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mouse na k atpase (Developmental Studies Hybridoma Bank)

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Developmental Studies Hybridoma Bank mouse na k atpase

Loss of dTau results in physiological defects in MT (A and B) DIC images showing lumen morphology. (C) Scatter dot plot showing mean (±SE) lumen width, categorized as wide or narrow types ( n = 10 pairs of MTs per genotype). (D) Salt sensitivity assay reared on food containing 0.5 M NaCl ( n = 300). (E and F) Immunostaining for Na + /K + <t>ATPase</t> (green) expression. (G and H) Rhodamine 123 efflux assay (green). All the MT images shown are from the wandering third-instar larvae. All scale bars represent 20 μm. All images are maximum intensity projections of all the sections. DAPI (magenta)-stained nuclei. Statistical analysis was done using unpaired t test, ∗∗ p < 0.01 and ∗∗∗∗ p < 0.0001. Error bars, mean ± SE. All images represent three or more independent biological replicates.

Mouse Na K Atpase, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+na+k+atpase/anti-ATPase/pmc12887266-5-0-3
Average 96 stars, based on 1 article reviews

mouse na k atpase - by Bioz Stars, 2026-09

96/100 stars

Images

1) Product Images from "Tau and Futsch play non-neuronal roles in mediating morphogenesis and function of Drosophila Malpighian tubules"

Article Title: Tau and Futsch play non-neuronal roles in mediating morphogenesis and function of Drosophila Malpighian tubules

Journal: iScience

doi: 10.1016/j.isci.2026.114737

Figure Legend Snippet: Loss of dTau results in physiological defects in MT (A and B) DIC images showing lumen morphology. (C) Scatter dot plot showing mean (±SE) lumen width, categorized as wide or narrow types ( n = 10 pairs of MTs per genotype). (D) Salt sensitivity assay reared on food containing 0.5 M NaCl ( n = 300). (E and F) Immunostaining for Na + /K + ATPase (green) expression. (G and H) Rhodamine 123 efflux assay (green). All the MT images shown are from the wandering third-instar larvae. All scale bars represent 20 μm. All images are maximum intensity projections of all the sections. DAPI (magenta)-stained nuclei. Statistical analysis was done using unpaired t test, ∗∗ p < 0.01 and ∗∗∗∗ p < 0.0001. Error bars, mean ± SE. All images represent three or more independent biological replicates.

Techniques Used: Sensitive Assay, Immunostaining, Expressing, Staining

Incubation:

Article Title: Functional profiling and visualization of the sphingolipid metabolic network in vivo
Article Snippet: .. The brains were permeabilized with 2% PBST for 30 min, then blocked in 0.25% PBST with 1% BSA for 1 h. Next, the samples were incubated with primary antibodies, rat anti-Elav (1:200, Rat-Elav-7E8A10, DSHB), mouse anti-Repo (1:200, 8D12 anti-Repo, DSHB), mouse anti-lamin (1:200, ADL67.10, DSHB), mouse anti-ATP5A (1:500, ab14748, Abcam), mouse anti-Cathepsin L (1:500, MAB22591, R and D Systems), mouse anti-Na + /K + -ATPase (1:200, a5, DSHB), rabbit anti-Ref2P (1:200, ab178440, abcam), mouse anti-DLG (1:200, 4F3 anti-discs large, DSHB), rabbit anti-GM130 (1:200, ab30637, Abcam), goat anti-Golgin245 (1:500, Golgin245, DSHB), mouse anti-Cnx99A (1:200, Cnx99A 6-2-1, DSHB), mouse anti-Golgin84 (1:200, Golgin84 12-1, DSHB), chicken anti-GFP (1:500, ab13970, Abcam), rabbit anti-Ifc (1:200, Jung et al, ) rabbit anti-Calnexin (1:200, ab75801, Abcam), rabbit anti-rab5 (1:200, ab31261, Abcam), diluted in 0.25% PBST with 1% BSA overnight at 4 °C, washed in 1% PBST four times for 30 min, and incubated in secondary antibody (1:500, 111-605-003, 715-545-150, 711-545-152, 112-545-167, 111-165-003, 115-605-166, Jackson ImmunoResearch Laboratories) diluted in 0.25% PBST with 1% BSA overnight at 4 °C. .. The brains were then washed with 1% PBST four times for 30 min and mounted in Vectashield (H-1000, Vector Laboratories) or RapiClear 1.47 (#RC147002, SunJin Lab) for subsequent confocal imaging.

