> Chemicals & Drugs > Amino Acid > OPA1 protein, human

OPA1 protein, human

OPA1 protein is a dynamin-like GTPase that plays a crucial role in mitochondrial dynamics.
It is involved in the regulation of mitochondrial fusion, cristae organization, and apoptosis.
Mutations in the OPA1 gene have been associated with autosomal dominant optic atrophy, a leading cause of inherited blindness.
Understanding the funcation and regulation of OPA1 is esential for developing theraputic approaches to mitochondrial disorders and neurodegenerative diseases.
This AI-driven platform can optimize OPA1 protein research by facilitating access to relevant protocols from literature, pre-prints, and patents, while leveraging AI-comparisons to identify the best protocols and products.
This can enhance reproducibility and accruacy in OPA1 protein studies.

Most cited protocols related to «OPA1 protein, human»

Real-time PCR for Gene Expression Analysis

Cited 21 times

Real-time PCR was performed using an ABI 7700 Sequence Detection System (PE Applied-Biosystems) in the presence of SYBR-green. The optimisation of the real-time PCR reaction was performed according to the manufacturer's instructions (PE Applied-Biosystems, User Bulletin 2 applied to the SYBR-Green I core reagent protocol) but scaled down to 25 μl per reaction. The PCR conditions were standard (SYBR-Green I core reagent protocol) and all reagents were provided in the SYBR-Green I core reagent kit, including AmpliTaq-GOLD polymerase (PE Applied-Biosystems). After optimisation (see Results section), nucleotide primers were used at various concentrations for the detection and quantification of GAPDH, signal and coding TREC, GLI, MYC-C, MYC-N, OPA1, FLAG and Hop.

Ponchel F., Toomes C., Bransfield K., Leong F.T., Douglas S.H., Field S.L., Bell S.M., Combaret V., Puisieux A., Mighell A.J., Robinson P.A., Inglehearn C.F., Isaacs J.D, & Markham A.F. (2003). Real-time PCR based on SYBR-Green I fluorescence: An alternative to the TaqMan assay for a relative quantification of gene rearrangements, gene amplifications and micro gene deletions. BMC Biotechnology, 3, 18.

Publication 2003

GAPDH protein, human Gold Nucleotides Oligonucleotide Primers OPA1 protein, human Real-Time Polymerase Chain Reaction SYBR Green I

Conditional Knockout of the Opa1 Gene

Cited 7 times

All animal work was done according to guidelines established by the Johns Hopkins University Committee on Animal Care. We inserted a neomycin-resistant marker flanked by FRT and loxP sites next to exons 10 and 13, which are located in an essential GTPase domain. The targeting vector was transfected into C57BL/6–129/SvEv ES cells by electroporation. G418-resistant colonies were screened by PCR. Targeted ES cells were injected into C57BL/6 blastocysts to create chimeric mice. To create the null Opa1 allele, we crossed Flox-neo mice with EIIa-Cre transgenic mice as described (Wakabayashi et al., 2009 (link)). In addition, upon loxP recombination, a stop codon was generated immediately after exon 9 due to a frame shift. To generate the conditional allele, Flox-neo mice were crossed with a transgenic strain that ubiquitously expresses Flp recombinase (Wakabayashi et al., 2009 (link)). We bred these strains with a wild-type strain and isolated mice heterozygous for the null or conditional allele but not for Cre or Flp recombinase. All mice were kept on a mixed C57BL/6–129/SvEv background. We used RIP2-Opa1KO mice (RIP2-Cre Opa1^flox/−) and littermate controls (RIP2-Cre Opa1^flox/+) at 8–12 wk in all of the experiments.

Zhang Z., Wakabayashi N., Wakabayashi J., Tamura Y., Song W.J., Sereda S., Clerc P., Polster B.M., Aja S.M., Pletnikov M.V., Kensler T.W., Shirihai O.S., Iijima M., Hussain M.A, & Sesaki H. (2011). The dynamin-related GTPase Opa1 is required for glucose-stimulated ATP production in pancreatic beta cells. Molecular Biology of the Cell, 22(13), 2235-2245.

