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anti phb2 mouse monoclonal antibody (Santa Cruz Biotechnology)

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Santa Cruz Biotechnology anti phb2 mouse monoclonal antibody
$Characterization of NcGA7-binding proteins. (A) Silver staining for SDS–PAGE to identify NcGRA7-binding proteins by an anti-FLAG immunoprecipitation assay using 293T cells transfected with empty plasmid (Mock, Lanes 1 and 2) or NcGRA7 cDNA fused with a FLAG tag (Lanes 3 and 4). Enriched or exclusively detected proteins are shown as five bands, while the other three bands (#1, #2 and #3) were excluded from the MS analyses. M: molecular marker. Each experiment (biological replicate) was repeated two times. (B, C) Western blots of the fractions eluted from the anti-FLAG immunoprecipitate were analyzed by immunoblotting using antibodies against FLAG (B) , XPOT, XPO1, SLC25A13, DNAJA1, UQCRC2, PHB1, and <t>PHB2</t> (C) . 293T cells transfected with empty plasmid (E) or NcGRA7 cDNA fused with a FLAG tag (G7) at 20 h posttransfection and HFFs infected with the parental strain Nc1 of N. caninum (WT) and NcGRA7-complemented (7c) parasites at 40 h postinfection were used. Each experiment (similar biological replicate) was repeated two time (B, C) .$
Anti Phb2 Mouse Monoclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti phb2 mouse monoclonal antibody/product/Santa Cruz Biotechnology
Average 95 stars, based on 60 article reviews

anti phb2 mouse monoclonal antibody - by Bioz Stars, 2026-05

95/100 stars

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1) Product Images from "Mitochondrial damage and IL-1β production in monocytes caused by Neospora caninum infection are mediated by dense granule protein 7 and prohibitins"

Article Title: Mitochondrial damage and IL-1β production in monocytes caused by Neospora caninum infection are mediated by dense granule protein 7 and prohibitins

Journal: Frontiers in Immunology

doi: 10.3389/fimmu.2025.1408992

$Characterization of NcGA7-binding proteins. (A) Silver staining for SDS–PAGE to identify NcGRA7-binding proteins by an anti-FLAG immunoprecipitation assay using 293T cells transfected with empty plasmid (Mock, Lanes 1 and 2) or NcGRA7 cDNA fused with a FLAG tag (Lanes 3 and 4). Enriched or exclusively detected proteins are shown as five bands, while the other three bands (#1, #2 and #3) were excluded from the MS analyses. M: molecular marker. Each experiment (biological replicate) was repeated two times. (B, C) Western blots of the fractions eluted from the anti-FLAG immunoprecipitate were analyzed by immunoblotting using antibodies against FLAG (B) , XPOT, XPO1, SLC25A13, DNAJA1, UQCRC2, PHB1, and PHB2 (C) . 293T cells transfected with empty plasmid (E) or NcGRA7 cDNA fused with a FLAG tag (G7) at 20 h posttransfection and HFFs infected with the parental strain Nc1 of N. caninum (WT) and NcGRA7-complemented (7c) parasites at 40 h postinfection were used. Each experiment (similar biological replicate) was repeated two time (B, C) .$
Figure Legend Snippet: Characterization of NcGA7-binding proteins. (A) Silver staining for SDS–PAGE to identify NcGRA7-binding proteins by an anti-FLAG immunoprecipitation assay using 293T cells transfected with empty plasmid (Mock, Lanes 1 and 2) or NcGRA7 cDNA fused with a FLAG tag (Lanes 3 and 4). Enriched or exclusively detected proteins are shown as five bands, while the other three bands (#1, #2 and #3) were excluded from the MS analyses. M: molecular marker. Each experiment (biological replicate) was repeated two times. (B, C) Western blots of the fractions eluted from the anti-FLAG immunoprecipitate were analyzed by immunoblotting using antibodies against FLAG (B) , XPOT, XPO1, SLC25A13, DNAJA1, UQCRC2, PHB1, and PHB2 (C) . 293T cells transfected with empty plasmid (E) or NcGRA7 cDNA fused with a FLAG tag (G7) at 20 h posttransfection and HFFs infected with the parental strain Nc1 of N. caninum (WT) and NcGRA7-complemented (7c) parasites at 40 h postinfection were used. Each experiment (similar biological replicate) was repeated two time (B, C) .