Article Title: Functional profiling and visualization of the sphingolipid metabolic network in vivo.
Article Snippet: .. The brains were permeabilized with 2% PBST for 30 min, then blocked in 0.25% PBST with 1% BSA for 1 h. Next, the samples were incubated with primary antibodies, rat anti-Elav (1:200, Rat-Elav-7E8A10, DSHB), mouse anti-Repo (1:200, 8D12 anti-Repo, DSHB), mouse antilamin (1:200, ADL67.10, DSHB), mouse anti-ATP5A (1:500, ab14748, Abcam), mouse anti-Cathepsin L (1:500, MAB22591, R and D Systems), mouse anti-Na+/K+-ATPase (1:200, a5, DSHB), rabbit anti-Ref2P (1:200, ab178440, abcam), mouse anti-DLG (1:200, 4F3 anti-discs large, DSHB), rabbit anti-GM130 (1:200, ab30637, Abcam), goat anti-Golgin245 (1:500, Golgin245, DSHB), mouse anti-Cnx99A (1:200, Cnx99A 6-2-1, DSHB), mouse antiGolgin84 (1:200, Golgin84 12-1, DSHB), chicken anti-GFP (1:500, ab13970, Abcam), rabbit anti-Ifc (1:200, Jung et al, 2017) rabbit anti-Calnexin (1:200, ab75801, Abcam), rabbit anti-rab5 (1:200, ab31261, Abcam), diluted in 0.25% PBST with 1% BSA overnight at 4 °C, washed in 1% PBST four times for 30 min, and incubated in secondary antibody (1:500, 111-605-003, 715-545-150, 711-545- 152, 112-545-167, 111-165-003, 115-605-166, Jackson ImmunoResearch Laboratories) diluted in 0.25% PBST with 1% BSA overnight at 4 °C. .. The brains were then washed with 1% PBST four times for 30 min and mounted in Vectashield (H-1000, Vector Laboratories) or RapiClear 1.47 (#RC147002, SunJin Lab) for subsequent confocal imaging.

Article Title: Dihydroceramide desaturase modulates autolysosome maturation and ameliorates CRB1 retinopathy.
Article Snippet: Variants in the CRB1 gene cause retinal degeneration and subsequent vision impairment in patients of retinitis pigmentosa (RP).. No treatments are currently available to cure or impede the progression of CRB1-associated retinopathy.. Previous studies have revealed alterations in the endolysosomal systems and autophagy in the absence of CRB1, but their roles in the pathogenesis of CRB1 retinopathy are unclear.

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Mt2 expression markedly reduces Neo1 levels in Hep3B cells . A , diagram of Mt2 and fMt2. The MYC (m) and FLAG (f) epitopes were added to the C-terminus of Mt2. B , diagram of fNeo1. The MYC (m) and FLAG (f) epitopes were added to the C-terminus of Neo1. C , coexpression of fMt2 with fNeo1 markedly reduces fNeo1 levels in whole cell extracts (input) and on cell surface by biotinylation. AP, aprotinin. Experiments were repeated three times with consistent results. D , quantification of cell surface fNeo1 bands in C ( panel 4 ). The relative amounts to Na + K + ATPase ( panel-5 ) are presented (n = 3). The data shown are means ± SD. One-way ANOVA was used to analyze the data. ns, no statistical difference. ∗, p < 0.05; ∗∗∗∗, p < 0.0001. NEO1, neogenin.

Journal: The Journal of Biological Chemistry

Article Title: Matriptase-2-mediated suppression of hepatic hepcidin expression in mice requires hepatocyte neogenin

doi: 10.1016/j.jbc.2026.111142

Figure Lengend Snippet: Mt2 expression markedly reduces Neo1 levels in Hep3B cells . A , diagram of Mt2 and fMt2. The MYC (m) and FLAG (f) epitopes were added to the C-terminus of Mt2. B , diagram of fNeo1. The MYC (m) and FLAG (f) epitopes were added to the C-terminus of Neo1. C , coexpression of fMt2 with fNeo1 markedly reduces fNeo1 levels in whole cell extracts (input) and on cell surface by biotinylation. AP, aprotinin. Experiments were repeated three times with consistent results. D , quantification of cell surface fNeo1 bands in C ( panel 4 ). The relative amounts to Na + K + ATPase ( panel-5 ) are presented (n = 3). The data shown are means ± SD. One-way ANOVA was used to analyze the data. ns, no statistical difference. ∗, p < 0.05; ∗∗∗∗, p < 0.0001. NEO1, neogenin.

Article Snippet: The biotinylated proteins and ∼10% fraction of whole cell extracts were subjected to SDS-PAGE and immunodetection by using an HRP-coupled mouse anti-FLAG M2 IgG (Sigma) or by using rabbit anti-human NEO1 , mouse anti-Na + K + ATPase (Santa Cruz Biotechnology; sc-21712), mouse anti-β-actin (Sigma), and the corresponding secondary antibodies.

Techniques: Expressing

Journal: iScience

Article Title: Tau and Futsch play non-neuronal roles in mediating morphogenesis and function of Drosophila Malpighian tubules

doi: 10.1016/j.isci.2026.114737

Figure Lengend Snippet: Loss of dTau results in physiological defects in MT (A and B) DIC images showing lumen morphology. (C) Scatter dot plot showing mean (±SE) lumen width, categorized as wide or narrow types ( n = 10 pairs of MTs per genotype). (D) Salt sensitivity assay reared on food containing 0.5 M NaCl ( n = 300). (E and F) Immunostaining for Na + /K + ATPase (green) expression. (G and H) Rhodamine 123 efflux assay (green). All the MT images shown are from the wandering third-instar larvae. All scale bars represent 20 μm. All images are maximum intensity projections of all the sections. DAPI (magenta)-stained nuclei. Statistical analysis was done using unpaired t test, ∗∗ p < 0.01 and ∗∗∗∗ p < 0.0001. Error bars, mean ± SE. All images represent three or more independent biological replicates.