Publication 2011

Alleles Animals Animals, Transgenic antibiotic G 418 Blastocyst Cells Chimera Cloning Vectors Codon, Terminator Electroporation Embryonic Stem Cells Exons FLP recombinase Guanosine Triphosphate Phosphohydrolases Heterozygote Mice, Laboratory Mice, Transgenic Neomycin OPA1 protein, human Reading Frames Recombination, Genetic RIPK2 protein, human Strains

Subcellular Localization of GCN5L1

Cited 6 times

Confocal microscopy was used to localize GCN5L1-FLAG and dsRed-mito (Clontech) in fixed hepatocytes, by indirect immunolabeling of FLAG using Alexa 488 (Invitrogen). Immunogold labeling and electron microscopy was used to localize endogenous GCN5L1 and the ETC protein ATP5a. Sub-mitochondrial localization was performed by osmotic pressure subfractionation and proteinase K protection assays. Antibodies used for westerns include: monoclonal acetyl-lysine (Ac-K), OPA1, GAPDH, VDAC (Cell Signaling); polyclonal Ac-K, ATP5a, NDUFA9, GDH (Abcam); FLAG (Sigma). In co-immunoprecipitation experiments between GCN5L1-FLAG and NDUFA9-Myc or ATP5a-Myc, cells were co-transfected with plasmids for 24 h. Lysates were harvested and incubated with FLAG- or Myc-conjugated beads (Sigma and Cell Signaling, respectively). Beads were washed and analyzed by western blot. Endogenous co-immunoprecipitation experiments followed a similar protocol, however lysates were incubated with the relevant antibodies overnight, and interacting proteins were captured using protein A/G beads (Santa Cruz). Western blots were quantified using image analysis software, and those shown are representative of at least three independent experiments.

Scott I., Webster B.R., Li J.H, & Sack M.N. (2012). Identification of a molecular component of the mitochondrial acetyl transferase program; a novel role for GCN5L1. The Biochemical journal, 443(3), 655-661.

Publication 2012

Antibodies Biological Assay Cells Co-Immunoprecipitation Electron Microscopy Endopeptidase K G-substrate GAPDH protein, human Hepatocyte Lysine Microscopy, Confocal Mitochondria Mitomycin OPA1 protein, human Osmotic Pressure Plasmids Proteins Western Blot Western Blotting

Dissecting Mitochondrial Dynamics in Neurodegeneration

Cited 6 times

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Publication 2012

Animals, Transgenic Clone Cells Cloning Vectors DNA, Complementary Drosophila Embryo Gelsolin Homo sapiens Homozygote In Situ Nick-End Labeling Mice, Transgenic Mitochondria Null Mutation OPA1 protein, human Proliferating Cell Nuclear Antigen RNA, Small Interfering RNA Interference Strains Transgenes WAS protein, human

Retroviral Expression of Human OPA1 Isoforms

Cited 6 times

The eight isoforms of human OPA1 cDNA were amplified by PCR from first-strand cDNA and subcloned into the retroviral vector pMSCV-puro. Retrovirus production and infection were performed as described previously (Chen et al., 2003 (link)). Western blots of cell lysates were probed with an affinity-purified anti-OPA1 antibody raised against the C-terminal region of human OPA1 (gift of L. Griparic and A. van der Bliek, University of California, Los Angeles, Los Angeles, CA; Griparic et al., 2004 (link)).

Song Z., Chen H., Fiket M., Alexander C, & Chan D.C. (2007). OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. The Journal of Cell Biology, 178(5), 749-755.

