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Lamin Type A

Q: What are the key functions of Lamin Type A in the cell nucleus?

Lamin Type A is a structural protein that plays a crucial role in maintaining the integrity and shape of the cell nucleus. It is involved in important cellular processes such as DNA repair, transcription regulation, and cell signaling. Dysfunctions in Lamin A have been linked to various genetic disorders, including Progeria and muscular dystrophy.

Q: Are there different variations or types of Lamin A that researchers should be aware of?

Lamin A is part of the lamin family of proteins, which are important for the integrity and shape of the cell nucleus. While Lamin Type A is the primary focus, there are also other lamin subtypes, such as Lamin B, that researchers may need to consider depending on their specific area of study and the genetic disorders they are investigating.

Lamin Type A is a structural protein found in the cell nucleus.
It is part of the lamin family, which are important for maintaining the integrity and shape of the cell nucleus.
Lamin A plays a crucial role in cellular processes such as DNA repair, transcription regulation, and cell signaling.
Dysfunctions in Lamin A have been linked to a range of genetic disorders, including Progeria and various types of muscular dystrophy.
Researchers studying Lamin Type A can utilize PubCompare.ai's AI-powered platform to optimize their research protocols, locate the most reproducible and accuarate methods from literature, preprints, and patents, and streamline their research process.

Most cited protocols related to «Lamin Type A»

Lamin A Complementation in MEFs

Cited 28 times

A human lamin A cDNA was subcloned into the pTracer-CMV vector (Invitrogen Corp.). The linearized vector was transfected into lamin A/C −/− mouse embryonic fibroblasts (MEFs). Stable clones were selected using Zeocin, according to the manufacturer's instructions and the clones pooled. Subsequent analysis showed that the cells in the pool were heterogeneous with regard to lamin A expression.

Sullivan T., Escalante-Alcalde D., Bhatt H., Anver M., Bhat N., Nagashima K., Stewart C.L, & Burke B. (1999). Loss of a-Type Lamin Expression Compromises Nuclear Envelope Integrity Leading to Muscular Dystrophy. The Journal of Cell Biology, 147(5), 913-920.

Publication 1999

Clone Cells Cloning Vectors DNA, Complementary Embryo Fibroblasts Genetic Heterogeneity Homo sapiens Lamin Type A LMNA protein, human Mus Zeocin

Comprehensive Mapping of Lamin B1 and Lamin A in Multiple Cell Types

Cited 11 times

DamID maps of lamin B1 in mouse ESCs, ACs, NPCs, and MEFs were taken from Peric-Hupkes et al. (2010) (link), and of lamin B1 in human Tig3 fibroblasts from Guelen et al. (2008) (link). Coordinates of LADs in fly and worm were from van Bemmel et al. (2010) (link) and Ikegami et al. (2010) (link), respectively. For this study, we generated new DamID maps of lamin B1 in human ESCs and HT1080 cells and in mouse POU2F1^−/− and matching wild-type MEFs; and of lamin A in human HT1080 cells and in mouse NPCs and ACs.

Meuleman W., Peric-Hupkes D., Kind J., Beaudry J.B., Pagie L., Kellis M., Reinders M., Wessels L, & van Steensel B. (2013). Constitutive nuclear lamina–genome interactions are highly conserved and associated with A/T-rich sequence. Genome Research, 23(2), 270-280.

Publication 2013

Cells Enhanced S-Cone Syndrome Fibroblasts Helminths Homo sapiens Lamin Type A LMNB1 protein, human Microtubule-Associated Proteins Mus

Characterization of mTOR and Lipin 1 Signaling

Cited 11 times

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Publication 2011

Antibodies EIF4EBP1 protein, human FRAP1 protein, human Immunoglobulins Lamin Type A lipine LMNA protein, human Monoclonal Antibodies Muscle Tissue Rabbits SREBF1 protein, human

