Mouse Cathepsin D Biotinylated Antibody Summary
Ile21-Leu410
Accession # Q3UCD9
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Mouse Cathepsin D by Western Blot VEGF replenishment reverses defective autophagy in NP–C mice.(a) Western blot analysis of LC3, beclin-1, p62 and cathepsin D in primary cultured PNs derived from WT, NP–C and VEGF/NP–C mice (WT, n=5; NP–C, n=6; and VEGF/NP–C, n=6). (b) Immunocytochemistry of LC3 in WT, NP–C and VEGF/NP–C PNs (n=6 per group; scale bar, 20 μm). (c) Cathepsin D activity in primary cultured PNs (WT, n=5; NP–C, n=6; and VEGF/NP–C, n=6). (d) Western blot analysis of LC3, beclin-1, p62 and cathepsin D in the cerebellums of 6-week-old WT, NP–C and VEGF/NP–C mice (WT, n=6; NP–C, n=7; and VEGF/NP–C, n=7). (e) Cathepsin D activity in the cerebellums of WT, NP–C and VEGF/NP–C mice (WT, n=5; NP–C, n=6; and VEGF/NP–C, n=6). (f) EM images and quantification data of the cerebellum (n=5 per group; low-magnification scale bar, 1 μm; high-magnification scale bar, 200 nm). Arrow indicates autophagic vacuole. (g) Western blot analysis of Rab5 and Rab7 levels in the cerebellum (n=6 per group). (h) Cerebellar sections were immunostained with anti-active caspase-3 and the number of active caspase-3-positive cells in PCL was quantified (n=5 per group; scale bar, 50 μm). a–g, one-way analysis of variance, Tukey’s post hoc test. h, Student’s t-test. *P<0.05, **P<0.01, ***P<0.005. All error bars indicate s.e.m. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/25417698), licensed under a CC-BY license. Not internally tested by R&D Systems.
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Detection of Mouse Cathepsin D by Western Blot VEGF replenishment reverses defective autophagy in NP–C mice.(a) Western blot analysis of LC3, beclin-1, p62 and cathepsin D in primary cultured PNs derived from WT, NP–C and VEGF/NP–C mice (WT, n=5; NP–C, n=6; and VEGF/NP–C, n=6). (b) Immunocytochemistry of LC3 in WT, NP–C and VEGF/NP–C PNs (n=6 per group; scale bar, 20 μm). (c) Cathepsin D activity in primary cultured PNs (WT, n=5; NP–C, n=6; and VEGF/NP–C, n=6). (d) Western blot analysis of LC3, beclin-1, p62 and cathepsin D in the cerebellums of 6-week-old WT, NP–C and VEGF/NP–C mice (WT, n=6; NP–C, n=7; and VEGF/NP–C, n=7). (e) Cathepsin D activity in the cerebellums of WT, NP–C and VEGF/NP–C mice (WT, n=5; NP–C, n=6; and VEGF/NP–C, n=6). (f) EM images and quantification data of the cerebellum (n=5 per group; low-magnification scale bar, 1 μm; high-magnification scale bar, 200 nm). Arrow indicates autophagic vacuole. (g) Western blot analysis of Rab5 and Rab7 levels in the cerebellum (n=6 per group). (h) Cerebellar sections were immunostained with anti-active caspase-3 and the number of active caspase-3-positive cells in PCL was quantified (n=5 per group; scale bar, 50 μm). a–g, one-way analysis of variance, Tukey’s post hoc test. h, Student’s t-test. *P<0.05, **P<0.01, ***P<0.005. All error bars indicate s.e.m. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/25417698), licensed under a CC-BY license. Not internally tested by R&D Systems.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Cathepsin D
Cathepsin D is a lysosomal aspartic protease of the pepsin family (4). Mouse Cathepsin D is synthesized as a precursor protein, consisting of a signal peptide (residues 1‑20), a propeptide (residues 21‑64), and a mature chain (residues 65‑410) (1‑3). It is expressed in most cells and overexpressed in breast cancer cells (5). It is a major enzyme in protein degradation in lysosomes, and also involved in the presentation of antigenic peptides. Mice deficient in this enzyme showed a progressive atrophy of the intestinal mucosa, a massive destruction of lymphoid organs, and a profound neuronal ceroid lipofucinosis, indicating that Cathepsin D is essential for proteolysis of proteins regulating cell growth and tissue homeostasis (6). Cathepsin D secreted from human prostate carcinoma cells is responsible for the generation of angiostatin, a potent endogeneous inhibitor of angiogenesis (6).
- Diedrich, et al. (1990) Nucl. Acid Res. 18:7184.
- Grusby, et al. (1990) Nucl. Acid Res. 18:4008.
- Hetman, et al. (1994) DNA Cell Biol. 13:419.
- Conner (2004) in Handbook of Proteolytic Enzymes (Barrett, et al. eds) Elsevier Academic Press, San Diego, p. 43.
- Rochefort, et al. (2000) Clin. Chim. Acta. 291:157.
- Tsukuba, et al. (2000) Mol. Cells 10:601.
Product Datasheets
Citation for Mouse Cathepsin D Biotinylated Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Pathological roles of the VEGF/SphK pathway in niemann-Pick type C neurons.
Authors: Lee H, Lee Jk, Park Mh et al.
Nat Commun.
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