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Proteintech mt cytb
A Immunoblot blot analysis <t>of</t> <t>Oxa1L</t> and mitochondrial OXPHOS complex subunits in control and MPP⁺-treated SH-SY5Y cells. Mitochondrial genome-encoded subunits <t>(MT-CYTB,</t> 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.
Mt Cytb, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 107 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mt cytb - by Bioz Stars, 2026-03
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Images

1) Product Images from "Oxa1L-Mediated Co-translational Protein Insertion Maintains Mitochondrial Function in Parkinson’s Disease Models"

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

Journal: bioRxiv

doi: 10.64898/2025.12.22.696118

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.
Figure Legend 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.

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



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Image Search Results


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