Techniques Used: Binding Assay, Silver Staining, SDS Page, Immunoprecipitation, Transfection, Plasmid Preparation, FLAG-tag, Marker, Western Blot, Infection

$Localization of NcGRA7 in host mitochondria and binding to host mitochondrial proteins. (A) Schematic diagram of isolated mitochondria under isotonic and swelling conditions. Schematics of the isotonic (left) and swelling (right) conditions used in this study. Under isotonic conditions, proteinase K can access outer mitochondrial membrane (OMM) proteins but not the intermembrane space (IMS), inner mitochondrial membrane (IMM), or matrix proteins through membrane barriers. In addition, under swelling conditions, the protease can reach the IMS, followed by cleavage of both the OMM and IMS proteins. The inset shows mitochondrial proteins as markers for each category. (B) The mitochondrial fraction (Mt) isolated from HFFs was treated with proteinase K under isotonic (–) or hypotonic swelling (+) conditions. The reactants were developed by immunoblotting with antibodies against NcGRA7 or against several mitochondrial markers as indicated. OMM protein: Mfn1. IMS proteins: AIF, PHB1 and PHB2. IMM protein: COX IV. Matrix protein: mHsp70. Each experiment (biological replicate) was repeated two times. (C) Western blot of eluted fractions of HFFs infected with the parental strain Nc1 of N. caninum (WT) or NcGRA7-complemented parasites (7c) at 40 h post infection from anti-FLAG immunoprecipitation were analyzed by immunoblotting using antibodies against several mitochondrial markers as indicated. *Because mouse antibodies against FLAG, AIF and mHsp70 were used, the anti-mouse HRP secondary antibody was used to detect the anti-FLAG mouse antibody.$
Figure Legend Snippet: Localization of NcGRA7 in host mitochondria and binding to host mitochondrial proteins. (A) Schematic diagram of isolated mitochondria under isotonic and swelling conditions. Schematics of the isotonic (left) and swelling (right) conditions used in this study. Under isotonic conditions, proteinase K can access outer mitochondrial membrane (OMM) proteins but not the intermembrane space (IMS), inner mitochondrial membrane (IMM), or matrix proteins through membrane barriers. In addition, under swelling conditions, the protease can reach the IMS, followed by cleavage of both the OMM and IMS proteins. The inset shows mitochondrial proteins as markers for each category. (B) The mitochondrial fraction (Mt) isolated from HFFs was treated with proteinase K under isotonic (–) or hypotonic swelling (+) conditions. The reactants were developed by immunoblotting with antibodies against NcGRA7 or against several mitochondrial markers as indicated. OMM protein: Mfn1. IMS proteins: AIF, PHB1 and PHB2. IMM protein: COX IV. Matrix protein: mHsp70. Each experiment (biological replicate) was repeated two times. (C) Western blot of eluted fractions of HFFs infected with the parental strain Nc1 of N. caninum (WT) or NcGRA7-complemented parasites (7c) at 40 h post infection from anti-FLAG immunoprecipitation were analyzed by immunoblotting using antibodies against several mitochondrial markers as indicated. *Because mouse antibodies against FLAG, AIF and mHsp70 were used, the anti-mouse HRP secondary antibody was used to detect the anti-FLAG mouse antibody.

Techniques Used: Binding Assay, Isolation, Membrane, Western Blot, Infection, Immunoprecipitation

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anti phb2 mouse monoclonal antibody (Santa Cruz Biotechnology)

