pljm1 empty vector Search Results


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Addgene inc blast plasmid addgene rrid addgene 111887 recombinant dna reagent pljm1 empty
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Addgene inc empty vector control hek293 cells
a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed <t>HEK293</t> cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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Addgene inc pbabe-haii
a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed <t>HEK293</t> cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
Pbabe Haii, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Promega fugene hd
a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed <t>HEK293</t> cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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Thermo Fisher reference mammalian selection pcdna3 1 1 empty vector control invitrogen
a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed <t>HEK293</t> cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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Addgene inc pljm1 bsd blasticidin pmd2 g lentivirus generation addgene
a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed <t>HEK293</t> cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
Pljm1 Bsd Blasticidin Pmd2 G Lentivirus Generation Addgene, supplied by Addgene inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Thermo Fisher lipofectamine 3000 transfection reagent
a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed <t>HEK293</t> cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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Addgene inc pljm1 flag ha ago2 wt
a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed <t>HEK293</t> cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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Addgene inc plasmid pljm1 mcs
a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed <t>HEK293</t> cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
Plasmid Pljm1 Mcs, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: FAM210A is essential for cold-induced mitochondrial remodeling in brown adipocytes

doi: 10.1038/s41467-023-41988-y

Figure Lengend Snippet: a YME1L, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). b Quantification of OPA1 Δ C protein level in ( a ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.000762, and 0.003106). c OMA1, OPA1 Δ C, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and OMA1 and OPA1 Δ C were incubated with and without the presence of FAM210A ( n = 3 independent experiments). d Quantification of OPA1 Δ C protein level in ( c ) (mean ± s.e.m; two-tailed unpaired Student’s t test). e Co-immunoprecipitation (Co-IP) of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments). f Proximity ligation assay (PLA) showing the protein interaction of FAM210A-FLAG and YME1L in Fam210a-flag overexpressed HEK293 cell line ( n = 3 independent experiments; scale bar: 10 µm). g YME1L, OMA1, and FAM210A were synthesized by E. coli cell-free protein synthesis system, and YME1L and OMA1 were incubated with or without the presence of FAM210A ( n = 3 independent experiments). h Quantification of OMA1 protein level in ( g ) (mean ± s.e.m; two-tailed unpaired Student’s t test; P = 0.02497). i Immunoblotting analysis of OPA1 in BAT of control and Fam210a iAKO after cold exposure for 0 h and 6 h by using the large format electrophoresis chamber ( n = 3 mice per group). j Quantification of OPA1-b/e in ( i ) (mean ± s.e.m; two-tailed paired Student’s t test; P = 0.02418). k Diagram depicting that FAM210A enhances YME1L activity thus suppressing OMA1, which protects L-OPA1 from over-cleavage during cold exposure to facilitate mitochondrial cristae remodeling (diagram created with BioRender.com). * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

Article Snippet: The Fam210a-flag overexpressed and empty vector control HEK293 cells were generated using pLJM-EGFP (Addgene #19319).

Techniques: Synthesized, Incubation, Two Tailed Test, Immunoprecipitation, Co-Immunoprecipitation Assay, Proximity Ligation Assay, Western Blot, Control, Electrophoresis, Activity Assay