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Proteintech rabbit antibodies against mff

vMIA-mediated mitochondrial fragmentation is independent on the fission machinery proteins DLP1 and <t>MFF.</t> (A) Immunofluorescence analyses of MEFs MAVS-MITO cells: (a) control cells, (b) DLP1 silenced cells, (c) MFF silenced cells: (a–c) anti-TIM23; (d–f) overexpression of vMIA-Myc: (d) anti-TIM23, (e) anti-Myc, (f) merge image of d and e; (g–i) overexpression of vMIA-Myc in DLP1 silenced cells: (g) anti-TIM23, (h) anti-Myc, (i) merge image of g and h; (j–l) overexpression of vMIA-Myc in MFF silenced cells: (j) anti-TIM23, (k) anti-Myc, (l) merge image of j and k. Bars represent 10 µm. (B,C) Statistical analysis of mitochondrial morphologies upon overexpression of vMIA-Myc in MEFs MAVS-MITO cells in the absence of DLP1 or MFF, respectively. Approximately 600 cells were analysed per condition. Data represents the means ± SEM of three independent experiments analysed using two-way ANOVA with Bonferroni’s multi comparations test (ns = non-significant, ****– p < 0.0001). Error bars represent SEM.

Rabbit Antibodies Against Mff, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 241 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+antibodies+against+mff/MFF+Antibody/pmc09014249-29-0-5
Average 96 stars, based on 241 article reviews

rabbit antibodies against mff - by Bioz Stars, 2026-09

96/100 stars

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1) Product Images from "Human Cytomegalovirus vMIA Inhibits MAVS Oligomerization at Peroxisomes in an MFF-Dependent Manner"

Article Title: Human Cytomegalovirus vMIA Inhibits MAVS Oligomerization at Peroxisomes in an MFF-Dependent Manner

Journal: Frontiers in Cell and Developmental Biology

doi: 10.3389/fcell.2022.871977

vMIA-mediated mitochondrial fragmentation is independent on the fission machinery proteins DLP1 and MFF. (A) Immunofluorescence analyses of MEFs MAVS-MITO cells: (a) control cells, (b) DLP1 silenced cells, (c) MFF silenced cells: (a–c) anti-TIM23; (d–f) overexpression of vMIA-Myc: (d) anti-TIM23, (e) anti-Myc, (f) merge image of d and e; (g–i) overexpression of vMIA-Myc in DLP1 silenced cells: (g) anti-TIM23, (h) anti-Myc, (i) merge image of g and h; (j–l) overexpression of vMIA-Myc in MFF silenced cells: (j) anti-TIM23, (k) anti-Myc, (l) merge image of j and k. Bars represent 10 µm. (B,C) Statistical analysis of mitochondrial morphologies upon overexpression of vMIA-Myc in MEFs MAVS-MITO cells in the absence of DLP1 or MFF, respectively. Approximately 600 cells were analysed per condition. Data represents the means ± SEM of three independent experiments analysed using two-way ANOVA with Bonferroni’s multi comparations test (ns = non-significant, ****– p < 0.0001). Error bars represent SEM.

Figure Legend Snippet: vMIA-mediated mitochondrial fragmentation is independent on the fission machinery proteins DLP1 and MFF. (A) Immunofluorescence analyses of MEFs MAVS-MITO cells: (a) control cells, (b) DLP1 silenced cells, (c) MFF silenced cells: (a–c) anti-TIM23; (d–f) overexpression of vMIA-Myc: (d) anti-TIM23, (e) anti-Myc, (f) merge image of d and e; (g–i) overexpression of vMIA-Myc in DLP1 silenced cells: (g) anti-TIM23, (h) anti-Myc, (i) merge image of g and h; (j–l) overexpression of vMIA-Myc in MFF silenced cells: (j) anti-TIM23, (k) anti-Myc, (l) merge image of j and k. Bars represent 10 µm. (B,C) Statistical analysis of mitochondrial morphologies upon overexpression of vMIA-Myc in MEFs MAVS-MITO cells in the absence of DLP1 or MFF, respectively. Approximately 600 cells were analysed per condition. Data represents the means ± SEM of three independent experiments analysed using two-way ANOVA with Bonferroni’s multi comparations test (ns = non-significant, ****– p < 0.0001). Error bars represent SEM.