Publication 2007

Antibodies, Anti-Idiotypic Cells Cloning Vectors DNA, Complementary Homo sapiens Infection OPA1 protein, human Protein Isoforms Retroviridae Western Blot

Most recents protocols related to «OPA1 protein, human»

Mitochondrial Dynamics Gene Expression

Expression levels of OPA1, SOD2 and Drp-1 genes were measured by RT-PCR. AGS cells were seeded (2 x 10⁶) in a 6-well plate and incubated at 37°C in a 5% CO₂ atmosphere overnight, until cell attachment. The next day, cells were incubated with Hpcf (1:2) for 3 hours in presence or not of HS-FEN 25 μg/mL. After incubation, RNA was extracted using TRIzol LS reagent (Thermo Fisher Scientific). Briefly, cells were lysed in 1 mL of Trizol reagent and incubated on ice for 5 minutes. 200 μL of chloroform were added and each sample was centrifuged at 13,000 rpm, 4°C for 15 minutes. The aqueous phase (upper phase) was transferred into a new tube and 500 μL of isopropanol were added. The mixture was then vortexed, incubated on ice for 5 minutes and centrifuged at 13,000 rpm, 4°C for 10 minutes. Supernatant was discarded and RNA pellet suspended using ethanol 75%. After centrifugation (13,000 rpm, 4°C for 7 minutes), supernatant was removed, and pellet eluted in 30 μL of RNase free water. The quality and quantity of RNA was assessed using NanoDrop 2000c (Thermo Fisher Scientific). cDNA was finally prepared using the high-capacity cDNA Reverse transcription kit (Thermo Fisher Scientific).
Real-time PCR reactions were performed on a StepOne Real-Time PCR System (Thermo Fisher Scientific), using Power SYBR Green PCR Master Mix (Applied Biosystem) as amplification system [37 ]. Gene-specific primers are listed in S2 Table. The 2^{- ΔΔCt} method was used to determinate relative changes in target gene expression. As housekeeping gene, GAPDH was used as internal control, to normalize data.

Verrillo M., Cuomo P., Montone A.M., Savy D., Spaccini R., Capparelli R, & Piccolo A. (2023). Humic substances from composted fennel residues control the inflammation induced by Helicobacter pylori infection in AGS cells. PLOS ONE, 18(3), e0281631.

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Publication 2023

Atmosphere Cell-Matrix Junction Cells Centrifugation Chloroform DNA, Complementary Endoribonucleases Ethanol GAPDH protein, human Gene Expression Genes Genes, Housekeeping Isopropyl Alcohol Oligonucleotide Primers OPA1 protein, human Reverse Transcriptase Polymerase Chain Reaction Reverse Transcription SOD2 protein, human SYBR Green I trizol

Pathway Analysis of Microglia and Astrocyte Subsets

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Publication 2023

ADORA2B protein, human ADRB1 protein, human ApoE protein, human Astrocytes ATP2A2 protein, human ATP2B3 protein, human ATP5B protein, human ATP8A2 protein, human B3GNT5 protein, human c-Mer Tyrosine Kinase C3AR1 protein, human CAMKII gamma protein, human cardiotrophin-like cytokine Caspase 3 CCR5 protein, human CHRM3 protein, human CRKL protein CSF1 protein, human CTSB protein, human CTSD protein, human CTSL protein, human CTSS protein, human CUL1 protein, human CYBB protein, human DNM1L protein, human DRD1 protein, human EGR1 protein, human EMP1 protein, human ENO2 protein, human Esterase Inhibitor, C1 FRAP1 protein, human Galectin 3 Gene, c-fms Genes GPR56 protein, human GZMB protein, human IGF1 protein, human IGFBP5 protein, human IL1A protein, human IL1B protein, human MAFB protein, human Metabolism Microglia Nitric Oxide Synthase Type II OPA1 protein, human PARP2 protein, human PDPK1 protein, human phosphoglycerate mutase 1, human PPP3CB protein, human PPP3R1 protein, human PRF1 protein, human PRKACB protein, human PRKCI protein, human PSMB8 protein, human PTGS2 protein, human PTK2B protein, human PTPN1 protein, human Receptor, Transforming Growth Factor-beta Type I SMAD3 protein, human SPARC protein, human SPI1 protein, human SPP1 protein, human STAT1 protein, human TGFB1 protein, human TICAM1 protein, human Tissue Inhibitor of Metalloproteinase-2 TJP1 protein, human TLR2 protein, human TREM2 protein, human VDAC1 protein, human

Flow cytometry analysis of lung cell subsets

Single-cell suspensions of the lung tissue were prepared for flow cytometry. In brief, lung tissue was incubated in collagenase I (1 mg/mL, Roche, Mannheim, Germany) at 37 °C with frequent agitation for 45 min. After all dissociation procedures, cells were washed with a dissociation medium, filtered through a 70-mesh and 40-mesh cell strainer, and centrifuged at 1200 rpm for 10 min. Cells were suspended in an ice-cold phosphate-buffered saline (PBS) buffer. Samples were stained using the following antibodies: Fixable viability stain 450, PE-conjugated CD64 (FcγRI), APC-Cy7-conjugated CD45 (30-F11), APC-conjugated CD11b, BV510-conjugated Siglec-F, PE/Cyanine7-conjugated F4-80, Brilliant violet 605-conjugated CD11c and CoraLite®488-conjugated MLKL monoclonal antibody. The information of those antibodies is shown in Table 1. The cells were washed with PBS, and the cytometry buffer was added. The cells were subjected to analysis using a BD FACS Verse (BD Biosciences, San Jose, CA, USA) flow cytometer and analyzed using FlowJo software (version 10, Tree Star Inc., San Jose, CA, USA).Table 1

Antibody sources and dilutions

Antibody	Source	Catalog	Dilution ratio
Primary antibodies for Western blotting
Rabbit anti-MLKL polyclonal antibody	Abcam	Ab172868	1:2000
Rabbit anti-phospho-MLKL phospho-S345 monoclonal antibody	Abcam	Ab196436	1:2000
Rabbit-anti-RIPK3 polyclonal antibody	Abcam	Ab62344	1:2000
Rabbit anti-phospho-RIPK3 phospho-S232 monoclonal antibody	Abcam	Ab195117	1:2000
Anti-IL-1β polyclonal antibody	R&D	AF-401-NA	1:2000
Anti-DRP1 antibody	Abcam	Ab184247	1:2000
Anti-p-DRP1 (phospho S616) antibody	CST	3455	1:2000
Rabbit-anti-TOM20 antibody	Proteintech	11802-1-AP	1:2000
Mouse-anti-OPA1 antibody	BD	612606	1:2000
Rabbit-anti-MFN2 antibody	Proteintech	12186-1-AP	1:2000
Rabbit-anti-MTFP1 antibody	Proteintech	14257-1-AP	1:1000
Rabbit-anti-PGAM5 antibody	Proteintech	28,445–1-AP	1:3000
Anti-BAX antibody	CST	2772	1:2000
Rabbit-anti-BCL2 antibody	Cohesion	CPA1095	1:1000
Rabbit-anti-caspase3 antibody	CST	9662	1:2000
Rabbit-anti-caspase6 antibody	CST	9762	1:2000
GSDMDC1 Antibody (H-11)	Santa Cruz	sc-393581	1:2000
Rabbit-anti-LC3A/B(D3U4C) antibody	CST	12741	1:2000
Rabbit-anti-Pink1 antibody	Abcam	Ab23707	1:1000
Rabbit-anti-beclin1 antibody	CST	3738	1:2000
Anti-mTOR monoclonal antibody	Proteintech	66888-1-lg	1:2000
Anti-phospho-mTOR (Ser2448) Antibody	Proteintech	67778-1-lg	1:2000
Rabbit-anti-EIF4E antibody	Proteintech	11149-1-AP	1:2000
Rabbit-anti-P-EIF4EBP1-S65 antibody	Proteintech	#12721	1:2000
Anti-α-tubulin monoclonal antibody	Servicebio	GB11200	1:10,000
Secondary antibodies for Western blotting
HRP-conjugated goat anti-rabbit IgG	SAB	#L3012-2	1: 5000
Goat anti-Mouse IgG	SAB	L3032	1: 5000
Primary antibodies for immunofluorescence
Rabbit anti-TOM20 polyclonal antibody	Proteintech	11802-1-AP	1: 200
CoraLite®488-conjugated MLKL antibody	Proteintech	CL488-66675	1: 300
Antibodies for Flow Cytometry
PE-conjugated CD64 (FcγRI)	BioLegend	139304	1:100
Fixable Viability Stain 450	BioLegend	562247	1:1000
APC-Cy7-conjugated CD45 (30-F11)	BioLegend	557659	1:100
BV510-conjugated Siglec-F	BioLegend	740158	1:100
APC-conjugated CD11b	BioLegend	101212	1:100
Brilliant Violet 605-conjugated CD11c	BioLegend	301636	1:100
PE/Cyanine7-conjugated F4-80	BioLegend	123114	1:100
CoraLite®488-conjugated MLKL antibody	Proteintech	CL488-66675	1: 200

