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Recombinant Human CTRL protein (rFc Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg2214

Validation Data Gallery

  • Purity of Recombinant Human CTRL was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

    Purity of Recombinant Human CTRL was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Human CTRL protein Cys19-Asn264 (Accession# P40313) with a rabbit IgG Fc tag at the C-terminus.
GeneID 1506
Accession P40313
PredictedSize 52.4 kDa
SDS-PAGE 52-65 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

CTRL(Chymotrypsin-like protease) is also named as CTRL1 and belongs to the peptidase S1 family. CTRL encode a protein of 264 amino acid and the protein has a signal peptide of 18 amino acid and a propeptide of 15 amino acid.The CTRL1 enzyme is active over a broad pH range. It expresses in pancreas and presence in intestinal fluid after stimulation of pancreatic secretion as a digestive enzyme. CTRL is a novel human exocrine pancreatic enzyme with substrate specificity similar to that of chymotrypsin. It contains the conserved sequences in the vicinity of the active site serine, aspartic acid, and histidine residues found in this family of serine proteases.

References:

1. J E Reseland, et al. (1997) J Biol Chem. 272(12):8099-104.
2. S Brenner, et al. (1988) Nature. 334(6182):528-30.