Measuring DNA Repair Pathways with Fluorescent Reporters

Cited 8 times

The direct repeat (DR)-GFP assay to measure the frequency of HR and the strand annealing EJ2-GFP assay to measure the frequency of MMEJ were performed as previously described^{30 (link)}. Briefly, U2OS DR-GFP or U2OS EJ2-GFP cells were transfected with 10 nM siRNA (Dharmacon) using Lipofectamine RNAiMAX (Invitrogen). 24 h later, the cells were transfected with the pCBASceI plasmid (Addgene #26477) and plasmids, using Lipofectamine 2000 (Invitrogen). 48 h post-plasmid transfection, the cells were trypsinized and the percentage of GFP-expressing cells was analyzed using the BD FACSCalibur flow cytometer.
The Lamin A (LMNA) assay to measure the frequency of introduction of the coding sequence for mClover at the 5’ end of LMNA using the CRISPR/Cas9 was performed as previously described^{12 (link)}. Parental or 53BP1Δ U2OS cell lines were transfected with the indicated plasmids using Lipofectamine RNAiMAX (Invitrogen). 24 h later, the cells were electroporated with 2.5 µg of sgRNA plasmids and 2.5 µg of donor template using a Nucleofector (Lonza; protocol X-001). Under those condition, omission of the sgRNA gives negligible levels of mClover-positive cells^{12 (link)}. Parental or 53BP1Δ U2OS cells stably expressing CtIP-T847E mutant were transfected with an siRNA against KEAP1 and the indicated plasmids and processed as previously described^{12 (link)}.
A FACS-based gene targeting assay was developed to monitor the targeting efficiency of a Zsgreen reporter at the 3’end of Hsp90 locus. A homology repair template plasmid was generated with the coding sequence of Zsgreen and homology arms (600 base pairs) that correspond to sequence flanking the Hsp90 STOP codon. MEFs transduced with AAV i53 and control cells expressing DM were co-transfected with a repair template plasmid and a plasmid expressing Cas9 (pX330-U6-Chimeric_BB-CBh-hSpCas9) and a gRNA (5’-CGATGAGGATGCCTCGCGCA-3’). One million cells were transfected with 200ng of Cas9/gRNA plasmid and 800ng of template plasmid using Lipofectamine 3000 (Invitrogen) according to the manufacturer’s instruction. 16 hours later, cells were selected with puromycin (2 µg/ml) for 48 hours to enrich for Cas9-expressing cells. To determine the percentage of Zsgreen positive cells, cells were by analyzed by flow cytometry using a FACS Aria III cell sorter 8 days post-transfection.
The HISTH2BK (H2B) targeting assay was adapted from ref²⁰ for use with Cas9 RNPs. For the targeting assay, 1.25 µg of plasmid donor was used per nucleofection.

Canny M.D., Moatti N., Wan L.C., Fradet-Turcotte A., Krasner D., Mateos-Gomez P.A., Zimmermann M., Orthwein A., Juang Y.C., Zhang W., Noordermeer S.M., Seclen E., Wilson M.D., Vorobyov A., Munro M., Ernst A., Ng T.F., Cho T., Cannon P.M., Sidhu S.S., Sicheri F, & Durocher D. (2017). Inhibition of 53BP1 favors homology-dependent DNA repair and increases CRISPR-Cas9 genome-editing efficiency. Nature biotechnology, 36(1), 95-102.

Publication 2017

Arm, Upper Biological Assay Cell Lines Cells Chimera Clustered Regularly Interspaced Short Palindromic Repeats Codon, Terminator Direct Repeat Flow Cytometry HSP90 Heat-Shock Proteins KEAP1 protein, human Lamin Type A Lipofectamine lipofectamine 2000 NRG1 protein, human Open Reading Frames Parent Plasmids Puromycin RBBP8 protein, human Ribonucleoproteins RNA, Small Interfering Tissue Donors Transfection

