Technical Data
Cathepsin D (Cathepsin-D, CatD, CLN10, CPSD, CTSD, Lysosomal Aspartyl Peptidase, MGC2311)
Cathepsin D is a ubiquitously expressed lysosomal protease that is involved in proteolytic degradation, cell invasion, and apoptosis (1). It is suspected to play important roles in protein catabolism, antigen processing, degenerative diseases, and breast cancer progression (2). Cathepsin D is induced by estrogens in mammary cancer cells where its concentration is correlated with a higher risk of metastasis (3). It is possibly involved in Alzheimer's disease-related neurodegeneration through cleavage of amyloid precursor protein into amyloidogenic components (4). Preprocathepsin D (43kDa) is cleaved and glycosylated to form procathepsin D (46kDa), and then further cleaved, forming light and a heavy chains (15kDa and 28kDa, respectively) (5).

Suitable for use in Western Blot, Immunohistochemistry and Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Western Blot: 1:2000-1:10,000
Immunohistochemistry: 1:250-1:500
Immunocytochemistry: 1:250-1:500
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 months 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.

Manufactured incorporating RabMAb® technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
100ul-20°CBlue IceHumanRabbit
Not determined
A synthetic peptide corresponding to residues on human Cathepsin D
Supplied as a liquid in 50mM Tris-Glycine (pH 7.4), 0.15M NaCl, 40% glycerol, 0.01% sodium azide and 0.05% BSA.
Recognizes human Cathepsin D.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Steinfeld R, et al. Am J Hum Genet. 78(6):988-98, 2006 2. Baldwin ET, et al. Proc Natl Acad Sci U S A. 90(14):6796-800, 1993 3. Augereau P, et al. Mol Endocrinol. 8(6):693-703, 1994 4. Papassotiropoulos A, et al. Ann Neurol. 47(3):399-403,2000 5. Shewale JG, et al. PNAS 81(12): 3703-3707, 1984-06