Zhong W.J., Zhang J., Duan J.X., Zhang C.Y., Ma S.C., Li Y.S., Yang N.S., Yang H.H., Xiong J.B., Guan C.X., Jiang Z.X., You Z.J, & Zhou Y. (2023). TREM-1 triggers necroptosis of macrophages through mTOR-dependent mitochondrial fission during acute lung injury. Journal of Translational Medicine, 21, 179.

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Publication 2023

alpha-Tubulin Anti-Antibodies Antibodies BCL2 protein, human BECN1 protein, human Buffers Caspase 3 Caspase 6 Cells Collagenase, Clostridium histolyticum Common Cold Eukaryotic Initiation Factor-4E Flow Cytometry FRAP1 protein, human Goat Immunoglobulins Interleukin-1 beta ITGAM protein, human Lung mitofusin 2 protein, human Monoclonal Antibodies Mus OPA1 protein, human Phosphates Rabbits RIPK3 protein, human Saline Solution Sialic Acid Binding Immunoglobulin-like Lectins Stains Tissues Trees Viola

Mitochondrial Dynamics and Apoptosis Regulation in Liver Cells

The liver tissue and HepG2 cells were lysed by RIPA lysis solution (Beyotime, China) to extract the protein. The protein concentration was detected by BCA reaction kit. After quantitative analysis, the total protein was denatured in this study. SDS-Page gel was used for electrophoresis, electrophoresis apparatus (Bio-RAD, USA) was adjusted to 120 V for electrophoresis, PVDF membrane (Millipore, USA) was used for membrane transfer, and skim milk (Sigma, USA) for blocking. Primary antibodies (Abcam, UK): Sirt1 (1:1000; ab189494), optic atrophy 1 (Opa1, 1:1000; ab157457), mitofusin 2 (Mfn2, 1:1000; ab124773), Drp1 (1:1000; ab184247), NRF1 (1:1000; ab34682), mitochondrial transcription factor A (TFAM, 1:1000; ab252432; Abcam; UK), Bcl-2 (1:2000; ab182858), cleaved-caspase 3 (1:500; ab2302), BCL2-associated X protein (Bax, 1:1000; ab32503), cleaved-caspase 9 (1:2000; ab32539) and GAPDH (1:2500; ab9485) were then added overnight to incubate. The next day, goat anti-rabbit antibody (1:2000; ab288151) was incubated for 1 h with slow shaking at 25 °C. The immunoreactive bands were visualized by intensive chemiluminescent reagent. The gray value was analyzed by ImageJ software.

Hu Z., Zhang H., Wang Y., Li B., Liu K., Ran J, & Li L. (2023). Exercise activates Sirt1-mediated Drp1 acetylation and inhibits hepatocyte apoptosis to improve nonalcoholic fatty liver disease. Lipids in Health and Disease, 22, 33.

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Publication 2023

Antibodies Antibodies, Anti-Idiotypic Bax Protein BCL2 protein, human Caspase 3 Caspase 9 Electrophoresis GAPDH protein, human Goat Hep G2 Cells Liver Milk, Cow's mitofusin 2 protein, human OPA1 protein, human Optic Atrophy 1 polyvinylidene fluoride Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE Sirtuin 1 TFAM protein, human Tissue, Membrane Tissues

