Difference between revisions of "Part:BBa K143035"
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<partinfo>BBa_K143035 short</partinfo> | <partinfo>BBa_K143035 short</partinfo> | ||
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Elastin is a polymeric extracellular matrix protein found in tissues that require the ability to extend and recoil. Examples of elastin containing tissues include arteries, lungs, ligaments and skin. | Elastin is a polymeric extracellular matrix protein found in tissues that require the ability to extend and recoil. Examples of elastin containing tissues include arteries, lungs, ligaments and skin. | ||
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Construct EP20-24-24 for human elastin polypeptide consists of distinct exons which code for alternating hydrophobic regions and crosslinking domains from the human elastin polypeptide gene <cite>1</cite>. | Construct EP20-24-24 for human elastin polypeptide consists of distinct exons which code for alternating hydrophobic regions and crosslinking domains from the human elastin polypeptide gene <cite>1</cite>. | ||
Under appropriate conditions of temperature and ionic strength, elastin polypeptide undergoes a self-aggregation process known as coacervation. Coacervation is usually induced by an increase in temperature and causes the protein to separate from the solution as a second phase. Unlike most proteins which undergo denaturation when the temperature of the solution increases, elastin polypeptides become more ordered through coacervation <cite>2</cite>. | Under appropriate conditions of temperature and ionic strength, elastin polypeptide undergoes a self-aggregation process known as coacervation. Coacervation is usually induced by an increase in temperature and causes the protein to separate from the solution as a second phase. Unlike most proteins which undergo denaturation when the temperature of the solution increases, elastin polypeptides become more ordered through coacervation <cite>2</cite>. | ||
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LipA is a signal peptide from the ''B. subtilis'' genome. In general, signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached)through an appropriate secretory pathway<cite>3</cite>. LipA has been successfully used in the secretion of heterologous proteins such as cutinase by ''B. subtilis''. | LipA is a signal peptide from the ''B. subtilis'' genome. In general, signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached)through an appropriate secretory pathway<cite>3</cite>. LipA has been successfully used in the secretion of heterologous proteins such as cutinase by ''B. subtilis''. | ||
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#2 pmid=11911775 | #2 pmid=11911775 | ||
#3 pmid=16997527 | #3 pmid=16997527 | ||
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</biblio> | </biblio> | ||
Latest revision as of 13:15, 18 September 2008
LipA-Human Elastin (EP20-24-24) Fusion Protein
Elastin is a polymeric extracellular matrix protein found in tissues that require the ability to extend and recoil. Examples of elastin containing tissues include arteries, lungs, ligaments and skin.
Construct EP20-24-24 for human elastin polypeptide consists of distinct exons which code for alternating hydrophobic regions and crosslinking domains from the human elastin polypeptide gene 1.
Under appropriate conditions of temperature and ionic strength, elastin polypeptide undergoes a self-aggregation process known as coacervation. Coacervation is usually induced by an increase in temperature and causes the protein to separate from the solution as a second phase. Unlike most proteins which undergo denaturation when the temperature of the solution increases, elastin polypeptides become more ordered through coacervation 2.
LipA is a signal peptide from the B. subtilis genome. In general, signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached)through an appropriate secretory pathway3. LipA has been successfully used in the secretion of heterologous proteins such as cutinase by B. subtilis.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Reference
<biblio>
- 1 pmid=11738083
- 2 pmid=11911775
- 3 pmid=16997527
</biblio>