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$Characterization of NcGA7-binding proteins. (A) Silver staining for SDS–PAGE to identify NcGRA7-binding proteins by an anti-FLAG immunoprecipitation assay using 293T cells transfected with empty plasmid (Mock, Lanes 1 and 2) or NcGRA7 cDNA fused with a FLAG tag (Lanes 3 and 4). Enriched or exclusively detected proteins are shown as five bands, while the other three bands (#1, #2 and #3) were excluded from the MS analyses. M: molecular marker. Each experiment (biological replicate) was repeated two times. (B, C) Western blots of the fractions eluted from the anti-FLAG immunoprecipitate were analyzed by immunoblotting using antibodies against FLAG (B) , XPOT, XPO1, SLC25A13, DNAJA1, UQCRC2, PHB1, and <t>PHB2</t> (C) . 293T cells transfected with empty plasmid (E) or NcGRA7 cDNA fused with a FLAG tag (G7) at 20 h posttransfection and HFFs infected with the parental strain Nc1 of N. caninum (WT) and NcGRA7-complemented (7c) parasites at 40 h postinfection were used. Each experiment (similar biological replicate) was repeated two time (B, C) .$
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$Characterization of NcGA7-binding proteins. (A) Silver staining for SDS–PAGE to identify NcGRA7-binding proteins by an anti-FLAG immunoprecipitation assay using 293T cells transfected with empty plasmid (Mock, Lanes 1 and 2) or NcGRA7 cDNA fused with a FLAG tag (Lanes 3 and 4). Enriched or exclusively detected proteins are shown as five bands, while the other three bands (#1, #2 and #3) were excluded from the MS analyses. M: molecular marker. Each experiment (biological replicate) was repeated two times. (B, C) Western blots of the fractions eluted from the anti-FLAG immunoprecipitate were analyzed by immunoblotting using antibodies against FLAG (B) , XPOT, XPO1, SLC25A13, DNAJA1, UQCRC2, PHB1, and <t>PHB2</t> (C) . 293T cells transfected with empty plasmid (E) or NcGRA7 cDNA fused with a FLAG tag (G7) at 20 h posttransfection and HFFs infected with the parental strain Nc1 of N. caninum (WT) and NcGRA7-complemented (7c) parasites at 40 h postinfection were used. Each experiment (similar biological replicate) was repeated two time (B, C) .$
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$Characterization of NcGA7-binding proteins. (A) Silver staining for SDS–PAGE to identify NcGRA7-binding proteins by an anti-FLAG immunoprecipitation assay using 293T cells transfected with empty plasmid (Mock, Lanes 1 and 2) or NcGRA7 cDNA fused with a FLAG tag (Lanes 3 and 4). Enriched or exclusively detected proteins are shown as five bands, while the other three bands (#1, #2 and #3) were excluded from the MS analyses. M: molecular marker. Each experiment (biological replicate) was repeated two times. (B, C) Western blots of the fractions eluted from the anti-FLAG immunoprecipitate were analyzed by immunoblotting using antibodies against FLAG (B) , XPOT, XPO1, SLC25A13, DNAJA1, UQCRC2, PHB1, and <t>PHB2</t> (C) . 293T cells transfected with empty plasmid (E) or NcGRA7 cDNA fused with a FLAG tag (G7) at 20 h posttransfection and HFFs infected with the parental strain Nc1 of N. caninum (WT) and NcGRA7-complemented (7c) parasites at 40 h postinfection were used. Each experiment (similar biological replicate) was repeated two time (B, C) .$
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$Characterization of NcGA7-binding proteins. (A) Silver staining for SDS–PAGE to identify NcGRA7-binding proteins by an anti-FLAG immunoprecipitation assay using 293T cells transfected with empty plasmid (Mock, Lanes 1 and 2) or NcGRA7 cDNA fused with a FLAG tag (Lanes 3 and 4). Enriched or exclusively detected proteins are shown as five bands, while the other three bands (#1, #2 and #3) were excluded from the MS analyses. M: molecular marker. Each experiment (biological replicate) was repeated two times. (B, C) Western blots of the fractions eluted from the anti-FLAG immunoprecipitate were analyzed by immunoblotting using antibodies against FLAG (B) , XPOT, XPO1, SLC25A13, DNAJA1, UQCRC2, PHB1, and <t>PHB2</t> (C) . 293T cells transfected with empty plasmid (E) or NcGRA7 cDNA fused with a FLAG tag (G7) at 20 h posttransfection and HFFs infected with the parental strain Nc1 of N. caninum (WT) and NcGRA7-complemented (7c) parasites at 40 h postinfection were used. Each experiment (similar biological replicate) was repeated two time (B, C) .$
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Image Search Results

Journal: Frontiers in Immunology

Article Title: Mitochondrial damage and IL-1β production in monocytes caused by Neospora caninum infection are mediated by dense granule protein 7 and prohibitins

doi: 10.3389/fimmu.2025.1408992

Figure Lengend Snippet: Characterization of NcGA7-binding proteins. (A) Silver staining for SDS–PAGE to identify NcGRA7-binding proteins by an anti-FLAG immunoprecipitation assay using 293T cells transfected with empty plasmid (Mock, Lanes 1 and 2) or NcGRA7 cDNA fused with a FLAG tag (Lanes 3 and 4). Enriched or exclusively detected proteins are shown as five bands, while the other three bands (#1, #2 and #3) were excluded from the MS analyses. M: molecular marker. Each experiment (biological replicate) was repeated two times. (B, C) Western blots of the fractions eluted from the anti-FLAG immunoprecipitate were analyzed by immunoblotting using antibodies against FLAG (B) , XPOT, XPO1, SLC25A13, DNAJA1, UQCRC2, PHB1, and PHB2 (C) . 293T cells transfected with empty plasmid (E) or NcGRA7 cDNA fused with a FLAG tag (G7) at 20 h posttransfection and HFFs infected with the parental strain Nc1 of N. caninum (WT) and NcGRA7-complemented (7c) parasites at 40 h postinfection were used. Each experiment (similar biological replicate) was repeated two time (B, C) .

