Cathepsin D is a protein that in humans is encoded by the CTSD gene. This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor.
Cathepsins are a group of intracellular proteolytic enzymes located within the lysosomes. On the basis of the specificity towards their substrates, the cathepsins have been assigned the names: Cathepsins A, B, C, D, E, G H and L.
Cathepsin D (EC 3.4.23.5) has been found to be widely distributed in various tissues but spleen is a rich source of this enzyme. Cathepsins A and D work synergistically to hydrolyze protein substrates. Cathepsin D acts as a true proteinase on substrates such as denatured hemoglobin at the pH range of 2.8–3.0. In this respect it behaves enzymatically similar to pepsin.
Source:Native Protein, from Human Plasma
Molecular Weight:~42kD
Specific Activity:~300units/mg.
Unit Definition:One unit of activity is defined as the amount of enzyme which digests hemoglobin-releasing peptides which are soluble in 10% TCA. The reaction is measured by an increase of an A280 of 1/60 minutes at 37°C.
Storage and Stability:Lyophilized and reconstituted products are stable for 6 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：50ug
Source Antigen：Human Plasma
Grade：Highly Purified
Purity：≥98%
Form：Supplied as a lyophilized powder from 2mM sodium phosphate, pH 6.5. Reconstitute with sterile ddH2O.
