antigen exemplary seq id nos description npc 1 npc Search Results


npc1 antibody / niemann pick c1  (NSJ Bioreagents)
N/A
Additional name(s) for this target protein: Niemann Pick type C1
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npc1/niemann-pick c1 protein antibody, rabbit pab, antigen affinity purified  (Sino Biological)
N/A
Produced in rabbits immunized with purified, recombinant Human NPC1/Niemann-Pick C1 protein (rh NPC1/Niemann-Pick C1 protein; Catalog#16499-H32H; NP_000262.2; Arg372-Phe622). NPC1/Niemann-Pick C1 protein specific IgG was purified by Human NPC1/Niemann-Pick C1 protein affinity chromatography.
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antigen exemplary seq id nos description npc 1 npc  (ATCC)
97
ATCC antigen exemplary seq id nos description npc 1 npc
Antigen Exemplary Seq Id Nos Description Npc 1 Npc, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/antigen+exemplary+seq+id+nos+description+npc+1+npc/Antigen/us11078245-657-2-16
Average 97 stars, based on 1 article reviews
antigen exemplary seq id nos description npc 1 npc - by Bioz Stars, 2026-09
97/100 stars
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npc1  (Novus Biologicals)
90
Novus Biologicals npc1
Figure 1 Effect of U18666A treatment and <t>NPC1</t> overexpres- sion on protein synthesis and secretion in Huh7 cells. (a) Immunoblotting of cell lysates (NPC1, green fluorescent protein [GFP] and actin) and medium (holo-ceruloplasmin [Cp] and albumin) from untreated, GFP-transfected (as an NPC1 overexpression negative control) or NPC1-transfected Huh7 cells. U18666A treatment decreased the secretion of holo-Cp but not albumin. In U18666A-treated cells, NPC1 overexpression increased the secretion of holo-Cp to the culture medium. Arrowhead indicates holo-Cp. (b) Quantita- tive analysis of secretion of holo-Cp. The value was expressed by the ratio of the density to that of untreated control cells.
Npc1, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/antigen+exemplary+seq+id+nos+description+npc+1+npc/Niemann-Pick+C1+Antibody/10__1111_slash_j__1872___034x__2011__00788__x-29-7-8
Average 90 stars, based on 1 article reviews
npc1 - by Bioz Stars, 2026-09
90/100 stars
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rabbit anti- npc1 polyclonal antibody  (Cusabio)
N/A
Rabbit anti-Human NPC1 Polyclonal Antibody
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npc1 antibody  (ProSci Incorporated)
N/A
Npc1 Antibody raised in Goat validated in E.
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niemann pick c1 antibody / npc1  (NSJ Bioreagents)
N/A
Niemann-Pick disease, type C1 (NPC1) is a membrane protein that mediates intracellular cholesterol trafficking in mammals. In humans it is encoded by the NPC1 gene (chromosome location 18q11). This gene encodes a large protein that
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npc1 antibody (oaeb00172)  (Aviva Systems)
N/A
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npc1l1 antibody  (biorbyt)
N/A
Goat polyclonal antibody to NPC1L1 Host Note: Goat Conjugation Note: Unconjugated Reactivity Note: Mouse, Rat Application Note: P-ELISA
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Image Search Results


Figure 1 Effect of U18666A treatment and NPC1 overexpres- sion on protein synthesis and secretion in Huh7 cells. (a) Immunoblotting of cell lysates (NPC1, green fluorescent protein [GFP] and actin) and medium (holo-ceruloplasmin [Cp] and albumin) from untreated, GFP-transfected (as an NPC1 overexpression negative control) or NPC1-transfected Huh7 cells. U18666A treatment decreased the secretion of holo-Cp but not albumin. In U18666A-treated cells, NPC1 overexpression increased the secretion of holo-Cp to the culture medium. Arrowhead indicates holo-Cp. (b) Quantita- tive analysis of secretion of holo-Cp. The value was expressed by the ratio of the density to that of untreated control cells.

Journal: Hepatology Research

Article Title: Copper incorporation into ceruloplasmin is regulated by Niemann–Pick C1 protein

doi: 10.1111/j.1872-034x.2011.00788.x

Figure Lengend Snippet: Figure 1 Effect of U18666A treatment and NPC1 overexpres- sion on protein synthesis and secretion in Huh7 cells. (a) Immunoblotting of cell lysates (NPC1, green fluorescent protein [GFP] and actin) and medium (holo-ceruloplasmin [Cp] and albumin) from untreated, GFP-transfected (as an NPC1 overexpression negative control) or NPC1-transfected Huh7 cells. U18666A treatment decreased the secretion of holo-Cp but not albumin. In U18666A-treated cells, NPC1 overexpression increased the secretion of holo-Cp to the culture medium. Arrowhead indicates holo-Cp. (b) Quantita- tive analysis of secretion of holo-Cp. The value was expressed by the ratio of the density to that of untreated control cells.

