Review

rabbit anti mt co2 (Proteintech)

Name: rabbit anti mt co2
Brand: Proteintech
Rating: 96 (184 reviews)

Proteintech is a verified supplier

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Proteintech rabbit anti mt co2
Rabbit Anti Mt Co2, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 184 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit anti mt co2/product/Proteintech
Average 96 stars, based on 184 article reviews

rabbit anti mt co2 - by Bioz Stars, 2026-02

96/100 stars

Images

Image Search Results

Reduced levels of mt-tRNA Pro aminoacylation and OXPHOS complex proteins in dPARS2-deficient flies. (A) Northern blot analysis of mitochondrial tRNA Pro aminoacylation in total RNA samples from control and elav -Gal4-driven dPARS2 knockdown fly heads. Upper bands represent the charged tRNAs and lower bands represent the uncharged tRNAs. (B) Western blot analysis of mtDNA-encoded OXPHOS complex subunits in protein extracts from control and elav -Gal4-driven dPARS2 knockdown fly heads. Antibodies against individual subunits of OXPHOS complexes (MT-ND1, complex I; MT-CO2, complex IV) were used. Porin was used as a loading control. (C) Quantification of the Western blots shown in B. MT-ND1, N = 3; MT-CO2, N = 4. ∗p < 0.05, ∗∗p < 0.01. (D) Western blot analysis of nuclear-encoded OXPHOS complex subunits in protein extracts from control and elav -Gal4-driven dPARS2 knockdown fly heads. Antibodies against individual subunits of OXPHOS complexes (NDUFS3 and NDUFS1, complex I; SDHB, complex II; UQCRFS1, complex III; ATP5A, complex V) were used. Porin was used as a loading control. (E) Quantification of the Western blots shown in D. NDUFS1 and UQCRFS1, N = 3; NDUFS3, SDHB and ATP5A, N = 4. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗∗p < 0.0001, ns, not significant. (F) Northern blot analysis of mitochondrial tRNA Pro aminoacylation in total RNA samples from control and Da -Gal4-driven dPARS2 knockdown larvae. (G) Western blot analysis of mtDNA-encoded OXPHOS complex subunits in protein extracts from control and Da -Gal4-driven dPARS2 knockdown larvae. (H) Quantification of the Western blots shown in G. N = 3. ∗∗∗∗p < 0.0001. (I) Western blot analysis of nuclear-encoded OXPHOS complex subunits in protein extracts from control and Da -Gal4-driven dPARS2 knockdown larvae. (J) Quantification of the Western blots shown in I. NDUFS3, UQCRFS1 and ATP5A, N = 3; NDUFS1 and SDHB, N = 4. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001, ns, not significant.

Journal: Redox Biology

Article Title: Activation of the integrated stress response contributes to developmental delay and seizures caused by mitochondrial prolyl-tRNA synthetase (PARS2) deficiency

doi: 10.1016/j.redox.2025.103966

Figure Lengend Snippet: Reduced levels of mt-tRNA Pro aminoacylation and OXPHOS complex proteins in dPARS2-deficient flies. (A) Northern blot analysis of mitochondrial tRNA Pro aminoacylation in total RNA samples from control and elav -Gal4-driven dPARS2 knockdown fly heads. Upper bands represent the charged tRNAs and lower bands represent the uncharged tRNAs. (B) Western blot analysis of mtDNA-encoded OXPHOS complex subunits in protein extracts from control and elav -Gal4-driven dPARS2 knockdown fly heads. Antibodies against individual subunits of OXPHOS complexes (MT-ND1, complex I; MT-CO2, complex IV) were used. Porin was used as a loading control. (C) Quantification of the Western blots shown in B. MT-ND1, N = 3; MT-CO2, N = 4. ∗p < 0.05, ∗∗p < 0.01. (D) Western blot analysis of nuclear-encoded OXPHOS complex subunits in protein extracts from control and elav -Gal4-driven dPARS2 knockdown fly heads. Antibodies against individual subunits of OXPHOS complexes (NDUFS3 and NDUFS1, complex I; SDHB, complex II; UQCRFS1, complex III; ATP5A, complex V) were used. Porin was used as a loading control. (E) Quantification of the Western blots shown in D. NDUFS1 and UQCRFS1, N = 3; NDUFS3, SDHB and ATP5A, N = 4. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗∗p < 0.0001, ns, not significant. (F) Northern blot analysis of mitochondrial tRNA Pro aminoacylation in total RNA samples from control and Da -Gal4-driven dPARS2 knockdown larvae. (G) Western blot analysis of mtDNA-encoded OXPHOS complex subunits in protein extracts from control and Da -Gal4-driven dPARS2 knockdown larvae. (H) Quantification of the Western blots shown in G. N = 3. ∗∗∗∗p < 0.0001. (I) Western blot analysis of nuclear-encoded OXPHOS complex subunits in protein extracts from control and Da -Gal4-driven dPARS2 knockdown larvae. (J) Quantification of the Western blots shown in I. NDUFS3, UQCRFS1 and ATP5A, N = 3; NDUFS1 and SDHB, N = 4. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001, ns, not significant.

Article Snippet: Primary antibodies used were anti-MT-ND1 (Abcam, AB181848-1001), anti-MT- CO2 (Proteintech, 55070-1-AP), anti-MT-ATP8 (Proteintech, 26723-1-AP),anti-NDUFS1 (Proteintech, 12444-1-AP), anti-NDUFS3 (Abcam, ab14711), anti-UQCRFS1 (Abcam, ab14746), anti-ATP5A (Abcam, ab14748), anti-SDHB (Proteintech, 10620-1-AP), anti-Porin/VDAC (Abcam, ab14734), anti-P-eIF2α (Cell Signaling Technology, 3398), anti-eIF2α (Cell Signaling Technology, 2103), anti-P-PERK (ABclonal, AP0886), anti-PERK (ABclonal, A27664 ), anti-P-GCN2 (Abcam, ab75836), anti-GCN2 (ABclonal, A2307), anti-LDH (ThermoFisher, PA5-26531), anti-PARS2 (ABclonal, A16512), anti-His (yeasen, 30405ES50), anti-ATF4 (Abcam, ab1371), anti-Alpha actin (Proteintech, 23660-1-AP) and anti-Alpha tubulin (Proteintech, 66031-1-Ig).

Techniques: Northern Blot, Control, Knockdown, Western Blot

Defective assembly of OXPHOS complexes in dPARS2-deficient flies. (A) BN-PAGE followed by Western blot analysis of isolated mitochondria from control and elav -Gal4-driven dPARS2 knockdown fly heads. Antibodies against individual subunits of OXPHOS complexes (NDUFS3, complex I; SDHB, complex II; UQRCFS1, complex III; MT-CO2, complex IV; ATP5A, complex V) were used. Porin was used as a loading control. (B) Quantification of the Western blots shown in A. complex II, complex III and complex V, N = 3; complex IV, N = 4; complex I, N = 5. ∗∗p < 0.01, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001. (C) BN-PAGE followed by Western blot analysis of isolated mitochondria from control and Da -Gal4-driven dPARS2 knockdown larvae. (D) Quantification of the Western blots shown in C. complex II and complex III, N = 3; complex I and complex V, N = 4; complex IV, N = 5. ∗∗p < 0.01, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001.

Journal: Redox Biology

Article Title: Activation of the integrated stress response contributes to developmental delay and seizures caused by mitochondrial prolyl-tRNA synthetase (PARS2) deficiency

doi: 10.1016/j.redox.2025.103966

Figure Lengend Snippet: Defective assembly of OXPHOS complexes in dPARS2-deficient flies. (A) BN-PAGE followed by Western blot analysis of isolated mitochondria from control and elav -Gal4-driven dPARS2 knockdown fly heads. Antibodies against individual subunits of OXPHOS complexes (NDUFS3, complex I; SDHB, complex II; UQRCFS1, complex III; MT-CO2, complex IV; ATP5A, complex V) were used. Porin was used as a loading control. (B) Quantification of the Western blots shown in A. complex II, complex III and complex V, N = 3; complex IV, N = 4; complex I, N = 5. ∗∗p < 0.01, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001. (C) BN-PAGE followed by Western blot analysis of isolated mitochondria from control and Da -Gal4-driven dPARS2 knockdown larvae. (D) Quantification of the Western blots shown in C. complex II and complex III, N = 3; complex I and complex V, N = 4; complex IV, N = 5. ∗∗p < 0.01, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001.

