Cathepsin D Rabbit Polyclonal Antibody

Function

The cathepsin family of proteolytic enzymes contains several diverse classes of proteases. The cysteine protease class comprises cathepsins B, L, H, K, S, and O. The aspartyl protease class is composed of cathepsins D and E. Cathepsin G is in the serine protease class. Most cathepsins are lysosomal and each is involved in cellular metabolism, participating in various events such as peptide biosynthesis and protein degradation. Cathepsins may also cleave some protein precursors, thereby releasing regulatory peptides. The promoter region of the cathepsin D gene contains five Sp1 binding sites and four AP-2 binding sites.

Background References

1. Sadleir KR et al. Presynaptic dystrophic neurites surrounding amyloid plaques are sites of microtubule disruption, BACE1 elevation, and increased A generation in Alzheimer\'s disease. Acta Neuropathol 132:235-56 (2016).

2. Santaguida S et al. Aneuploidy-induced cellular stresses limit autophagic degradation. Genes Dev 29:2010-21 (2015).ochem 34:200-10 (2015).

Sequence Similarity

Belongs to the peptidase A1 family.

Tissue Specificity

Expressed in the aorta extracellular space (at protein level). Expressed in liver (at protein level).

Post-translational Modification

N- and O-glycosylated.; Undergoes proteolytic cleavage and activation by ADAM30.; As well as the major heavy chain which starts at Leu-169, 2 minor forms starting at Gly-170 and Gly-171 have been identified. An additional form starting at Ala-168 has also been identified.

Subcellular Location

Lysosome, Secreted.

UNIPROT

SwissProt: P07339 Human

SwissProt: P18242 Mouse

SwissProt: P24268 Rat

Synonyms