Article Snippet: Antibodies against the following antigens were used: NPC1 (Novus Biologicals, Littleton, CO, USA); Cp (Dako Japan, Kyoto, Japan); holo-Cp (NIPRO, Osaka, Japan); albumin (ICN Biomedicals, Costa Mesa, CA, USA); a-fetoprotein (AFP) (Dako Japan); GFP (Santa Cruz Biotechnology, Santa Cruz, CA, USA); actin (Sigma); p230 (BD Biosciences, San Jose, CA, USA); and lysosome-associated membrane protein (Lamp)2.34 The following were used as secondary antibodies: fluorescein isothiocyanate (FITC)-conjugated rabbit antimouse immunoglobulin (Dako Japan); tetramethylrhodamine isothiocyanate (TRITC)-conjugated rabbit antimouse © 2011 The Japan Society of Hepatology nloaded from https://onlinelibrary.w iley.com /doi/10.1111/j.1872-034X .2011.00788.x by U FSC - U niversidade Federal de Santa C atarina, W iley O nline L ibrary on [20/09/2024].

Techniques: Western Blot, Transfection, Over Expression, Negative Control, Control

Figure 2 (a–l) Confocal laser scanning microscopic images of Huh7 cells transfected with green fluorescent protein (GFP)-ATP7B (green). Cells were treated with or without U18666A for 24 h, and transfected with NPC1 to induce overexpression of NPC1. Cells were stained for p230 (red). GFP-ATP7B was not co-localized with p230 under any condition. Bar, 10 mm.

Journal: Hepatology Research

Article Title: Copper incorporation into ceruloplasmin is regulated by Niemann–Pick C1 protein

doi: 10.1111/j.1872-034x.2011.00788.x

Figure Lengend Snippet: Figure 2 (a–l) Confocal laser scanning microscopic images of Huh7 cells transfected with green fluorescent protein (GFP)-ATP7B (green). Cells were treated with or without U18666A for 24 h, and transfected with NPC1 to induce overexpression of NPC1. Cells were stained for p230 (red). GFP-ATP7B was not co-localized with p230 under any condition. Bar, 10 mm.

Article Snippet: Antibodies against the following antigens were used: NPC1 (Novus Biologicals, Littleton, CO, USA); Cp (Dako Japan, Kyoto, Japan); holo-Cp (NIPRO, Osaka, Japan); albumin (ICN Biomedicals, Costa Mesa, CA, USA); a-fetoprotein (AFP) (Dako Japan); GFP (Santa Cruz Biotechnology, Santa Cruz, CA, USA); actin (Sigma); p230 (BD Biosciences, San Jose, CA, USA); and lysosome-associated membrane protein (Lamp)2.34 The following were used as secondary antibodies: fluorescein isothiocyanate (FITC)-conjugated rabbit antimouse immunoglobulin (Dako Japan); tetramethylrhodamine isothiocyanate (TRITC)-conjugated rabbit antimouse © 2011 The Japan Society of Hepatology nloaded from https://onlinelibrary.w iley.com /doi/10.1111/j.1872-034X .2011.00788.x by U FSC - U niversidade Federal de Santa C atarina, W iley O nline L ibrary on [20/09/2024].

Techniques: Transfection, Over Expression, Staining

Figure 3 Confocal laser scanning microscopic images of Huh7 cells transfected with green fluorescent protein (GFP)-ATP7B (green). Cells were treated with or without U18666A for 24 h, and transfected with NPC1 to induce overexpression of NPC1. Cells were stained for lysosome-associated membrane protein (Lamp)2 (red). GFP-ATP7B was co-localized in part but not all with Lamp2 in cells without U18666A treatment (a–e). GFP-ATP7B was almost completely co-localized with Lamp2 after U18666A treatment (g–i). GFP-ATP7B was co-localized in part but not all with Lamp2 in U18666A-treated cells when NPC1 was overex- pressed (j–l). Arrowheads indicate GFP-ATP7B-negative and Lamp2-positive area. Bar, 10 mm.

Journal: Hepatology Research

Article Title: Copper incorporation into ceruloplasmin is regulated by Niemann–Pick C1 protein

doi: 10.1111/j.1872-034x.2011.00788.x

Figure Lengend Snippet: Figure 3 Confocal laser scanning microscopic images of Huh7 cells transfected with green fluorescent protein (GFP)-ATP7B (green). Cells were treated with or without U18666A for 24 h, and transfected with NPC1 to induce overexpression of NPC1. Cells were stained for lysosome-associated membrane protein (Lamp)2 (red). GFP-ATP7B was co-localized in part but not all with Lamp2 in cells without U18666A treatment (a–e). GFP-ATP7B was almost completely co-localized with Lamp2 after U18666A treatment (g–i). GFP-ATP7B was co-localized in part but not all with Lamp2 in U18666A-treated cells when NPC1 was overex- pressed (j–l). Arrowheads indicate GFP-ATP7B-negative and Lamp2-positive area. Bar, 10 mm.

