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Human Cathepsin D / CTSD Protein (His Tag)

CLN10,CPSD,HEL-S-130P

Catalog Number P12517-H08H
Organism Species Human
Host Human Cells
Synonyms CLN10,CPSD,HEL-S-130P
Molecular Weight The secreted recombinant human CTSD (pro form) consists of 405 amino acids and has a predicted molecular mass of 44 kDa. As a result of different glycosylation, the apparent molecular mass of rhCTSD is approximately 40-110 kDa in SDS-PAGE under reducing conditions.
predicted N Ser 19
SDS-PAGE
Purity > 97 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the pro form of human CTSD (P07339) (Met 1-Leu 412) was fused with a polyhistidine tag at the C-terminus.
Bio-activity Measured by its ability to bind biotinylated human CTSS-His (P10487-H08H) in a functional ELISA.
Research Area Neuroscience |Cell Adhesion Proteins |Membrane Proteins
Formulation Lyophilized from sterile 25mM MES, 150mM NaCl, pH 6.5
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Cathepsin D (CTSD), a well known lysosomal aspartyl protease and belongs to the peptidase C1 family, which is a normal and major component of lysosomes, and is found in almost all cells and tissues of mammals. Its mostly described function is intracellular catabolism in lysosomal compartments, other physiological effect include hormone and antigen processing. Cathepsin D has a specificity similar to but narrower than that of pepsin A. Cathepsin D plays an important role in the degradation of proteins, the generation of bioactive proteins, antigen processing, etc. Among different role in cell physiology, a new function of this enzyme is examined. Cathepsin D is an important regulator of apoptotic pathways in cells. It acts at different stage of intrinsic and extrinsic pathway of apoptosis. In addition, CTSD secreted from human prostate carcinoma cells are responsible for the generation of angiostatin, a potent endogenous inhibitor of angiogenesis, suggesting its contribution to the prevention of tumor growth and angiogenesis-dependent growth of metastases.
Reference
  • Fusek M, et al. (2005) Dual role of cathepsin D: ligand and protease. Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub. 149(1): 43-50.
  • Minarowska A, et al. (2007) Regulatory role of cathepsin D in apoptosis. Folia Histochem Cytobiol. 45(3): 159-63.
  • Zaidi N, et al. (2008) Cathepsin D: a cellular roadmap. Biochem Biophys Res Commun. 376(1): 5-9.