|Calculated MW||This protein is fused with polyhistidine tag at the C-terminus, has a calculated MW of 43.6 kDa. The predicted N-terminus is Ser 19. DTT-reduced Protein migrates as 45-55 kDa due to glycosylation.|
|Other Names||CTSD, Cathepsin D, CPSD, CLN10|
|Results||Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2. The specific activity is >450 pmol/min/ µg.|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in 50 mM MES, pH 6.5 with 100 mM NaCl. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.|
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Provided below are standard protocols that you may find useful for product applications.
Cathepsin D is also known as CTSD, CPSD, which belongs to the peptidase A1 family. Cathepsin D can be cleaved into the following 2 chains: cathepsin D light chain and cathepsin D heavy chain, which is expressed in the aorta extracellular space (at protein level). The catalytic activity of Cathepsin D is specificity similar to, but narrower than, that of pepsin A. Cathepsin D does not cleave the 4-Gln-|-His-5 bond in B chain of insulin. Cathepsin D involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.
Faust P.L.,et al.Proc. Natl. Acad. Sci. U.S.A. 82:4910-4914(1985).
Westley B.R.,et al.Nucleic Acids Res. 15:3773-3786(1987).
Redecker B.,et al.DNA Cell Biol. 10:423-431(1991).
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Kalnine N.,et al.Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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