Article Snippet: Anti-FLAG M2 mouse monoclonal antibody (Sigma–Aldrich), anti-XPOT (Exportin-T) rabbit antibody (A303-972A, Bethyl, Montgomery, TX, USA), anti-XPO1(CRM1) rabbit antibody (A300-469A, Bethyl), anti-SLC25A13 rabbit antibody (GTX109001, GeneTex, Irvine, CA, USA), anti-DNAJA1 rabbit antibody (A304-516A, Bethyl), anti-UQCRC2 rabbit antibody (GTX114873, GeneTex), anti-PHB1 rabbit antibody (GTX101105, GeneTex), anti-CoxIV rabbit monoclonal antibody (3E11, Cell Signaling Technology, Danvers, MA, USA), anti-GAPDH rabbit monoclonal antibody (14C10, Cell Signaling Technology), anti-Mfn1 rabbit antibody (13798-1-AP, Proteintech, Rosemont, IL, USA), anti-AIF mouse monoclonal antibody (sc-13116, Santa Cruz Biotechnology, Dallas, TX, USA), anti-mtHSP70 mouse monoclonal antibody (JG1, Invitrogen, Waltham, MA, USA), anti-VDAC1 rabbit antibody (4866, Cell Signaling Technology), anti-PHB2 mouse monoclonal antibody (sc-133094, Santa Cruz Biotechnology), anti-Histone H3 rabbit antibody (9715S, Cell Signaling Technology), anti-phospho-NF-κB p65 rabbit monoclonal antibody (93H1, Cell Signaling Technology) and anti-NFκB p65 rabbit polyclonal antibody (sc-109, Santa Cruz Biotechnology) were used for western blot and indirect fluorescent antibody test (IFAT) in this study.

Techniques: Binding Assay, Silver Staining, SDS Page, Immunoprecipitation, Transfection, Plasmid Preparation, FLAG-tag, Marker, Western Blot, Infection

Journal: Frontiers in Immunology

Article Title: Mitochondrial damage and IL-1β production in monocytes caused by Neospora caninum infection are mediated by dense granule protein 7 and prohibitins

doi: 10.3389/fimmu.2025.1408992

Figure Lengend Snippet: Localization of NcGRA7 in host mitochondria and binding to host mitochondrial proteins. (A) Schematic diagram of isolated mitochondria under isotonic and swelling conditions. Schematics of the isotonic (left) and swelling (right) conditions used in this study. Under isotonic conditions, proteinase K can access outer mitochondrial membrane (OMM) proteins but not the intermembrane space (IMS), inner mitochondrial membrane (IMM), or matrix proteins through membrane barriers. In addition, under swelling conditions, the protease can reach the IMS, followed by cleavage of both the OMM and IMS proteins. The inset shows mitochondrial proteins as markers for each category. (B) The mitochondrial fraction (Mt) isolated from HFFs was treated with proteinase K under isotonic (–) or hypotonic swelling (+) conditions. The reactants were developed by immunoblotting with antibodies against NcGRA7 or against several mitochondrial markers as indicated. OMM protein: Mfn1. IMS proteins: AIF, PHB1 and PHB2. IMM protein: COX IV. Matrix protein: mHsp70. Each experiment (biological replicate) was repeated two times. (C) Western blot of eluted fractions of HFFs infected with the parental strain Nc1 of N. caninum (WT) or NcGRA7-complemented parasites (7c) at 40 h post infection from anti-FLAG immunoprecipitation were analyzed by immunoblotting using antibodies against several mitochondrial markers as indicated. *Because mouse antibodies against FLAG, AIF and mHsp70 were used, the anti-mouse HRP secondary antibody was used to detect the anti-FLAG mouse antibody.

Techniques: Binding Assay, Isolation, Membrane, Western Blot, Infection, Immunoprecipitation