Techniques Used: Immunofluorescence, Control, Over Expression

$vMIA inhibits MAVS oligomerization at peroxisomes and mitochondria. MFF is essential for the vMIA-mediated inhibition of MAVS oligomerization at peroxisomes but not at mitochondria. (A,B) HEK293T cells infected with SeV in the presence or absence of vMIA. Density gradient assay was performed to demonstrate the separation of endogenous MAVS based on its density. 1—7 represent the fractions isolated from the gradient assay, where 1 represents the fraction with lowest density and 7 represents the fraction with highest density. (A) Peroxisome-enriched fraction, (B) Mitochondria-enriched fraction. (C,D) HEK293T cells infected with SeV in the presence or absence of vMIA and in the absence of MFF. Density gradient assay was performed to demonstrate the separation of endogenous MAVS based on its density. 1—7 represent the fractions isolated from the gradient assay, where 1 represents the fraction with lowest density and 7 represents the fraction with highest density. (C) Peroxisome-enriched fraction, (D) Mitochondria-enriched fraction. (A–D) Immunoblots were performed with antibodies against MAVS, Myc-tag, COXIV, PEX14 and PMP70. (E) Whole cell lysates were resolved by SDS-PAGE. SeV infection, and consequential activation of MAVS downstream signalling, was confirmed using anti-p-STAT1. vMIA-Myc overexpression and MFF silencing were also confirmed using anti-Myc and anti-MFF, respectively. Antibody against Actin was used as loading control.$
Figure Legend Snippet: vMIA inhibits MAVS oligomerization at peroxisomes and mitochondria. MFF is essential for the vMIA-mediated inhibition of MAVS oligomerization at peroxisomes but not at mitochondria. (A,B) HEK293T cells infected with SeV in the presence or absence of vMIA. Density gradient assay was performed to demonstrate the separation of endogenous MAVS based on its density. 1—7 represent the fractions isolated from the gradient assay, where 1 represents the fraction with lowest density and 7 represents the fraction with highest density. (A) Peroxisome-enriched fraction, (B) Mitochondria-enriched fraction. (C,D) HEK293T cells infected with SeV in the presence or absence of vMIA and in the absence of MFF. Density gradient assay was performed to demonstrate the separation of endogenous MAVS based on its density. 1—7 represent the fractions isolated from the gradient assay, where 1 represents the fraction with lowest density and 7 represents the fraction with highest density. (C) Peroxisome-enriched fraction, (D) Mitochondria-enriched fraction. (A–D) Immunoblots were performed with antibodies against MAVS, Myc-tag, COXIV, PEX14 and PMP70. (E) Whole cell lysates were resolved by SDS-PAGE. SeV infection, and consequential activation of MAVS downstream signalling, was confirmed using anti-p-STAT1. vMIA-Myc overexpression and MFF silencing were also confirmed using anti-Myc and anti-MFF, respectively. Antibody against Actin was used as loading control.

Techniques Used: Inhibition, Infection, Isolation, Western Blot, SDS Page, Activation Assay, Over Expression, Control

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Journal: Frontiers in Cell and Developmental Biology

Article Title: Human Cytomegalovirus vMIA Inhibits MAVS Oligomerization at Peroxisomes in an MFF-Dependent Manner

doi: 10.3389/fcell.2022.871977

Figure Lengend Snippet: vMIA-mediated mitochondrial fragmentation is independent on the fission machinery proteins DLP1 and MFF. (A) Immunofluorescence analyses of MEFs MAVS-MITO cells: (a) control cells, (b) DLP1 silenced cells, (c) MFF silenced cells: (a–c) anti-TIM23; (d–f) overexpression of vMIA-Myc: (d) anti-TIM23, (e) anti-Myc, (f) merge image of d and e; (g–i) overexpression of vMIA-Myc in DLP1 silenced cells: (g) anti-TIM23, (h) anti-Myc, (i) merge image of g and h; (j–l) overexpression of vMIA-Myc in MFF silenced cells: (j) anti-TIM23, (k) anti-Myc, (l) merge image of j and k. Bars represent 10 µm. (B,C) Statistical analysis of mitochondrial morphologies upon overexpression of vMIA-Myc in MEFs MAVS-MITO cells in the absence of DLP1 or MFF, respectively. Approximately 600 cells were analysed per condition. Data represents the means ± SEM of three independent experiments analysed using two-way ANOVA with Bonferroni’s multi comparations test (ns = non-significant, ****– p < 0.0001). Error bars represent SEM.

Article Snippet: Rabbit antibodies against MFF (17090-1-AP, ProteinTech, Manchester, UK) 30, Myc-tag (71D10, 2,278, Cell Signalling Technology, Beverly, MA, United States), FLAG epitope (F7425, Sigma-Aldrich, St. Louis, MO, United States), β-Actin (4,967, Cell Signalling, Danvers, MA, United States), PEX14 (GTX129230, GeneTex, CA,United States) and MAVS (A300-782A, Bethyl Laboratories, TX, United States), and mouse antibodies against MAVS (E-3, SC-166583, Santa Cruz Biotechnology, Dallas, TX, United States), p-STAT1 (Y701, BD Biosciences, San Jose, CA, United States), DLP1 (611,113, BD Bioscience, San Jose, CA, United States), PMP70 (SAB4200181, Sigma-Aldrich, St. Louis, MO, United States), COXIV (4,850, Cell Signalling Technology, Beverly, MA, United States) and α-Tubulin (T9026, Sigma-Aldrich, St. Louis, MO, United States) were used for immunoblotting.

Techniques: Immunofluorescence, Control, Over Expression

Journal: Frontiers in Cell and Developmental Biology

Article Title: Human Cytomegalovirus vMIA Inhibits MAVS Oligomerization at Peroxisomes in an MFF-Dependent Manner

doi: 10.3389/fcell.2022.871977

Figure Lengend Snippet: vMIA inhibits MAVS oligomerization at peroxisomes and mitochondria. MFF is essential for the vMIA-mediated inhibition of MAVS oligomerization at peroxisomes but not at mitochondria. (A,B) HEK293T cells infected with SeV in the presence or absence of vMIA. Density gradient assay was performed to demonstrate the separation of endogenous MAVS based on its density. 1—7 represent the fractions isolated from the gradient assay, where 1 represents the fraction with lowest density and 7 represents the fraction with highest density. (A) Peroxisome-enriched fraction, (B) Mitochondria-enriched fraction. (C,D) HEK293T cells infected with SeV in the presence or absence of vMIA and in the absence of MFF. Density gradient assay was performed to demonstrate the separation of endogenous MAVS based on its density. 1—7 represent the fractions isolated from the gradient assay, where 1 represents the fraction with lowest density and 7 represents the fraction with highest density. (C) Peroxisome-enriched fraction, (D) Mitochondria-enriched fraction. (A–D) Immunoblots were performed with antibodies against MAVS, Myc-tag, COXIV, PEX14 and PMP70. (E) Whole cell lysates were resolved by SDS-PAGE. SeV infection, and consequential activation of MAVS downstream signalling, was confirmed using anti-p-STAT1. vMIA-Myc overexpression and MFF silencing were also confirmed using anti-Myc and anti-MFF, respectively. Antibody against Actin was used as loading control.

Techniques: Inhibition, Infection, Isolation, Western Blot, SDS Page, Activation Assay, Over Expression, Control

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