +
            chains covalently linked to the core protein, composed of disaccharide repeating units of uronic acid
 +
            and
 +
            glucosamine, and the glucosamine residues 3-OH, 6-OH and -NH And the 2-OH of uronic acid is replaced by
 +
            a
 +
            sulfate group. HSPGs exist on the plasma membrane of all animals and are the main component of the
 +
            extracellular matrix. Factors such as size, location, degree of sulfation, and uronic acid in different
 +
            cells, tissues, and developmental stages contribute to the structural diversity of heparan sulphate
 +
            (HS).
 +
            This structural diversity is the basis for HSPGs to perform multiple functions. In previous research,
 +
            our
 +
            laboratory constructed a library of HS mutant mouse lung endothelial cells by knocking out key genes in
 +
            the
 +
            HS biosynthesis process. In this study, we prokaryotic expression and purification of recombinant ANG
 +
            protein, using heparin and heparin derivatives and HS mutant mouse lung endothelial cell library to
 +
            perform
 +
            enzyme-linked immunosorbent assay and flow cytometry experiments to explore the interaction between ANG
 +
            and
 +
            HS The specificity and clarify its structure-activity relationship.</div>
 +
        <div class="article-title">BBa_K4005005 </div>
 +
        <div class="article-content"><b>== Profile ==</b></div>
 +
        <div class="article-content">
 +
            Name: PET28a-rANG<br />
 +
            Base Pairs: 5683 bp<br />
 +
            Origin: human，synthetic<br />
 +
            Properties: A coding sequence for Angiogenin.
 +
        </div>
 +
        <div class="article-content"><b>== Usage and Biology ==</b></div>
 +
        <div class="article-content">Angiogenin (Angiogenin, ANG) belongs to the secreted ribonuclease superfamily,
 +
            and
 +
            was originally discovered to be an angiogenic factor derived from human tumors. Subsequent studies have
 +
            shown that ANG is also present in normal human tissues and body fluids. ANG increases the transcription
 +
            of
 +
            ribosomal RNA (rRNA) in the nucleus, while vascular endothelial growth factor (VEGF) and fibroblast
 +
            growth
 +
            factor-2 (FGF-2) activate mTOR and S6 kinase pathways to promote protein synthesis. Therefore, ANG can
 +
            cooperate with VEGF and FGF-2 to promote protein synthesis in endothelial cells. In addition, ANG is
 +
            necessary for endothelial cell proliferation. In addition to promoting angiogenesis, ANG is also
 +
            involved in
 +
            many other physiological and pathological processes, such as neuroprotection, inflammation, and
 +
            tumorigenesis. Loss of function mutations in the ANG gene have been found in both amyotrophic lateral
 +
            sclerosis (ALS) and Parkinson's disease (PD). </div>
 +
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<h1>Contribution </h1>
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Bronze Medal Criterion #4
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<p>Make a useful contribution for future iGEM teams. Use this page to document that contribution.
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Latest revision as of 18:38, 19 October 2021

