Cathepsin D(CatD) is a ubiquitously expressed lysosomal aspartyl
protease involved in the normal degradation of proteins apoptosis and
autophagy. Human CatD is synthesized on the endoplasmic reticulum as
a pre-pro-enzyme. Preprocathepsin D(412aa) is cleaved and glycosylated
to form an inactive procathepsin D (392aa) and then further cleaved to
generate an active intermediate (348aa) single-chain molecule. The active
intermediate is further processed into mature two chain form of cathepsin
D, this processing step is carried out by cathepsin B or L. The two-chain
form consists of an amino terminal light chain (14 kDa) and a
carboxyl-terminal heavy chain (34 kDa). Additionally, several more amino
acids are removed from the carboxyl terminus of the 34 kDa heavy chain.
Procathepsin D (pCD), secreted from cancer cells, acts as a mitogen on
both cancer and stromal cells and stimulates their proinvasive and
pro-metastatic properties.

Western Blot: 1:5,000;

Type: Primary
Antigen: CTSD (cathepsin D)
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human, Rat