Article Snippet: Antibodies against the following antigens were used: NPC1 (Novus Biologicals, Littleton, CO, USA); Cp (Dako Japan, Kyoto, Japan); holo-Cp (NIPRO, Osaka, Japan); albumin (ICN Biomedicals, Costa Mesa, CA, USA); a-fetoprotein (AFP) (Dako Japan); GFP (Santa Cruz Biotechnology, Santa Cruz, CA, USA); actin (Sigma); p230 (BD Biosciences, San Jose, CA, USA); and lysosome-associated membrane protein (Lamp)2.34 The following were used as secondary antibodies: fluorescein isothiocyanate (FITC)-conjugated rabbit antimouse immunoglobulin (Dako Japan); tetramethylrhodamine isothiocyanate (TRITC)-conjugated rabbit antimouse © 2011 The Japan Society of Hepatology nloaded from https://onlinelibrary.w iley.com /doi/10.1111/j.1872-034X .2011.00788.x by U FSC - U niversidade Federal de Santa C atarina, W iley O nline L ibrary on [20/09/2024].

Techniques: Transfection, Over Expression, Staining, Membrane

Figure 4 Hypothetical mechanism of copper metabolism in hepatocytes. U18666A induces the NPC phenotype by inhibiting the function of NPC1 or NPC1-related proteins. The NPC phenotype induces the formation of late endosome–lysosome hybrid organelles, and impairs the vesicular transport of MPR from the late endosome to TGN. If ATP7B were localized in the late endosomes, ATP7B would translocate copper into the late endosomes from the cytoplasm and then copper would be transported from the late endosomes to the TGN by the MPR recycling vesicles. The secretion of holo-Cp to the medium would be decreased by inducing the NPC phenotype. If ATP7B were localized in the TGN, the secretion of holo-Cp to the medium would not be affected by U18666A. ER, endoplasmic reticulum; ERGIC, ER–Golgi intermediate compartment; hCTR, human copper transporter; LE, late endosome; MPR, mannose 6-phosphate receptor; TGN, trans-Golgi network.

Journal: Hepatology Research

Article Title: Copper incorporation into ceruloplasmin is regulated by Niemann–Pick C1 protein

doi: 10.1111/j.1872-034x.2011.00788.x

Figure Lengend Snippet: Figure 4 Hypothetical mechanism of copper metabolism in hepatocytes. U18666A induces the NPC phenotype by inhibiting the function of NPC1 or NPC1-related proteins. The NPC phenotype induces the formation of late endosome–lysosome hybrid organelles, and impairs the vesicular transport of MPR from the late endosome to TGN. If ATP7B were localized in the late endosomes, ATP7B would translocate copper into the late endosomes from the cytoplasm and then copper would be transported from the late endosomes to the TGN by the MPR recycling vesicles. The secretion of holo-Cp to the medium would be decreased by inducing the NPC phenotype. If ATP7B were localized in the TGN, the secretion of holo-Cp to the medium would not be affected by U18666A. ER, endoplasmic reticulum; ERGIC, ER–Golgi intermediate compartment; hCTR, human copper transporter; LE, late endosome; MPR, mannose 6-phosphate receptor; TGN, trans-Golgi network.

Article Snippet: Antibodies against the following antigens were used: NPC1 (Novus Biologicals, Littleton, CO, USA); Cp (Dako Japan, Kyoto, Japan); holo-Cp (NIPRO, Osaka, Japan); albumin (ICN Biomedicals, Costa Mesa, CA, USA); a-fetoprotein (AFP) (Dako Japan); GFP (Santa Cruz Biotechnology, Santa Cruz, CA, USA); actin (Sigma); p230 (BD Biosciences, San Jose, CA, USA); and lysosome-associated membrane protein (Lamp)2.34 The following were used as secondary antibodies: fluorescein isothiocyanate (FITC)-conjugated rabbit antimouse immunoglobulin (Dako Japan); tetramethylrhodamine isothiocyanate (TRITC)-conjugated rabbit antimouse © 2011 The Japan Society of Hepatology nloaded from https://onlinelibrary.w iley.com /doi/10.1111/j.1872-034X .2011.00788.x by U FSC - U niversidade Federal de Santa C atarina, W iley O nline L ibrary on [20/09/2024].

Techniques: