Difference between revisions of "Part:BBa K1166004"

 
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<partinfo>BBa_K1166004 short</partinfo>
 
<partinfo>BBa_K1166004 short</partinfo>
  
Contains the T7 expression cassette for the soluble part of TRAIL with an N-terminal histidine tag (x6) to enhance its purification. It is known to cause apoptosis by binding a membrane receptor.
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Contains the T7 expression cassette for a soluble part of TRAIL with an N-terminal histidine tag (x6) to enhance its purification. It is known to cause apoptosis in various cancer cell lines with minimal cytotoxicity toward normal cells (Walczak, et al., 1999).
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TRAIL (TNF Related Apoptosis Inducing Ligand) induces apoptosis by binding to two death receptor domains, TRAIL-R1(DR4) and TRAIL-R2(DR5) (Schneider, et al., 1997). The binding of TRAIL triggers the trimerization of the death receptors that recruit and activate FADD a death domain-containing protein, FADD then recruits and activates caspase-8, leading to the formation of the death-inducing signaling complex (DISC) (Zhang L, et al., 2005).
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References
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Schneider P, Thome M, Burns K, Bodmer JL, Hofmann K, Kataoka T, Holler N, Tschopp J. (1997). TRAIL receptors 1 (DR4) and 2 (DR5) signal FADD-dependent apoptosis and activate NF-kappaB. Immunity. 7(6):831-6.
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Zhang L, Fang B. (2005). Mechanisms of resistance to TRAIL-induced apoptosis in cancer. Cancer Gene Ther. 12(3):228-37.
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Walczak H, Miller RE, Ariail K, Gliniak B, Griffith TS, Kubin M, Chin W, Jones J, Woodward A, Le T, Smith C, Smolak P, Goodwin RG, Rauch CT, Schuh JC, Lynch DH. (1999). Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat Med. 5(2):157-63.
  
 
<!-- Add more about the biology of this part here
 
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Revision as of 18:04, 27 September 2013

sTRAIL

Contains the T7 expression cassette for a soluble part of TRAIL with an N-terminal histidine tag (x6) to enhance its purification. It is known to cause apoptosis in various cancer cell lines with minimal cytotoxicity toward normal cells (Walczak, et al., 1999).

TRAIL (TNF Related Apoptosis Inducing Ligand) induces apoptosis by binding to two death receptor domains, TRAIL-R1(DR4) and TRAIL-R2(DR5) (Schneider, et al., 1997). The binding of TRAIL triggers the trimerization of the death receptors that recruit and activate FADD a death domain-containing protein, FADD then recruits and activates caspase-8, leading to the formation of the death-inducing signaling complex (DISC) (Zhang L, et al., 2005).

References

Schneider P, Thome M, Burns K, Bodmer JL, Hofmann K, Kataoka T, Holler N, Tschopp J. (1997). TRAIL receptors 1 (DR4) and 2 (DR5) signal FADD-dependent apoptosis and activate NF-kappaB. Immunity. 7(6):831-6.

Zhang L, Fang B. (2005). Mechanisms of resistance to TRAIL-induced apoptosis in cancer. Cancer Gene Ther. 12(3):228-37.

Walczak H, Miller RE, Ariail K, Gliniak B, Griffith TS, Kubin M, Chin W, Jones J, Woodward A, Le T, Smith C, Smolak P, Goodwin RG, Rauch CT, Schuh JC, Lynch DH. (1999). Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat Med. 5(2):157-63.

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]