slyD (1-196) Escherichia coli Protein

CAT#: AR03015PU-L

slyD (1-196) e. coli recombinant protein, 0.5 mg

Product Images

Specifications

Product Data

• Species: Escherichia coli
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH
• Predicted MW: 21 kDa
• Concentration: lot specific
• Purity: >95% by SDS PAGE
• Presentation: Purified
• Buffer: Presentation State: Purified
  State: Liquid purified protein
  Buffer System: 20 mM Tris pH 7.5
• Bioactivity: Specific: > 220 nmoles/min/mg, defined as the amount of enzyme that cleaves
  1 umole of suc-AAPF-pNA per minute at 25°C in Tris-HCl pH 8.0 using chymotrypsin.
• Preparation: Liquid purified protein
• Applications: Protocol: Activity Assay
  1. Prepare 170 ul assay buffer into a suitable container and pre-chill on ice before use:
  The final concentrations are 200 mM Tris-HCl, pH 8.0, and 20nM chymotrypsin.
  2. Add 10 ul of recombinant SlyD protein with 1 ug in assay buffer.
  3. Mix by inversion and equilibrate to 1°C and monitor the A405nm until the value is constant using a spectrophotometer.
  4. Add 20 ul pre-chilled 5mM suc-AAFP-pNA. (Substrate was dissolved in TFE that contained 460mM LiCl to a concentration of 3 mM)
  5. Record the increase in A405 nm for 30 minutes at 25°C.
• Protein Description: Recombinant E.coli slyD was expressed in E.coli and purified by conventional chromatography.
• Storage: Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -70°C for longer.
  Avoid repeated freezing and thawing.
• Stability: Shelf life: one year from despatch.

Reference Data

• Summary: SlyD is a putative folding helper protein from the Escherichia coli cytosol, which consists of an N-terminal prolyl isomerase domain of the FKBP type and a presumably unstructured C-terminal tail. It is involved in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase.