Cathepsin B Antibody [Unconjugated]

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.

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.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//www.nature.com/articles/s41598-017-02988-3), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//www.nature.com/articles/s41598-017-02988-3), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//pubmed.ncbi.nlm.nih.gov/31101909), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//dx.plos.org/10.1371/journal.pone.0120348), licensed under a CC-BY license. Not internally tested by R&D Systems.

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 (//dx.plos.org/10.1371/journal.pone.0120348), licensed under a CC-BY license. Not internally tested by R&D Systems.

Evaluation of lysosomal activation in SWCNT-exposed cells. Panel a: Epi-fluorescence images of macrophages unexposed (upper line) or exposed (lower line) to 50 μg/ml SWCNT for 24 hours stained with Acridine Orange (for lysosomes, in red) and DAPI (RNA/DNA, in green). Merge: combination of Acridine Orange and DAPI staining (overlapping appeared yellow). Panel b: Cathepsin activity in macrophages exposed to SWCNT for 3 hours. *: p < 0.001 between groups. Panel c: Western Blot images of LAMP-1 (120 kDa) and Cathepsin B (37 kDa) expression in macrophages exposed for 24 hours to SWCNT. beta -Actin is given as internal standard. Panel d: quantification of LAMP-1 and Cathepsin B expression, normalized to beta -Actin expression. *: p < 0.05 between groups. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23800198), licensed under a CC-BY license. Not internally tested by R&D Systems.

• Reactivity: Mu
• Applications: WB, IHC, B/N
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Unconjugated
• Concentration: LYOPH

Cathepsin B Antibody [Unconjugated] Summary

• Immunogen: Mouse myeloma cell line NS0-derived recombinant mouse Cathepsin B
  His18-Phe339
  Accession # P10605
• 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: N/A
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Gene: CTSB
• Purity Statement: Antigen Affinity-purified

Applications/Dilutions

• Dilutions:
  • Immunohistochemistry 5-15 ug/mL
  • Neutralization 0.33 ug/mL
  • Western Blot 0.1 ug/mL

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 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.
• Buffer: 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.
• Preservative: No Preservative
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute at 0.2 mg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Cathepsin B Antibody [Unconjugated]

• APP secretase
• APPS
• Cathepsin B
• Cathepsin B1
• CPSBamyloid precursor protein secretase
• CTSB
• cysteine protease
• EC 3.4.22
• EC 3.4.22.1

Background

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).

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.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for Cathepsin B Antibody (AF965)(53)

Publications using AF965

• Makar, AN;Boraman, A;Mosen, P;Simpson, JE;Marques, J;Michelberger, T;Aitken, S;Wheeler, AP;Winter, D;von Kriegsheim, A;Gammoh, N; The V-ATPase complex component RNAseK is required for lysosomal hydrolase delivery and autophagosome degradation Nature communications 2024-09-05 [PMID: 39231962] (Western Blot, Mouse)
• Takahashi, H;Bhagwagar, S;Nies, SH;Ye, H;Han, X;Chiasseu, MT;Wang, G;Mackenzie, IR;Strittmatter, SM; Reduced progranulin increases tau and ?-synuclein inclusions and alters mouse tauopathy phenotypes via glucocerebrosidase Nature communications 2024-02-16 [PMID: 38365772] (Western Blot, Mouse)
• Do?ru, AG;Rehders, M;Brix, K; Investigations on Primary Cilia of Nthy-ori 3-1 Cells upon Cysteine Cathepsin Inhibition or Thyrotropin Stimulation International journal of molecular sciences 2023-05-26 [PMID: 37298246] (Western Blot, Human)
• 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; TMEM106B regulates microglial proliferation and survival in response to demyelination Science advances 2023-05-05 [PMID: 37146150] (Western Blot, Mouse)
• Jennifer Hua, Elvira Garcia de Paco, Nathalie Linck, Tangui Maurice, Catherine Desrumaux, Bénédicte Manoury et al. Microglial P2X4 receptors promote ApoE degradation and contribute to memory deficits in Alzheimer’s disease Cellular and Molecular Life Sciences 5/5/2023 [PMID: 37145189]
• Xinyu Zhu, Sanjana Surya Prakash, Geoffrey McAuliffe, Ping-Yue Pan Synaptojanin1 Modifies Endolysosomal Parameters in Cultured Ventral Midbrain Neurons eNeuro 4/18/2023 [PMID: 37072173]
• Á Gaudioso, X Jiang, J Casas, EH Schuchman, MD Ledesma Sphingomyelin 16:0 is a therapeutic target for neuronal death in acid sphingomyelinase deficiency Cell Death & Disease, 2023-04-06;14(4):248. 2023-04-06 [PMID: 37024473] (ICC, Mouse)
• Y Qiu, X Shen, O Ravid, D Atrakchi, D Rand, AE Wight, HJ Kim, S Liraz-Zalt, I Cooper, M Schnaider, H Cantor Definition of the contribution of an Osteopontin-producing CD11c+ microglial subset to Alzheimer&#039;s disease Proceedings of the National Academy of Sciences of the United States of America, 2023-02-02;120(6):e2218915120. 2023-02-02 [PMID: 36730200] (IHC, Mouse)
• Parchure A, Tian M, Stalder D et al. Liquid-liquid phase separation facilitates the biogenesis of secretory storage granules The Journal of cell biology 12/5/2022 [PMID: 36173346]
• Parchure A, Tian M, Stalder D et al. Liquid-liquid phase separation facilitates the biogenesis of secretory storage granules The Journal of cell biology 2022-12-05 [PMID: 36173346]
• E Ratto, SR Chowdhury, NS Siefert, M Schneider, M Wittmann, D Helm, W Palm Direct control of lysosomal catabolic activity by mTORC1 through regulation of V-ATPase assembly Nature Communications, 2022-08-17;13(1):4848. 2022-08-17 [PMID: 35977928] (Western Blot, Mouse)
• T Feng, L Luan, II Katz, M Ullah, VM Van Deerli, JQ Trojanowsk, EB Lee, F Hu TMEM106B deficiency impairs cerebellar myelination and synaptic integrity with Purkinje cell loss Acta neuropathologica communications, 2022-03-14;10(1):33. 3/14/2022 [PMID: 35287730]
• K Uehara, M Koyanagi-A, T Koide, T Itoh, T Aoi Epithelial-derived factors induce muscularis mucosa of human induced pluripotent stem cell-derived gastric organoids Stem Cell Reports, 2022-03-03;0(0):. 2022-03-03 [PMID: 35245440] (Western Blot, Mouse)
• Jiandong Sun, Yan Liu, Xiaoning Hao, Weiju Lin, Wenyue Su, Emerald Chiang et al. LAMTOR1 inhibition of TRPML1‐dependent lysosomal calcium release regulates dendritic lysosome trafficking and hippocampal neuronal function The EMBO Journal 3/1/2022 [PMID: 35099830]
• TT Dang, SH Back Translation Inhibitors Activate Autophagy Master Regulators TFEB and TFE3 International Journal of Molecular Sciences, 2021-11-08;22(21):. 11/8/2021 [PMID: 34769510]
• Torres JLN, Shanahan SL, Chassefeyre R, Bueno SL LC3B phosphorylation regulates FYCO1 binding and directional transport of autophagosomes Curr Biol 6/19/2021 [PMID: 34146484]
• Du H, Wong MY, Zhang T et al. A multifaceted role of progranulin in regulating amyloid-beta dynamics and responses Life science alliance 7/1/2021 [PMID: 34103390]
• Roney JC, Li S, Farfel-Becker T et al. Lipid-mediated motor-adaptor sequestration impairs axonal lysosome delivery leading to autophagic stress and dystrophy in Niemann-Pick type C Developmental cell 4/13/2021 [PMID: 33878344]
• H Iwama, S Mehanna, M Imasaka, S Hashidume, H Nishiura, KI Yamamura, C Suzuki, Y Uchiyama, E Hatano, M Ohmuraya Cathepsin B and D deficiency in the mouse pancreas induces impaired autophagy and chronic pancreatitis Scientific Reports, 2021-03-23;11(1):6596. 2021-03-23 [PMID: 33758261] (IHC, Mouse)
• Yasuhiko Bando, Nobuko Tokuda, Yudai Ogasawara, Go Onozawa, Arata Nagasaka, Koji Sakiyama et al. Expression and enhancement of FABP4 in septoclasts of the growth plate in FABP5-deficient mouse tibiae Histochemistry and Cell Biology 4/1/2021 [PMID: 33398436]
• 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 LRRK2 mediates tubulation and vesicle sorting from lysosomes Sci Adv, 2020-11-11;6(46):. 2020-11-11 [PMID: 33177079] (ICC, Human)
• M Huang, E Modeste, E Dammer, P Merino, G Taylor, DM Duong, Q Deng, CJ Holler, M Gearing, D Dickson, NT Seyfried, T Kukar Network analysis of the progranulin-deficient mouse brain proteome reveals pathogenic mechanisms shared in human frontotemporal dementia caused by GRN mutations Acta Neuropathol Commun, 2020-10-07;8(1):163. 2020-10-07 [PMID: 33028409] (Western Blot, Mouse)
• Georg Werner, Markus Damme, Martin Schludi, Johannes Gnörich, Karin Wind, Katrin Fellerer et al. Loss of TMEM 106B potentiates lysosomal and FTLD ‐like pathology in progranulin‐deficient mice EMBO reports 10/5/2020 [PMID: 32929860]
• Zhang J, Velmeshev D, Hashimoto K et al. Neurotoxic microglia promote TDP-43 proteinopathy in progranulin deficiency Nature 12/17/2020 [PMID: 32866962]
• Zhang J, Velmeshev D, Hashimoto K et al. Neurotoxic microglia promote TDP-43 proteinopathy in progranulin deficiency Nature 2020-12-17 [PMID: 32866962]
• Feng T, Mai S, Roscoe JM et al. Loss of TMEM106B and PGRN leads to severe lysosomal abnormalities and neurodegeneration in mice EMBO Rep. 8/10/2020 [PMID: 32852886]
• Panos G. Ziros, Cédric O. Renaud, Dionysios V. Chartoumpekis, Massimo Bongiovanni, Ioannis G. Habeos, Xiao-Hui Liao et al. Mice Hypomorphic for Keap1, a Negative Regulator of the Nrf2 Antioxidant Response, Show Age-Dependent Diffuse Goiter with Elevated Thyrotropin Levels Thyroid 2021-01-01 [PMID: 32689903] (Western Blot, Transgenic Mouse)
• Panos G. Ziros, Cédric O. Renaud, Dionysios V. Chartoumpekis, Massimo Bongiovanni, Ioannis G. Habeos, Xiao-Hui Liao et al. Mice Hypomorphic for Keap1, a Negative Regulator of the Nrf2 Antioxidant Response, Show Age-Dependent Diffuse Goiter with Elevated Thyrotropin Levels Thyroid 1/1/2021 [PMID: 32689903]