Techniques: Western Blot, Isolation, Control, Knockdown

PARS2 V95I mutation causes mitochondrial dysfunction and ISR activation in human cells (A) Western blot analysis of ectopically expressed PARS2 proteins. Lysates from HEK-293T cells transfected with plasmids encoding His-tagged wild-type (WT) or the indicated PARS2 variants were immunoblotted with an anti-His antibody. α-actin was used as a loading control. (B) Quantification of the Western blots shown in A. N = 5, ∗∗p < 0.01, ∗∗∗p < 0.001. (C) Western blot analysis of endogenous PARS2 in protein extracts from the wild-type controls and the PARS2 V95I cells. α-actin was used as a loading control. (D) Quantification of the Western blots shown in C. N = 4, ∗∗∗p < 0.001. (E) Western blot analysis of mtDNA-encoded CO2 and ATP8 and nuclear-DNA encoded NDUFS1, NDUFS3, UQCRFS1 and ATP5A in protein extracts from the wild-type controls and the PARS2 V95I cells. VDAC was used as a loading control. (F) Quantification of the Western blots shown in E. MT-CO2, MT-ATP8, NDUFS1, NDUFS3, and ATP5A, N = 4; UQCRFS1, N = 7. ∗p < 0.05, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001, ns, not significant. (G) CI, CII and CIV in-gel activity analysis of isolated mitochondria from the wild-type controls and the PARS2 V95I cells. (H) Western blot analysis of P-eIF2α and eIF2α in protein extracts from the wild-type controls and the PARS2 V95I cells. α-actin was used as a loading control. (I) Quantification of the Western blots shown in H. N = 5, ∗∗∗∗p < 0.0001. (J) Western blot analysis with anti-puromycin antibody and ponceau staining on protein extracts from the wild-type controls and the PARS2 V95I cells. α-actin was used as the loading control. (K) Quantification of the Western blots shown in J. N = 4. ∗∗∗∗p < 0.0001. (L) Western blot analysis of ATF4 in protein extracts from the wild-type controls and the PARS2 V95I cells. α-actin was used as a loading control. (M) Quantification of the Western blots shown in L. N = 5, ∗∗∗p < 0.001. (N) Western blot analysis of P-GCN2 and GCN2 in protein extracts from the wild-type controls and the PARS2 V95I cells. α-tubulin was used as a loading control. (O) Quantification of the Western blots shown in N. N = 4, ∗∗p < 0.01. (P) Western blot analysis of P-PERK and PERK in protein extracts from the wild-type controls and the PARS2 V95I cells. α-tubulin was used as a loading control. (Q) Quantification of the Western blots shown in P. N = 5, ns, not significant.

Journal: Redox Biology

Article Title: Activation of the integrated stress response contributes to developmental delay and seizures caused by mitochondrial prolyl-tRNA synthetase (PARS2) deficiency

doi: 10.1016/j.redox.2025.103966

Figure Lengend Snippet: PARS2 V95I mutation causes mitochondrial dysfunction and ISR activation in human cells (A) Western blot analysis of ectopically expressed PARS2 proteins. Lysates from HEK-293T cells transfected with plasmids encoding His-tagged wild-type (WT) or the indicated PARS2 variants were immunoblotted with an anti-His antibody. α-actin was used as a loading control. (B) Quantification of the Western blots shown in A. N = 5, ∗∗p < 0.01, ∗∗∗p < 0.001. (C) Western blot analysis of endogenous PARS2 in protein extracts from the wild-type controls and the PARS2 V95I cells. α-actin was used as a loading control. (D) Quantification of the Western blots shown in C. N = 4, ∗∗∗p < 0.001. (E) Western blot analysis of mtDNA-encoded CO2 and ATP8 and nuclear-DNA encoded NDUFS1, NDUFS3, UQCRFS1 and ATP5A in protein extracts from the wild-type controls and the PARS2 V95I cells. VDAC was used as a loading control. (F) Quantification of the Western blots shown in E. MT-CO2, MT-ATP8, NDUFS1, NDUFS3, and ATP5A, N = 4; UQCRFS1, N = 7. ∗p < 0.05, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001, ns, not significant. (G) CI, CII and CIV in-gel activity analysis of isolated mitochondria from the wild-type controls and the PARS2 V95I cells. (H) Western blot analysis of P-eIF2α and eIF2α in protein extracts from the wild-type controls and the PARS2 V95I cells. α-actin was used as a loading control. (I) Quantification of the Western blots shown in H. N = 5, ∗∗∗∗p < 0.0001. (J) Western blot analysis with anti-puromycin antibody and ponceau staining on protein extracts from the wild-type controls and the PARS2 V95I cells. α-actin was used as the loading control. (K) Quantification of the Western blots shown in J. N = 4. ∗∗∗∗p < 0.0001. (L) Western blot analysis of ATF4 in protein extracts from the wild-type controls and the PARS2 V95I cells. α-actin was used as a loading control. (M) Quantification of the Western blots shown in L. N = 5, ∗∗∗p < 0.001. (N) Western blot analysis of P-GCN2 and GCN2 in protein extracts from the wild-type controls and the PARS2 V95I cells. α-tubulin was used as a loading control. (O) Quantification of the Western blots shown in N. N = 4, ∗∗p < 0.01. (P) Western blot analysis of P-PERK and PERK in protein extracts from the wild-type controls and the PARS2 V95I cells. α-tubulin was used as a loading control. (Q) Quantification of the Western blots shown in P. N = 5, ns, not significant.