Shanghai_Metro_Utd

Contribution
BBa_K4005000
== Profile ==
Name: rANG
Base Pairs: 375bp
Origin: human，synthetic
Properties: A coding sequence for Angiogenin.
== Usage and Biology ==
Angiogenin (Angiogenin, ANG) belongs to the secreted ribonuclease superfamily, and was originally discovered to be an angiogenic factor derived from human tumors. Subsequent studies have shown that ANG is also present in normal human tissues and body fluids. ANG increases the transcription of ribosomal RNA (rRNA) in the nucleus, while vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF-2) activate mTOR and S6 kinase pathways to promote protein synthesis. Therefore, ANG can cooperate with VEGF and FGF-2 to promote protein synthesis in endothelial cells. In addition, ANG is necessary for endothelial cell proliferation. In addition to promoting angiogenesis, ANG is also involved in many other physiological and pathological processes, such as neuroprotection, inflammation, and tumorigenesis. Loss of function mutations in the ANG gene have been found in both amyotrophic lateral sclerosis (ALS) and Parkinson's disease (PD). According to literature reports, heparan sulphate proteoglycans (HSPGs) are required for ANG to enter cells. HSPGs are linear anionic glycosaminoglycan (GAG) chains covalently linked to the core protein, composed of disaccharide repeating units of uronic acid and glucosamine, and the glucosamine residues 3-OH, 6-OH and -NH And the 2-OH of uronic acid is replaced by a sulfate group. HSPGs exist on the plasma membrane of all animals and are the main component of the extracellular matrix. Factors such as size, location, degree of sulfation, and uronic acid in different cells, tissues, and developmental stages contribute to the structural diversity of heparan sulphate (HS). This structural diversity is the basis for HSPGs to perform multiple functions. In previous research, our laboratory constructed a library of HS mutant mouse lung endothelial cells by knocking out key genes in the HS biosynthesis process. In this study, we prokaryotic expression and purification of recombinant ANG protein, using heparin and heparin derivatives and HS mutant mouse lung endothelial cell library to perform enzyme-linked immunosorbent assay and flow cytometry experiments to explore the interaction between ANG and HS The specificity and clarify its structure-activity relationship.
BBa_K4005001
== Profile ==
Name: P7
Base Pairs: 19bp
Origin: T7 phage, genome
Properties: A promoter for initiation of the transcription.
== Construct design ==
Figure 1. The rANG protein expression box.
BBa_K4005004
== Profile ==
Name: pro-rANG-His-ter
Base Pairs: ~480bp
Origin: human，synthetic
Properties: A coding sequence for Angiogenin.
== Usage and Biology ==
Angiogenin (Angiogenin, ANG) belongs to the secreted ribonuclease superfamily, and was originally discovered to be an angiogenic factor derived from human tumors. Subsequent studies have shown that ANG is also present in normal human tissues and body fluids. ANG increases the transcription of ribosomal RNA (rRNA) in the nucleus, while vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF-2) activate mTOR and S6 kinase pathways to promote protein synthesis. Therefore, ANG can cooperate with VEGF and FGF-2 to promote protein synthesis in endothelial cells. In addition, ANG is necessary for endothelial cell proliferation. In addition to promoting angiogenesis, ANG is also involved in many other physiological and pathological processes, such as neuroprotection, inflammation, and tumorigenesis. Loss of function mutations in the ANG gene have been found in both amyotrophic lateral sclerosis (ALS) and Parkinson's disease (PD). According to literature reports, heparan sulphate proteoglycans (HSPGs) are required for ANG to enter cells. HSPGs are linear anionic glycosaminoglycan (GAG) chains covalently linked to the core protein, composed of disaccharide repeating units of uronic acid and glucosamine, and the glucosamine residues 3-OH, 6-OH and -NH And the 2-OH of uronic acid is replaced by a sulfate group. HSPGs exist on the plasma membrane of all animals and are the main component of the extracellular matrix. Factors such as size, location, degree of sulfation, and uronic acid in different cells, tissues, and developmental stages contribute to the structural diversity of heparan sulphate (HS). This structural diversity is the basis for HSPGs to perform multiple functions. In previous research, our laboratory constructed a library of HS mutant mouse lung endothelial cells by knocking out key genes in the HS biosynthesis process. In this study, we prokaryotic expression and purification of recombinant ANG protein, using heparin and heparin derivatives and HS mutant mouse lung endothelial cell library to perform enzyme-linked immunosorbent assay and flow cytometry experiments to explore the interaction between ANG and HS The specificity and clarify its structure-activity relationship.
BBa_K4005005
== Profile ==
Name: PET28a-rANG
Base Pairs: 5683 bp
Origin: human，synthetic
Properties: A coding sequence for Angiogenin.
== Usage and Biology ==
Angiogenin (Angiogenin, ANG) belongs to the secreted ribonuclease superfamily, and was originally discovered to be an angiogenic factor derived from human tumors. Subsequent studies have shown that ANG is also present in normal human tissues and body fluids. ANG increases the transcription of ribosomal RNA (rRNA) in the nucleus, while vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF-2) activate mTOR and S6 kinase pathways to promote protein synthesis. Therefore, ANG can cooperate with VEGF and FGF-2 to promote protein synthesis in endothelial cells. In addition, ANG is necessary for endothelial cell proliferation. In addition to promoting angiogenesis, ANG is also involved in many other physiological and pathological processes, such as neuroprotection, inflammation, and tumorigenesis. Loss of function mutations in the ANG gene have been found in both amyotrophic lateral sclerosis (ALS) and Parkinson's disease (PD).

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