Mouse Cathepsin B Antibody

Catalog # Availability Size / Price Qty
AF965
AF965-SP

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Cathepsin B in Mouse Thymus.
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Product Details
Citations (21)
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Mouse Cathepsin B Antibody Summary

Species Reactivity
Mouse
Specificity
Detects mouse Cathepsin B in direct ELISAs and Western blots. In direct ELISAs, approximately 15% cross-reactivity with recombinant human Cathepsin B is observed and less than 5% cross-reactivity with recombinant mouse Cathepsin H is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse Cathepsin B
His18-Phe339
Accession # P10605
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Mouse Cathepsin B (Catalog # 965-CY)
Immunohistochemistry
5-15 µg/mL
See below
Neutralization
Measured by its ability to neutralize Recombinant Mouse Cathepsin B (0.1 µg/mL, Catalog # 965-CY) cleavage of the fluorogenic peptide substrate Z-LR-AMC (10 µM, Catalog # ES008). The Neutralization Dose (ND50) is typically 0.33 µg/mL.

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

Immunohistochemistry Cathepsin B antibody in Mouse Thymus by Immunohistochemistry (IHC-Fr). View Larger

Cathepsin B in Mouse Thymus. Cathepsin B was detected in perfusion fixed frozen sections of mouse thymus using 5 µg/mL Goat Anti-Mouse Cathepsin B Antigen Affinity-purified Polyclonal Antibody (Catalog # AF965) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence EMT in BSA-induced damaged tubule was associated with increased levels of DPP-4, integrin beta 1 and CAV1; TENE treatment ameliorated these alterations. (a–e) Multiplex immunofluorescence microscopy analysis of the EMT program and association with CAV1. Formaldehyde-fixed, paraffin-embedded (FFPE) kidney samples were labeled with epithelial markers for E-cadherin, alpha SMA and CAV1. An immunofluorescence analysis was performed by confocal microscopy. (d) The enlarged image of the inset shown in (c). The alpha SMA-positive damaged tubular cells were surrounded by alpha SMA-positive interstitial cells (f–j). Multiplex immunofluorescence was performed to analyze the crosstalk among DPP-4, integrin beta 1 and CAV1 in the BSA-injected diabetic mice. (i) The enlarged image of the inset shown in (h). DPP-4, integrin beta 1, and CAV1 were localized at the same location (likely the luminal side of the proximal tubule). The crosstalk occurred more frequently in the damaged tubular cells. Representative images from n = 7 in each group are shown. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunohistochemistry Detection of Mouse Cathepsin B by Immunohistochemistry View Larger

Detection of Mouse Cathepsin B by Immunohistochemistry BSA-injected diabetic mice exhibited high tubular levels of DPP-4, CAV1 and EMT program; TENE treatment ameliorated these alterations. Immunohistochemical analysis of (a–d) DPP-4, (e–h) CAV1, (i–l) snail and (m–p) AQP-1 from the BSA-injected control or diabetic mice with or without the TENE treatment. Scale bar, 50 μm. Representative images from n = 7 in each group are shown. Each group was analyzed with an unpaired two-tailed t-test. *P < 0.05, **P < 0.01. Data are presented as mean ± s.e.m (q–t). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence EMT in BSA-induced damaged tubule was associated with increased levels of DPP-4, integrin beta 1 and CAV1; TENE treatment ameliorated these alterations. (a–e) Multiplex immunofluorescence microscopy analysis of the EMT program and association with CAV1. Formaldehyde-fixed, paraffin-embedded (FFPE) kidney samples were labeled with epithelial markers for E-cadherin, alpha SMA and CAV1. An immunofluorescence analysis was performed by confocal microscopy. (d) The enlarged image of the inset shown in (c). The alpha SMA-positive damaged tubular cells were surrounded by alpha SMA-positive interstitial cells (f–j). Multiplex immunofluorescence was performed to analyze the crosstalk among DPP-4, integrin beta 1 and CAV1 in the BSA-injected diabetic mice. (i) The enlarged image of the inset shown in (h). DPP-4, integrin beta 1, and CAV1 were localized at the same location (likely the luminal side of the proximal tubule). The crosstalk occurred more frequently in the damaged tubular cells. Representative images from n = 7 in each group are shown. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence Alteration of the size of lysosomes and the expression of LAMP-1 in in Rab7 delta pan pancreatic acinar cells. (a–d) Immunofluorescence images of wild (a,c) and Rab7 delta pan (b,d) pancreases stained with anti-LAMP1(a,b) or anti-cathepsin B (c,d) antibodies (red). DAPI was used for nuclear staining (blue). Bars: 20 µm. (e) Quantification of the positive signals in immunofluorescence images of LAMP-1 (left panel) and cathepsin B (right panel). *P < 0.05. (f) WB of LAMP-1 using total pancreas homogenate of wild and Rab7 delta pan mice. An antibody against LAMP-1 N-terminal (top panel) and an antibody against LAMP-1 C-terminal (middle panel) were utilized. Anti-LAMP-1 N-terminal antibody revealed the shifting of intense bands to a lower position (top panel, arrow head) than that of full-length LAMP-1 (120 kDa) in Rab7 delta pan pancreas. In contrast, anti-LAMP-1 C-terminal antibody revealed bands at 120 kDa only in both wild and Rab7 delta pan pancreas (middle panel). beta -actin was used as an internal loading control (bottom panel). Image collected and cropped by CiteAb from the following open publication (https://www.nature.com/articles/s41598-017-02988-3), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence Alteration of the size of lysosomes and the expression of LAMP-1 in in Rab7 delta pan pancreatic acinar cells. (a–d) Immunofluorescence images of wild (a,c) and Rab7 delta pan (b,d) pancreases stained with anti-LAMP1(a,b) or anti-cathepsin B (c,d) antibodies (red). DAPI was used for nuclear staining (blue). Bars: 20 µm. (e) Quantification of the positive signals in immunofluorescence images of LAMP-1 (left panel) and cathepsin B (right panel). *P < 0.05. (f) WB of LAMP-1 using total pancreas homogenate of wild and Rab7 delta pan mice. An antibody against LAMP-1 N-terminal (top panel) and an antibody against LAMP-1 C-terminal (middle panel) were utilized. Anti-LAMP-1 N-terminal antibody revealed the shifting of intense bands to a lower position (top panel, arrow head) than that of full-length LAMP-1 (120 kDa) in Rab7 delta pan pancreas. In contrast, anti-LAMP-1 C-terminal antibody revealed bands at 120 kDa only in both wild and Rab7 delta pan pancreas (middle panel). beta -actin was used as an internal loading control (bottom panel). Image collected and cropped by CiteAb from the following open publication (https://www.nature.com/articles/s41598-017-02988-3), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence EMT in BSA-induced damaged tubule was associated with increased levels of DPP-4, integrin beta 1 and CAV1; TENE treatment ameliorated these alterations. (a–e) Multiplex immunofluorescence microscopy analysis of the EMT program and association with CAV1. Formaldehyde-fixed, paraffin-embedded (FFPE) kidney samples were labeled with epithelial markers for E-cadherin, alpha SMA and CAV1. An immunofluorescence analysis was performed by confocal microscopy. (d) The enlarged image of the inset shown in (c). The alpha SMA-positive damaged tubular cells were surrounded by alpha SMA-positive interstitial cells (f–j). Multiplex immunofluorescence was performed to analyze the crosstalk among DPP-4, integrin beta 1 and CAV1 in the BSA-injected diabetic mice. (i) The enlarged image of the inset shown in (h). DPP-4, integrin beta 1, and CAV1 were localized at the same location (likely the luminal side of the proximal tubule). The crosstalk occurred more frequently in the damaged tubular cells. Representative images from n = 7 in each group are shown. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunohistochemistry Detection of Mouse Cathepsin B by Immunohistochemistry View Larger

Detection of Mouse Cathepsin B by Immunohistochemistry BSA-injected diabetic mice exhibited high tubular levels of DPP-4, CAV1 and EMT program; TENE treatment ameliorated these alterations. Immunohistochemical analysis of (a–d) DPP-4, (e–h) CAV1, (i–l) snail and (m–p) AQP-1 from the BSA-injected control or diabetic mice with or without the TENE treatment. Scale bar, 50 μm. Representative images from n = 7 in each group are shown. Each group was analyzed with an unpaired two-tailed t-test. *P < 0.05, **P < 0.01. Data are presented as mean ± s.e.m (q–t). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Western Blot Detection of Mouse Cathepsin B by Western Blot View Larger

Detection of Mouse Cathepsin B by Western Blot TENE treatment suppressed the crosstalk among DPP-4, integrin beta 1 and CAV1 via inhibition of TGF-beta /smad3 signaling pathway in vitro. Duolink in situ analysis of (a-c) DPP-4/integrin beta 1, (d–f) DPP-4/CAV1 and (g–i) integrin beta 1/CAV1 in HK-2 cells with or without TGF-beta 1 (10 ng/ml) was performed by confocal microscopy (×1260). Scale bar: 50 μm in each panel. (j) Representative western blot analysis. As a densitometric analysis, each protein level was normalized with actin. n = 6 per group were analyzed. (k–n) Duolink in situ analysis of integrin beta 1/CAV1 in DPP-4 overexpressed HK-2 cells with or without TENE and SIS3. (o) Immunoprecipitation analysis revealed TGF-beta treatment increased crosstalk among DPP-4, integrin beta 1 (ITG beta 1) and CAV1. (p) Immunoprecipitation assay revealed TGF-beta neutralization suppressed crosstalk among DPP-4, integrin beta 1 and CAV1 induced by DPP-4 overexpression. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunohistochemistry Detection of Mouse Cathepsin B by Immunohistochemistry View Larger

Detection of Mouse Cathepsin B by Immunohistochemistry BSA-injected diabetic mice exhibited high tubular levels of DPP-4, CAV1 and EMT program; TENE treatment ameliorated these alterations. Immunohistochemical analysis of (a–d) DPP-4, (e–h) CAV1, (i–l) snail and (m–p) AQP-1 from the BSA-injected control or diabetic mice with or without the TENE treatment. Scale bar, 50 μm. Representative images from n = 7 in each group are shown. Each group was analyzed with an unpaired two-tailed t-test. *P < 0.05, **P < 0.01. Data are presented as mean ± s.e.m (q–t). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Western Blot Detection of Mouse Cathepsin B by Western Blot View Larger

Detection of Mouse Cathepsin B by Western Blot TENE treatment suppressed the crosstalk among DPP-4, integrin beta 1 and CAV1 via inhibition of TGF-beta /smad3 signaling pathway in vitro. Duolink in situ analysis of (a-c) DPP-4/integrin beta 1, (d–f) DPP-4/CAV1 and (g–i) integrin beta 1/CAV1 in HK-2 cells with or without TGF-beta 1 (10 ng/ml) was performed by confocal microscopy (×1260). Scale bar: 50 μm in each panel. (j) Representative western blot analysis. As a densitometric analysis, each protein level was normalized with actin. n = 6 per group were analyzed. (k–n) Duolink in situ analysis of integrin beta 1/CAV1 in DPP-4 overexpressed HK-2 cells with or without TENE and SIS3. (o) Immunoprecipitation analysis revealed TGF-beta treatment increased crosstalk among DPP-4, integrin beta 1 (ITG beta 1) and CAV1. (p) Immunoprecipitation assay revealed TGF-beta neutralization suppressed crosstalk among DPP-4, integrin beta 1 and CAV1 induced by DPP-4 overexpression. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Western Blot Detection of Mouse Cathepsin B by Western Blot View Larger

Detection of Mouse Cathepsin B by Western Blot TENE treatment suppressed the crosstalk among DPP-4, integrin beta 1 and CAV1 via inhibition of TGF-beta /smad3 signaling pathway in vitro. Duolink in situ analysis of (a-c) DPP-4/integrin beta 1, (d–f) DPP-4/CAV1 and (g–i) integrin beta 1/CAV1 in HK-2 cells with or without TGF-beta 1 (10 ng/ml) was performed by confocal microscopy (×1260). Scale bar: 50 μm in each panel. (j) Representative western blot analysis. As a densitometric analysis, each protein level was normalized with actin. n = 6 per group were analyzed. (k–n) Duolink in situ analysis of integrin beta 1/CAV1 in DPP-4 overexpressed HK-2 cells with or without TENE and SIS3. (o) Immunoprecipitation analysis revealed TGF-beta treatment increased crosstalk among DPP-4, integrin beta 1 (ITG beta 1) and CAV1. (p) Immunoprecipitation assay revealed TGF-beta neutralization suppressed crosstalk among DPP-4, integrin beta 1 and CAV1 induced by DPP-4 overexpression. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunohistochemistry Detection of Mouse Cathepsin B by Immunohistochemistry View Larger

Detection of Mouse Cathepsin B by Immunohistochemistry BSA-injected diabetic mice exhibited high tubular levels of DPP-4, CAV1 and EMT program; TENE treatment ameliorated these alterations. Immunohistochemical analysis of (a–d) DPP-4, (e–h) CAV1, (i–l) snail and (m–p) AQP-1 from the BSA-injected control or diabetic mice with or without the TENE treatment. Scale bar, 50 μm. Representative images from n = 7 in each group are shown. Each group was analyzed with an unpaired two-tailed t-test. *P < 0.05, **P < 0.01. Data are presented as mean ± s.e.m (q–t). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence EMT in BSA-induced damaged tubule was associated with increased levels of DPP-4, integrin beta 1 and CAV1; TENE treatment ameliorated these alterations. (a–e) Multiplex immunofluorescence microscopy analysis of the EMT program and association with CAV1. Formaldehyde-fixed, paraffin-embedded (FFPE) kidney samples were labeled with epithelial markers for E-cadherin, alpha SMA and CAV1. An immunofluorescence analysis was performed by confocal microscopy. (d) The enlarged image of the inset shown in (c). The alpha SMA-positive damaged tubular cells were surrounded by alpha SMA-positive interstitial cells (f–j). Multiplex immunofluorescence was performed to analyze the crosstalk among DPP-4, integrin beta 1 and CAV1 in the BSA-injected diabetic mice. (i) The enlarged image of the inset shown in (h). DPP-4, integrin beta 1, and CAV1 were localized at the same location (likely the luminal side of the proximal tubule). The crosstalk occurred more frequently in the damaged tubular cells. Representative images from n = 7 in each group are shown. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence EMT in BSA-induced damaged tubule was associated with increased levels of DPP-4, integrin beta 1 and CAV1; TENE treatment ameliorated these alterations. (a–e) Multiplex immunofluorescence microscopy analysis of the EMT program and association with CAV1. Formaldehyde-fixed, paraffin-embedded (FFPE) kidney samples were labeled with epithelial markers for E-cadherin, alpha SMA and CAV1. An immunofluorescence analysis was performed by confocal microscopy. (d) The enlarged image of the inset shown in (c). The alpha SMA-positive damaged tubular cells were surrounded by alpha SMA-positive interstitial cells (f–j). Multiplex immunofluorescence was performed to analyze the crosstalk among DPP-4, integrin beta 1 and CAV1 in the BSA-injected diabetic mice. (i) The enlarged image of the inset shown in (h). DPP-4, integrin beta 1, and CAV1 were localized at the same location (likely the luminal side of the proximal tubule). The crosstalk occurred more frequently in the damaged tubular cells. Representative images from n = 7 in each group are shown. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence Myc induces cathepsin L expression in beta-cells of pancreatic Islets.(A) Immunohistochemical analyses for CTS B, C, L or S expression (all in red) in combination with staining for the pan-leukocyte marker CD45 (green) in pancreatic islet tumors from the MycERTAM;Bcl-xL animals. Pancreata were harvested from the MycERTAM;Bcl-xL mice treated for 7 d with TAM (Myc-On, 7 days) or control vehicle in place of TAM (Myc-OFF). The islet area is indicated by dotted line. The asterisks indicate the area of tumor represented in the insets. The panels are representatives of at least three animals assayed at each data point, all immunohistochemical analyses were done in duplicate; eight randomized fields per analysis were examined. Scale bars, 100μm. (B) Immunohistochemical analysis for cathepsin L expression in beta-cells of pancreatic islets from MycERTAM;Bcl-xL animals identified by insulin expression. Pancreata were collected from the animals described above. Scale bars represent 25μm. The panels are representatives of three animals assayed at each data point, all immunohistochemical analyses were done in duplicate; ten randomized fields per analysis were examined. Image collected and cropped by CiteAb from the following open publication (https://dx.plos.org/10.1371/journal.pone.0120348), licensed under a CC-BY license. Not internally tested by R&D Systems.