Techniques: Mutagenesis, Activation Assay, Western Blot, Transfection, Control, Activity Assay, Isolation, Staining

A Immunoblot blot analysis of Oxa1L and mitochondrial OXPHOS complex subunits in control and MPP⁺-treated SH-SY5Y cells. Mitochondrial genome-encoded subunits (MT-CYTB, MT-CO1, MT-CO2, MT-ATP8) and nuclear genome-encoded subunits (NDUFB8, SDHB, ATP5A1) are indicated. B Immunoblot analysis of OXPHOS subunits in scramble and Oxa1L knockdown (shOxa1L) cells following MPP⁺ treatment, showing selective reduction of mitochondrial genome–encoded proteins upon Oxa1L deficiency. C-D Cryo-EM density map (C) and corresponding atomic model (D) of the Oxa1L-mitoribosome complex, revealing Oxa1L positioned adjacent to the ribosomal exit tunnel. E AlphaFold3-predicted structure of monomeric human Oxa1L, highlighting its five transmembrane helices. F Sequence alignment of Oxa1L transmembrane regions across representative species, illustrating strong evolutionary conservation. Multiple sequence alignment was performed using WebLogo. G AF3-predicted model of Oxa1L-uL24m-bL29m complex. The black box indicates the focused area shown in (H, I). H, I Enlarged views of interaction interfaces between Oxa1L and ribosomal proteins uL24m (H) and bL29m (I), identifying conserved matrix-exposed regions implicated in co-translational membrane insertion.

Journal: bioRxiv

Article Title: Oxa1L-Mediated Co-translational Protein Insertion Maintains Mitochondrial Function in Parkinson’s Disease Models

doi: 10.64898/2025.12.22.696118

Figure Lengend Snippet: A Immunoblot blot analysis of Oxa1L and mitochondrial OXPHOS complex subunits in control and MPP⁺-treated SH-SY5Y cells. Mitochondrial genome-encoded subunits (MT-CYTB, MT-CO1, MT-CO2, MT-ATP8) and nuclear genome-encoded subunits (NDUFB8, SDHB, ATP5A1) are indicated. B Immunoblot analysis of OXPHOS subunits in scramble and Oxa1L knockdown (shOxa1L) cells following MPP⁺ treatment, showing selective reduction of mitochondrial genome–encoded proteins upon Oxa1L deficiency. C-D Cryo-EM density map (C) and corresponding atomic model (D) of the Oxa1L-mitoribosome complex, revealing Oxa1L positioned adjacent to the ribosomal exit tunnel. E AlphaFold3-predicted structure of monomeric human Oxa1L, highlighting its five transmembrane helices. F Sequence alignment of Oxa1L transmembrane regions across representative species, illustrating strong evolutionary conservation. Multiple sequence alignment was performed using WebLogo. G AF3-predicted model of Oxa1L-uL24m-bL29m complex. The black box indicates the focused area shown in (H, I). H, I Enlarged views of interaction interfaces between Oxa1L and ribosomal proteins uL24m (H) and bL29m (I), identifying conserved matrix-exposed regions implicated in co-translational membrane insertion.

Article Snippet: Membranes were probed with primary antibodies against DYKDDDDK (FLAG) (Flag tag, proteintech, 1:5000), GAPDH (proteintech, 1:5000), Oxa1L (proteintech, 1:5000), MT-CYTB (proteintech, 1:2000), MT-CO1 (Cell Signaling Technology, 1:1000), MT-CO2 (proteintech, 1:2000), MT-ATP8 (abclonal, 1:1000), NDUFB8 (Cell Signaling Technology, 1:1000), SDHA (abclonal, 1:1000), SDHB (Cell Signaling Technology, 1:1000), and ATP5A1 (abclonal, 1:10000).

Techniques: Western Blot, Control, Knockdown, Cryo-EM Sample Prep, Sequencing, Membrane

Review

Structured Review

Images

Similar Products

Image Search Results