Cathepsin D (CTSD) Active Protein | CTSD active protein
Active Cathepsin D (CTSD)
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 degree C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition.
Activity Data
(Figure. The binding activity of CTSD with HSP90b1.Cathepsin D (CSTD) is an aspartic protease that depends critically on protonation of its active site Asp residue. Along with Asp-protonation, lower pH also leads to conformational switch in cathepsin-D: the N-terminal segment of the protease moves out of the active site as pH drops. Similar to other aspartic protainases, cathepsin D accommodates up to 8 amino acid residues in the binding cleft of the active site. The main physiological functions of cathepsin D consist of metabolic degradation of intracellular proteins, activation and degradation of polypeptide hormones and growth factors, activation of enzymatic precursors, processing of enzyme activators and inhibitors, brain antigen processing and regulation of programmed cell death. Besides, Heat Shock Protein 90kDa Beta 1 (HSP90b1) has been identified as an interactor of CSTD, thus a binding ELISA assay was conducted to detect the interaction of recombinant human CSTD and recombinant human HSP90b1. Briefly, CSTD were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100muL were then transferred to HSP90b1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CSTD pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of CSTD and HSP90b1 was shown in Figure 1, and this effect was in a dose dependent manner.)
NCBI and Uniprot Product Information
NCBI Description
This gene encodes a member of the A1 family of peptidases. The encoded preproprotein is proteolytically processed to generate multiple protein products. These products include the cathepsin D light and heavy chains, which heterodimerize to form the mature enzyme. This enzyme exhibits pepsin-like activity and plays a role in protein turnover and in the proteolytic activation of hormones and growth factors. Mutations in this gene play a causal role in neuronal ceroid lipofuscinosis-10 and may be involved in the pathogenesis of several other diseases, including breast cancer and possibly Alzheimer's disease. [provided by RefSeq, Nov 2015]
Uniprot Description
CTSD: Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease. Consists of a light chain and a heavy chain. Belongs to the peptidase A1 family.
Protein type: Protease; Autophagy; EC 3.4.23.5; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 11p15.5
Cellular Component: extracellular matrix; lysosomal lumen; extracellular space; lysosome; melanosome; extracellular region
Molecular Function: protein binding; aspartic-type endopeptidase activity
Biological Process: extracellular matrix disassembly; collagen catabolic process; extracellular matrix organization and biogenesis; antigen processing and presentation of exogenous peptide antigen via MHC class II; proteolysis
Disease: Ceroid Lipofuscinosis, Neuronal, 10
