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Cat. Number
069256111085040
Chemical Name
Prostaglandin E Synthase (cytosolic, FL) Polyclonal Antibody
References
Synonyms
  • cPGES
  • cPGE Synthase
  • p23
  • Hsp90 Co-chaperone
Formulation Peptide affinity-purified IgG
Stability 1 year
Storage -20°C
Shipping Wet ice in continental US; may vary elsewhere
Specificity
Human cPGES +
Mouse cPGES +
Microsomal PGES-1 +
Microsomal PGES-2 +
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Background Reading

Tanioka, T., Nakatani, Y., Semmyo, N., et al. Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 immediate prostaglandin E2 biosynthesis. J Biol Chem 275 32775-32782 (2000).

Jakobsson, P., Thorén, S., Morgenstern, R., et al. Identification of human prostaglandin E synthase: A microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc Natl Acad Sci USA 96 7220-7225 (1999).

Size Global Purchasing
500 µl  

Description

Antigen: full length, human recombinant cPGES · Host: rabbit · Application(s): WB and ICC · Cytosolic PGE synthase (cPGES) is a glutathione-dependent enzyme with a predicted size of 18.6 kDa (23 kDa on SDS-PAGE). The enzyme is expressed in a wide variety of tissues and cells, the levels of which are unaffected by treatment with IL-1β and TNFα.1 However, enzyme expression increases approximately 3-fold in rat brain following LPS treatment.1 Microsomal PGE synthase (mPGES) is a 16 kDa protein expressed in a variety of tissues.2 In contrast to cPGES, mPGES protein expression is increases in A549 cells following treatment with IL-1β.2 The two enzymes show <10% homology at the amino acid level.

1 Tanioka, T., Nakatani, Y., Semmyo, N., et al. Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 immediate prostaglandin E2 biosynthesis. J Biol Chem 275 32775-32782 (2000).

2 Jakobsson, P., Thorén, S., Morgenstern, R., et al. Identification of human prostaglandin E synthase: A microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc Natl Acad Sci USA 96 7220-7225 (1999).

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