Mitochondrial Ultrastructural Proteomic Profiling

To determine the mitochondrial apoptotic, dynamic, antioxidative, energetic, and homeostatic properties, which are determined by the expression of caspase-3, dynamin-related protein-1 (Drp-1), optic atrophy protein-1 (OPA-1), nuclear factor erythroid 2-related factor-2 (Nrf-2), haloacid dehalogenase-like hydrolase domain containing-3 (HDHD-3), and mitogen-activated protein kinase (MAPK), respectively, electron microscopic study was performed. Fixed mitochondria were washed with SPB and then refixed with osmium-tetroxide for 1 h. The samples were dehydrated in grading ethanol, infiltrated in grading LR White resin (EMS, USA), embedded in LR White resin, polymerized at 65 °C for 24–48 h, and sectioned to a thickness of 100 nm. Then, immunogold labeling assays were performed on every section. The sections were blocked with 50 mM glycine and 5% bovine serum albumin (BSA; EMS, USA) and incubated for 1 h at room temperature with caspase-3, Drp-1, OPA-1, Nrf-2, HDHD-3, and MAPK antibodies. The sections were incubated with immunoglobulin (Ig) G conjugated with 10 nm gold particles (EMS, USA) for 1 h. Silver enhancement was performed using the Aurion R-Gent SE-EM kit (EMS, USA). The sections were stained with lead citrate and uranyl acetate and evaluated using a transmission electron microscope (TEM; HT7700, HITACHI, Tokyo, Japan). In addition, mitochondrial architecture was examined, and the proportion of normal mitochondria/field was calculated.

Rabiablok A., Hanboonkunupakarn B., Tuentam K., Fongsodsri K., Kanjanapruthipong T, & Ampawong S. (2023). High-Dose Primaquine Induces Proximal Tubular Degeneration and Ventricular Cardiomyopathy Linked to Host Cells Mitochondrial Dysregulation. Toxics, 11(2), 146.

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Publication 2023

Antibodies Antioxidants Apoptosis Biological Assay Caspase 3 Citrate DNM1L protein, human Electron Microscopy Ethanol GA-Binding Protein Transcription Factor Glycine Gold haloacid dehalogenase Homeostasis Hydrolase Immunoglobulin G LR white Mitochondria Mitochondrial Dynamics Mitogen-Activated Protein Kinases NFE2L2 protein, human OPA1 protein, human Osmium Tetroxide Serum Albumin, Bovine Silver Transmission Electron Microscopy uranyl acetate

Top products related to «OPA1 protein, human»

Pvdf membrane by Merck Group

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PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.

Anti opa1 by BD

Sourced in United States

Anti-OPA1 is a laboratory reagent used to detect and quantify the presence of the OPA1 protein, which is involved in the regulation of mitochondrial morphology and function. It is a tool for researchers studying mitochondrial dynamics and cellular processes related to OPA1.

β actin by Cell Signaling Technology

Sourced in United States, United Kingdom, China, Germany, Japan, Canada, Morocco, Sweden, Netherlands, Switzerland, Italy, Belgium, Australia, France, India, Ireland

β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is an important component of the microfilament system and is involved in various cellular processes such as cell motility, structure, and integrity.

Lipofectamine 2000 by Thermo Fisher Scientific

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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.

β actin by Santa Cruz Biotechnology

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β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is a component of the microfilament system and plays a crucial role in various cellular processes, such as cell motility, maintenance of cell shape, and intracellular trafficking.

Ab57602 by Abcam

Sourced in United States, United Kingdom

Ab57602 is a laboratory equipment product. It is designed for use in scientific research applications. The core function of this product is to [CORE FUNCTION DESCRIPTION].

Ab157457 by Abcam

Sourced in United Kingdom, United States

Ab157457 is a lab equipment product manufactured by Abcam. It is a core function laboratory device used for research purposes. No further details can be provided in an unbiased and factual manner.

Gapdh by Santa Cruz Biotechnology

Sourced in United States, United Kingdom, China, Germany, Canada, Morocco, Italy, Japan, France, Switzerland, Macao

GAPDH is a housekeeping gene that encodes the enzyme glyceraldehyde 3-phosphate dehydrogenase, which is involved in the glycolytic pathway. This enzyme catalyzes the oxidative phosphorylation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate.

Trizol reagent by Thermo Fisher Scientific

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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.