• 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 Spatiotemporal proteomics uncovers cathepsin-dependent macrophage cell death during Salmonella infection Nat Microbiol, 2020-06-08;0(0):. 2020-06-08 [PMID: 32514074] (Western Blot, Mouse)
• Cui W, Sathyanarayan A, Lopresti M et al. Lipophagy-derived fatty acids undergo extracellular efflux via lysosomal exocytosis Autophagy 2/19/2020 [PMID: 32070194]
• 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 Cysteine-type cathepsins promote the effector phase of acute cutaneous delayed-type hypersensitivity reactions Theranostics, 2019-05-31;9(13):3903-3917. 2019-05-31 [PMID: 31281521] (Flow Cytometry, Western Blot, Mouse)
• T Farfel-Bec, JC Roney, XT Cheng, S Li, SR Cuddy, ZH Sheng Neuronal Soma-Derived Degradative Lysosomes Are Continuously Delivered to Distal Axons to Maintain Local Degradation Capacity Cell Rep, 2019-07-02;28(1):51-64.e4. 2019-07-02 [PMID: 31269450] (ICC, Mouse)
• Y Takagaki, S Shi, M Katoh, M Kitada, K Kanasaki, D Koya Dipeptidyl peptidase-4 plays a pathogenic role in BSA-induced kidney injury in diabetic mice Sci Rep, 2019-05-17;9(1):7519. 5/17/2019 [PMID: 31101909]
• Enrique Gabandé‐Rodríguez, Azucena Pérez‐Cañamás, Beatriz Soto‐Huelin, Daniel N Mitroi, Sara Sánchez‐Redondo, Elena Martínez‐Sáez et al. Lipid‐induced lysosomal damage after demyelination corrupts microglia protective function in lysosomal storage disorders The EMBO Journal 1/15/2019 [PMID: 30530526]
• JK Götzl, AV Colombo, K Fellerer, A Reifschnei, G Werner, S Tahirovic, C Haass, A Capell Early lysosomal maturation deficits in microglia triggers enhanced lysosomal activity in other brain cells of progranulin knockout mice Mol Neurodegener, 2018-09-04;13(1):48. 2018-09-04 [PMID: 30180904] (Western Blot, Mouse)
• Chan Choo Yap, Laura Digilio, Lloyd P. McMahon, A. Denise R. Garcia, Bettina Winckler Degradation of dendritic cargos requires Rab7-dependent transport to somatic lysosomes Journal of Cell Biology 9/3/2018 [PMID: 29907658]
• XT Cheng, YX Xie, B Zhou, N Huang, T Farfel-Bec, ZH Sheng Characterization of LAMP1-labeled nondegradative lysosomal and endocytic compartments in neurons J. Cell Biol., 2018-04-25;0(0):. 2018-04-25 [PMID: 29695488] (Western Blot, Rat)
• Rakshamani Tripathi, Leann S. Fiore, Dana L. Richards, Yuchen Yang, Jinpeng Liu, Chi Wang et al. Abl and Arg mediate cysteine cathepsin secretion to facilitate melanoma invasion and metastasis Science Signaling 2/22/2018 [PMID: 29463776]
• B Lloyd-Lewi, CC Krueger, TJ Sargeant, ME D'Angelo, MJ Deery, R Feret, JA Howard, KS Lilley, CJ Watson Stat3 mediated alterations in lysosomal membrane protein composition J. Biol. Chem., 2018-01-17;0(0):. 1/17/2018 [PMID: 29343516]
• Zoe A. Klein, Hideyuki Takahashi, Mengxiao Ma, Massimiliano Stagi, Melissa Zhou, TuKiet T. Lam et al. Loss of TMEM106B Ameliorates Lysosomal and Frontotemporal Dementia-Related Phenotypes in Progranulin-Deficient Mice Neuron 7/19/2017 [PMID: 28728022]
• K Takahashi, H Mashima, K Miura, D Maeda, A Goto, T Goto, GH Sun-Wada, Y Wada, H Ohnishi Disruption of Small GTPase Rab7 Exacerbates the Severity of Acute Pancreatitis in Experimental Mouse Models Sci Rep, 2017-06-06;7(1):2817. 2017-06-06 [PMID: 28588238] (IHC, Western Blot, Mouse)
• Yasuhiko Bando, Miyuki Yamamoto, Koji Sakiyama, Hide Sakashita, Fuyoko Taira, Genki Miyake et al. Retinoic acid regulates cell-shape and -death of E-FABP (FABP5)-immunoreactive septoclasts in the growth plate cartilage of mice Histochemistry and Cell Biology 9/1/2017 [PMID: 28500502]
• Yasuhiko Bando, Miyuki Yamamoto, Koji Sakiyama, Hide Sakashita, Fuyoko Taira, Genki Miyake et al. Retinoic acid regulates cell-shape and -death of E-FABP (FABP5)-immunoreactive septoclasts in the growth plate cartilage of mice Histochemistry and Cell Biology 2017-09-01 [PMID: 28500502] (Immunohistochemistry, Mouse)
• Cathepsin B modulates lysosomal biogenesis and host defense against Francisella novicida infection J Exp Med, 2016-08-22;0(0):. 8/22/2016 [PMID: 27551156]
• Brindle N, Joyce J, Rostker F, Lawlor E, Swigart-Brown L, Evan G, Hanahan D, Shchors K Deficiency for the cysteine protease cathepsin L impairs Myc-induced tumorigenesis in a mouse model of pancreatic neuroendocrine cancer. PLoS ONE, 2015-04-30;10(4):e0120348. 2015-04-30 [PMID: 25927437] (IHC, Mouse)
• Kern U, Wischnewski V, Biniossek M, Schilling O, Reinheckel T Lysosomal protein turnover contributes to the acquisition of TGFbeta-1 induced invasive properties of mammary cancer cells. Mol Cancer, 2015-02-15;14(0):39. 2015-02-15 [PMID: 25744631] (Western Blot, Mouse)
• 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 Eucommia ulmoides Oliver extract, aucubin, and geniposide enhance lysosomal activity to regulate ER stress and hepatic lipid accumulation. PLoS ONE, 2013-12-11;8(12):e81349. 2013-12-11 [PMID: 24349058] (ICC, Rat)
• Shin , Jin Na, Fattah , Elmoataz, Bhattacharya , Abhisek, Ko , Soyoung, Eissa , N Tony Inflammasome activation by altered proteostasis. J Biol Chem, 2013-10-31;288(50):35886-95. 2013-10-31 [PMID: 24178293] (Western Blot, Mouse)
• Cyrill Bussy, Erwan Paineau, Julien Cambedouzou, Nathalie Brun, Claudie Mory, Barbara Fayard et al. Intracellular fate of carbon nanotubes inside murine macrophages: pH-dependent detachment of iron catalyst nanoparticles Particle and Fibre Toxicology 12/1/2013 [PMID: 23800198]
• K Shchors, H Nozawa, J Xu, F Rostker, L Swigart-Brown, G Evan et al. Increased invasiveness of MMP-9-deficient tumors in two mouse models of neuroendocrine tumorigenesis Oncogene 1/24/2013 [PMID: 22391572]
• Shree T, Olson OC, Elie BT Macrophages and cathepsin proteases blunt chemotherapeutic response in breast cancer. Genes Dev., 2011-12-01;25(23):2465-79. 2011-12-01 [PMID: 22156207] (Western Blot, Mouse)
• Margot G. Paulick, Matthew Bogyo Development of Activity-Based Probes for Cathepsin X ACS Chemical Biology 6/17/2011 [PMID: 21322635]
• Nielsen R, Courtoy PJ, Jacobsen C, Dom G, Lima WR, Jadot M, Willnow TE, Devuyst O, Christensen EI Endocytosis provides a major alternative pathway for lysosomal biogenesis in kidney proximal tubular cells. Proc. Natl. Acad. Sci. U.S.A., 2007-03-16;104(13):5407-12. 2007-03-16 [PMID: 17369355] (Western Blot, Mouse)

Review for Cathepsin B Antibody (AF965) (1)

Average Rating: 5

(Based on 1 review)

We have 1 review tested in 1 species: Mouse.

reviewed by: Verified Customer IHC-P Mouse 12/19/2014

Summary

• Application: Immunohistochemistry-Paraffin
• Sample Tested: Kidney paraffin section
• Species: Mouse

Bioinformatics

• Gene Symbol: CTSB
• Uniprot:
  • P10605()