Immunocytochemistry/ Immunofluorescence Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence View Larger

Detection of Mouse Cathepsin B by Immunocytochemistry/ Immunofluorescence Myc induces cathepsin L expression in beta-cells of pancreatic Islets.(A) Immunohistochemical analyses for CTS B, C, L or S expression (all in red) in combination with staining for the pan-leukocyte marker CD45 (green) in pancreatic islet tumors from the MycERTAM;Bcl-xL animals. Pancreata were harvested from the MycERTAM;Bcl-xL mice treated for 7 d with TAM (Myc-On, 7 days) or control vehicle in place of TAM (Myc-OFF). The islet area is indicated by dotted line. The asterisks indicate the area of tumor represented in the insets. The panels are representatives of at least three animals assayed at each data point, all immunohistochemical analyses were done in duplicate; eight randomized fields per analysis were examined. Scale bars, 100μm. (B) Immunohistochemical analysis for cathepsin L expression in beta-cells of pancreatic islets from MycERTAM;Bcl-xL animals identified by insulin expression. Pancreata were collected from the animals described above. Scale bars represent 25μm. The panels are representatives of three animals assayed at each data point, all immunohistochemical analyses were done in duplicate; ten randomized fields per analysis were examined. Image collected and cropped by CiteAb from the following open publication (https://dx.plos.org/10.1371/journal.pone.0120348), licensed under a CC-BY license. Not internally tested by R&D Systems.

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Background: Cathepsin B

Cathepsin B is the first described member of the family of lysosomal cysteine proteases (1). Cathepsin B possesses both endopeptidase and exopeptidase activities, in the latter case acting as a peptidyl-dipeptidase. It is known to process a number of proteins, including pro and active caspases, prorenin and secretory leucoprotease inhibitor (SLPI) (2‑4). Therefore, Cathepsin B may play a role in activation and inactivation of caspases, activation of renin and inactivation of SLPI, the key steps in apoptosis, angiotensin production, and progression of emphysema, respectively. Because of its increased levels and redistribution in human and animal tumors, Cathepsin B may also have a role in invasion and metastasis (5). In addition to the lysosome, Cathepsin B can be secreted or associated with plasma membrane, cytoplasm, and nucleus. It is synthesized as a preproenzyme. Following removal of the signal peptide, the inactive proenzyme undergoes further modifications including removal of the pro region to result in the active enzyme (5).

References
  1. Mort, J.S. (2004) in Handbook of Proteolytic Enzymes (Barrett, A.J. et al. eds.) p. 1079, Academic Press, San Diego.
  2. Vancompernolle, K. et al. (1998) FEBS Lett. 438:150.
  3. Jutras, I. and T.L. Reudelhuber (1998) FEBS Lett. 443:48.
  4. Taggart, C.C. et al. (2001) J. Biol. Chem. 276:33345.
  5. Berquin, I.M. and B.F. Sloane (1996) Adv. Exp. Med. Biol. 389:281.
Entrez Gene IDs
1508 (Human); 13030 (Mouse)
Alternate Names
APP secretase; APPS; Cathepsin B; Cathepsin B1; CPSBamyloid precursor protein secretase; CTSB; cysteine protease; EC 3.4.22; EC 3.4.22.1

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Citations for Mouse Cathepsin B 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.

21 Citations: Showing 1 - 10
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  1. Investigations on Primary Cilia of Nthy-ori 3-1 Cells upon Cysteine Cathepsin Inhibition or Thyrotropin Stimulation
    Authors: Do?ru, AG;Rehders, M;Brix, K;
    International journal of molecular sciences
    Species: Human
    Sample Types: Cell Lysates
    Applications: Western Blot
  2. TMEM106B regulates microglial proliferation and survival in response to demyelination
    Authors: Zhang, T;Pang, W;Feng, T;Guo, J;Wu, K;Nunez Santos, M;Arthanarisami, A;Nana, AL;Nguyen, Q;Kim, PJ;Jankowsky, JL;Seeley, WW;Hu, F;
    Science advances
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  3. Sphingomyelin 16:0 is a therapeutic target for neuronal death in acid sphingomyelinase deficiency
    Authors: Á Gaudioso, X Jiang, J Casas, EH Schuchman, MD Ledesma
    Cell Death & Disease, 2023-04-06;14(4):248.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: ICC
  4. Definition of the contribution of an Osteopontin-producing CD11c+ microglial subset to Alzheimer's disease
    Authors: Y Qiu, X Shen, O Ravid, D Atrakchi, D Rand, AE Wight, HJ Kim, S Liraz-Zalt, I Cooper, M Schnaider, H Cantor
    Proceedings of the National Academy of Sciences of the United States of America, 2023-02-02;120(6):e2218915120.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC
  5. Direct control of lysosomal catabolic activity by mTORC1 through regulation of V-ATPase assembly
    Authors: E Ratto, SR Chowdhury, NS Siefert, M Schneider, M Wittmann, D Helm, W Palm
    Nature Communications, 2022-08-17;13(1):4848.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  6. Epithelial-derived factors induce muscularis mucosa of human induced pluripotent stem cell-derived gastric organoids
    Authors: K Uehara, M Koyanagi-A, T Koide, T Itoh, T Aoi
    Stem Cell Reports, 2022-03-03;0(0):.
    Species: Mouse
    Sample Types: Tissue Homogenates
    Applications: Western Blot
  7. Cathepsin B and D deficiency in the mouse pancreas induces impaired autophagy and chronic pancreatitis
    Authors: H Iwama, S Mehanna, M Imasaka, S Hashidume, H Nishiura, KI Yamamura, C Suzuki, Y Uchiyama, E Hatano, M Ohmuraya
    Scientific Reports, 2021-03-23;11(1):6596.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC
  8. LRRK2 mediates tubulation and vesicle sorting from lysosomes
    Authors: L Bonet-Ponc, A Beilina, CD Williamson, E Lindberg, JH Kluss, S Saez-Atien, N Landeck, R Kumaran, A Mamais, CKE Bleck, Y Li, MR Cookson
    Sci Adv, 2020-11-11;6(46):.
    Species: Human
    Sample Types: Whole Cells
    Applications: ICC
  9. Network analysis of the progranulin-deficient mouse brain proteome reveals pathogenic mechanisms shared in human frontotemporal dementia caused by GRN mutations
    Authors: M Huang, E Modeste, E Dammer, P Merino, G Taylor, DM Duong, Q Deng, CJ Holler, M Gearing, D Dickson, NT Seyfried, T Kukar
    Acta Neuropathol Commun, 2020-10-07;8(1):163.
    Species: Mouse
    Sample Types: Protein
    Applications: Western Blot
  10. Spatiotemporal proteomics uncovers cathepsin-dependent macrophage cell death during Salmonella infection
    Authors: J Selkrig, N Li, A Hausmann, MSJ Mangan, M Zietek, A Mateus, J Bobonis, A Sueki, H Imamura, B El Debs, G Sigismondo, BI Florea, HS Overkleeft, N Kopitar-Je, B Turk, P Beltrao, MM Savitski, E Latz, WD Hardt, J Krijgsveld, A Typas
    Nat Microbiol, 2020-06-08;0(0):.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  11. Neuronal Soma-Derived Degradative Lysosomes Are Continuously Delivered to Distal Axons to Maintain Local Degradation Capacity
    Authors: T Farfel-Bec, JC Roney, XT Cheng, S Li, SR Cuddy, ZH Sheng
    Cell Rep, 2019-07-02;28(1):51-64.e4.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: ICC
  12. Cysteine-type cathepsins promote the effector phase of acute cutaneous delayed-type hypersensitivity reactions
    Authors: J Schwenck, A Maurer, B Fehrenbach, R Mehling, P Knopf, N Mucha, D Haupt, K Fuchs, CM Griessinge, D Bukala, J Holstein, M Schaller, IG Menendez, K Ghoreschi, L Quintanill, M Gütschow, S Laufer, T Reinheckel, M Röcken, H Kalbacher, BJ Pichler, M Kneilling
    Theranostics, 2019-05-31;9(13):3903-3917.
    Species: Mouse
    Sample Types: Tissue Lysates, Whole Cells
    Applications: Flow Cytometry, Western Blot
  13. Early lysosomal maturation deficits in microglia triggers enhanced lysosomal activity in other brain cells of progranulin knockout mice
    Authors: JK Götzl, AV Colombo, K Fellerer, A Reifschnei, G Werner, S Tahirovic, C Haass, A Capell
    Mol Neurodegener, 2018-09-04;13(1):48.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  14. Characterization of LAMP1-labeled nondegradative lysosomal and endocytic compartments in neurons
    Authors: XT Cheng, YX Xie, B Zhou, N Huang, T Farfel-Bec, ZH Sheng
    J. Cell Biol., 2018-04-25;0(0):.
    Species: Rat
    Sample Types: Cell Culture Supernates
    Applications: Western Blot
  15. Disruption of Small GTPase Rab7 Exacerbates the Severity of Acute Pancreatitis in Experimental Mouse Models
    Authors: K Takahashi, H Mashima, K Miura, D Maeda, A Goto, T Goto, GH Sun-Wada, Y Wada, H Ohnishi
    Sci Rep, 2017-06-06;7(1):2817.
    Species: Mouse
    Sample Types: Tissue Homogenates, Whole Tissue
    Applications: IHC, Western Blot
  16. Deficiency for the cysteine protease cathepsin L impairs Myc-induced tumorigenesis in a mouse model of pancreatic neuroendocrine cancer.
    Authors: Brindle N, Joyce J, Rostker F, Lawlor E, Swigart-Brown L, Evan G, Hanahan D, Shchors K
    PLoS ONE, 2015-04-30;10(4):e0120348.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC
  17. Lysosomal protein turnover contributes to the acquisition of TGFbeta-1 induced invasive properties of mammary cancer cells.
    Authors: Kern U, Wischnewski V, Biniossek M, Schilling O, Reinheckel T
    Mol Cancer, 2015-02-15;14(0):39.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  18. Eucommia ulmoides Oliver extract, aucubin, and geniposide enhance lysosomal activity to regulate ER stress and hepatic lipid accumulation.
    Authors: Lee, Hwa-Youn, Lee, Geum-Hwa, Lee, Mi-Rin, Kim, Hye-Kyun, Kim, Nan-youn, Kim, Seung-Hy, Lee, Yong-Chu, Kim, Hyung-Ry, Chae, Han-Jung
    PLoS ONE, 2013-12-11;8(12):e81349.
    Species: Rat
    Sample Types: Whole Cells
    Applications: ICC
  19. Inflammasome activation by altered proteostasis.
    Authors: Shin, Jin Na, Fattah, Elmoataz, Bhattacharya, Abhisek, Ko, Soyoung, Eissa, N Tony
    J Biol Chem, 2013-10-31;288(50):35886-95.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  20. Macrophages and cathepsin proteases blunt chemotherapeutic response in breast cancer.
    Authors: Shree T, Olson OC, Elie BT
    Genes Dev., 2011-12-01;25(23):2465-79.
    Species: Mouse
    Sample Types: Tissue Homogenates
    Applications: Western Blot
  21. Endocytosis provides a major alternative pathway for lysosomal biogenesis in kidney proximal tubular cells.
    Authors: Nielsen R, Courtoy PJ, Jacobsen C, Dom G, Lima WR, Jadot M, Willnow TE, Devuyst O, Christensen EI
    Proc. Natl. Acad. Sci. U.S.A., 2007-03-16;104(13):5407-12.
    Species: Mouse
    Sample Types: Serum
    Applications: Western Blot

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