Anti drp1 by Cell Signaling Technology

Sourced in United States

Anti-DRP1 is a primary antibody that specifically binds to the dynamin-related protein 1 (DRP1), a key regulator of mitochondrial fission. This antibody can be used for the detection and analysis of DRP1 in various cell and tissue samples through techniques such as Western blotting, immunohistochemistry, and immunocytochemistry.

What is the OPA1 protein and what is its role in the body?

The OPA1 protein is a dynamin-like GTPase that plays a crucial role in mitochondrial dynamics. It is involved in the regulation of mitochondrial fusion, cristae organization, and apoptosis. Mutations in the OPA1 gene have been associated with autosomal dominant optic atrophy, a leading cause of inherited blindness. Understanding the function and regulation of OPA1 is essential for developing therapeutic approaches to mitochondrial disorders and neurodegenerative diseases.

How can PubCompare.ai help with OPA1 protein research?

PubCompare.ai allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to OPA1 protein, human for their specific research goals. The platform's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accruacy.

What are some common challenges in working with OPA1 protein?

One of the key challenges in working with OPA1 protein is ensuring reproducibility and accuracy in experimental protocols. Variations in protocol conditions, reagents, and techniques can significantly impact the results. Additionally, researchers may face difficulties in accessing relevant protocols from the literature, pre-prints, and patents, which can hinder progress in OPA1 protein studies.

Are there different variations or types of OPA1 protein?

Yes, there are different isoforms and variants of the OPA1 protein. These variations can arise due to alternative splicing or mutations in the OPA1 gene. The different isoforms of OPA1 may have distinct functionalities or subcellular localization, which can impact their role in mitochondrial dynamics and cellular processes. Understanding these variations is important for developing targeted theraputic approaches for mitochondrial disorders and neurodegenerative diseases.

What are some specific applications of OPA1 protein research?

OPA1 protein research has various applications, including: 1. Studying the role of mitochondrial dynamics in cellular function and disease pathogenesis. 2. Developing therapies for mitochondrial disorders, such as autosomal dominant optic atrophy, by targeting OPA1 function. 3. Investigating the link between OPA1 and neurodegenerative diseases, such as Parkinson's and Alzheimer's, to uncover new therapeutic avenues. 4. Utilizing OPA1 as a biomarker for early diagnosis and monitoring of mitochondrial-related diseases.

More about "OPA1 protein, human"

OPA1 (Optic Atrophy 1) is a crucial protein involved in mitochondrial dynamics, playing a central role in the regulation of mitochondrial fusion, cristae organization, and apoptosis.
Mutations in the OPA1 gene have been strongly associated with autosomal dominant optic atrophy (ADOA), a leading cause of inherited blindness.
Understanding the function and regulation of this dynamin-like GTPase is essential for developing therapeutic approaches to mitigate mitochondrial disorders and neurodegenerative diseases.
To optimize OPA1 protein research, an AI-driven platform like PubCompare.ai can be leveraged to facilitate access to relevant experimental protocols from scientific literature, preprints, and patents.
By utilizing AI-driven comparisons, researchers can identify the best protocols and products, enhancing reproducibility and accuracy in their OPA1 studies.
When conducting OPA1 experiments, researchers often employ techniques such as western blotting using PVDF membranes to analyze protein expression.
Antibodies like Anti-OPA1 and Anti-DRP1 (Dynamin-Related Protein 1) are commonly used to detect OPA1 and DRP1 proteins, respectively.
Loading controls like β-actin and GAPDH are frequently utilized to normalize protein levels.
Transfection reagents such as Lipofectamine 2000 can be employed to introduce genetic material, such as OPA1 constructs, into cells.
Additionally, RNA extraction using TRIzol reagent and subsequent analysis, such as qRT-PCR, can provide insights into OPA1 gene expression.
Immunohistochemistry using antibodies like Ab57602 and Ab157457 can also be valuable in visualizing the localization and distribution of OPA1 within cells and tissues.
By leveraging this AI-driven platform and incorporating these experimental techniques, researchers can optimize their OPA1 protein studies, leading to enhanced reproducibility, accuracy, and a deeper understanding of this crucial mitochondrial protein and its role in health and disease.