Article Snippet: Mouse-Na+/K+ ATPase , DSHB , Cat# a5 RRID: AB_ 2166869.

Techniques: Sensitive Assay, Immunostaining, Expressing, Staining

$( A ) Diagram of the transgene ( Catspere TG ) encoding a truncated CATSPERε ECD in mice. Shown is the domain organization of the mouse CATSPERε (UniProt: P0DP43 ) and CATSPERδ (UniProt: E9Q9F6 ). The transgene encodes the CATSPERδ-homologous region of CATSPERε fused to its native signal peptide and tags (~61 kDa), driven by the Clgn promoter for specific expression in testicular germ cells. ( B ) Topologies of the truncated (ε 723-985 ) and full-length (ε Full ) CATSPERε proteins. The truncated version retains only the canopy pole region. ( C ) Immunoblot of truncated CATSPERε in testis and sperm from Catspere TG+ ( TG+ ) mice. Proteins smaller than 50 kDa likely result from cleavage within the mCherry tag. Acetylated tubulin (AcTUB) serves as a loading control. ( D ) Immunoblot of truncated CATSPERε in cytosol and microsome fractions of testis from WT; TG+ males. Na + /K + ATPase and calmodulin (CaM) are controls for fraction and loading. Asterisks (*) indicate the roof-truncated CATSPERε proteins. ( E ) Confocal images of immunostained CATSPER1 and HA in sperm. Merged fluorescence and corresponding DIC images (right) show HA-immunostained sperm. ( F ) 3D SIM images of immunostained CATSPER1 in sperm. z -depth is color coded (left), and y - z projections show cross sections (right). ( G ) Coimmunoprecipitation of native CatSper subunits and truncated CATSPERε in WT, Catsperd -null ( d−/− ), and WT; Catspere TG ( TG+ ) testis. ( H ) Confocal images of truncated CATSPERε in developing spermatids. Shown are fluorescence (top) and merged DIC and DNA fluorescence images (bottom). WGA stains sugar residues, and Hoechst counterstains DNA (E and H). The truncated CATSPERε is probed by α-HA [(C), (D), (E), (G), and (H)]. See also fig. S3.$

Journal: Science Advances

Article Title: CATSPERε extracellular domains are essential for sperm calcium channel assembly and activity modulation

doi: 10.1126/sciadv.adw3414

Figure Lengend Snippet: ( A ) Diagram of the transgene ( Catspere TG ) encoding a truncated CATSPERε ECD in mice. Shown is the domain organization of the mouse CATSPERε (UniProt: P0DP43 ) and CATSPERδ (UniProt: E9Q9F6 ). The transgene encodes the CATSPERδ-homologous region of CATSPERε fused to its native signal peptide and tags (~61 kDa), driven by the Clgn promoter for specific expression in testicular germ cells. ( B ) Topologies of the truncated (ε 723-985 ) and full-length (ε Full ) CATSPERε proteins. The truncated version retains only the canopy pole region. ( C ) Immunoblot of truncated CATSPERε in testis and sperm from Catspere TG+ ( TG+ ) mice. Proteins smaller than 50 kDa likely result from cleavage within the mCherry tag. Acetylated tubulin (AcTUB) serves as a loading control. ( D ) Immunoblot of truncated CATSPERε in cytosol and microsome fractions of testis from WT; TG+ males. Na + /K + ATPase and calmodulin (CaM) are controls for fraction and loading. Asterisks (*) indicate the roof-truncated CATSPERε proteins. ( E ) Confocal images of immunostained CATSPER1 and HA in sperm. Merged fluorescence and corresponding DIC images (right) show HA-immunostained sperm. ( F ) 3D SIM images of immunostained CATSPER1 in sperm. z -depth is color coded (left), and y - z projections show cross sections (right). ( G ) Coimmunoprecipitation of native CatSper subunits and truncated CATSPERε in WT, Catsperd -null ( d−/− ), and WT; Catspere TG ( TG+ ) testis. ( H ) Confocal images of truncated CATSPERε in developing spermatids. Shown are fluorescence (top) and merged DIC and DNA fluorescence images (bottom). WGA stains sugar residues, and Hoechst counterstains DNA (E and H). The truncated CATSPERε is probed by α-HA [(C), (D), (E), (G), and (H)]. See also fig. S3.

Article Snippet: Mouse monoclonal anti-Na + /K + ATPase was from Santa Cruz Biotechnology (clone H-3, sc-48345).

Techniques: Expressing, Western Blot, Control, Fluorescence