Modeling Human Neuromuscular Maturation In Vitro

Cited 6 times

It is clear that in both human development and in vitro, LMNs and UMNs require significantly more time for neurogenesis and maturation to occur than murine counterparts. Aside from apparent challenges such as increased time in culture, study length and cost, the ability of in vitro hPSC-derived cells to exhibit mature, native functional properties are crucial for accurate in vitro modeling of adult-onset diseases. An interesting approach to artificially accelerate the aging process genetically manipulates iPSC-derived neurons to express progerin, a mutated form of lamin A, that causes the premature aging disease Progeria^{129 (link)}. Upon progerin overexpression, iPSC-derived dopaminergic neurons exhibit age-associated changes, however the non-age related effects of artificial Lamin A expression in neurons is unknown. By interfering with Notch signaling, small molecule γ-secretase inhibitors, namely DAPT and Compound E, have been shown to accelerate neuronal differentiation by delaying G1/S phase long enough to commit neurons to neurogenesis^{130 (link), 131 (link)}. These inhibitors have been shown to be effective in hPSC-LMN protocols as well²⁵. While these compounds have proven useful in promoting cell cycle exit, the consequences of this treatment in MN diversity is unexplored. As different MN subtype fates emerge at distinct developmental timepoints in vivo, premature cell cycle exit could obstruct later MN subtype programs.
An alternate method to generate human MNs in vitro is described as induced-MNs (iMN)^{28 (link)}. This process circumvents reprogramming to pluripotency by directly converting patient somatic cells to MNs through transgenic expression of transcription factors that drive MN differentiation. By avoiding the epigenetic “reset” that occurs during reprogramming to pluripotency^{132 (link)}, this approach has been shown to maintain age-related epigenetic signatures accrued over the lifetime of the patient¹³³. iMNs display unique age-related cellular defects not observed in hPSC-MN approaches. However, these approaches are challenged by genomic instability resulting from increased somatic cell expansion requirements, as well as deficient MN maturation in vitro.
It is widely accepted that the maturation status of iPSC-derived cells remains a significant hurdle to the field of regenerative medicine at large, and yet it remains largely under-explored in humans^{4 (link)}. The ability to harness cell signaling to promote maturation in vitro, rests on increased understanding of anatomical, molecular and electrophysiological data from fetal, adult and aged human spinal post mortem tissue. Projects such as the Allen Brain Atlas provide valuable templates to guide anatomical- and genomic-level evaluation of native human MN maturation and aging. However, detailed functional data on human MNs are lacking and therefore, comparative evaluation of functional maturity relies largely upon the characterization of other mammalian species, often at cost to fidelity.

Sances S., Bruijn L., Chandran S., Eggan K., Ho R., Klim J., Livesey M., Lowry E., Macklis J., Rushton D., Sadegh C., Sareen D., Wichterle H., Zhang S, & Svendsen C. (2016). Modeling ALS using motor neurons derived from human induced pluripotent stem cells. Nature neuroscience, 19(4), 542-553.

Publication 2016

1,2-dilinolenoyl-3-(4-aminobutyryl)propane-1,2,3-triol Adult Animals, Transgenic Autopsy Brain Cell Cycle Cellular Senescence Cortisone Diploid Cell Dopaminergic Neurons Fetus G1 Phase Genome, Human Genomic Instability Homo sapiens Human Development Induced Pluripotent Stem Cells inhibitors Lamin Type A Lateral meningocele syndrome Mammals Mus Neurogenesis Neurons Patients Premature Birth REST protein, human Secretase Tissues Transcription Factor

Most recents protocols related to «Lamin Type A»

Protein Expression Analysis of HBS1L

According to the manufacturer’s protocol, approximately 1X10⁶ erythroid cells were collected for protein extraction by NE-PER (Nuclear and Cytoplasmic Extraction Kit (Thermo Fisher Scientific, Inc, MA, USA). Protein concentrations were measured by Quick Start Bradford Protein Assay (Bio-Rad Laboratories, Inc.). The extracts were electrophoresed onto 12% SDS-polyacrylamide gel, transferred to polyvinylidene difluoride (PVDF) membrane, and blocked with 5% skim milk. The membranes were reacted with HBS1L specific primary antibody (NBP1-85123; Novus Biologicals, CO, USA), followed by goat anti-rabbit secondary antibody conjugated with horseradish peroxidase (ab97051; Abcam, Cambridge, UK). Enhanced chemiluminescence (ECL; Amersham GE Healthcare, Little Chalfont, UK) was utilized as a substrate for protein visualization by Azure^™ c400 Imaging System (Azure Biosystems, Inc., CA, USA). Anti-actin (ab49900) 1:50,000 (Abcam^®, Cambridge, UK) and anti-lamin A (L1293) 1:5000 (Sigma-Aldrich, Inc., MO, USA) were utilized as cytoplasmic and nuclear loading controls, respectively.

Chumchuen S., Sripichai O., Jearawiriyapaisarn N., Fucharoen S, & Peerapittayamongkol C. (2023). Induction of fetal hemoglobin: Lentiviral shRNA knockdown of HBS1L in β0-thalassemia/HbE erythroid cells. PLOS ONE, 18(3), e0281059.

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Publication 2023

Actins Antibodies, Anti-Idiotypic Azure A Biological Assay Biological Factors Chemiluminescence Cytoplasm Erythroid Cells Goat Horseradish Peroxidase Immunoglobulins Lamin Type A Milk, Cow's Novus polyacrylamide gels polyvinylidene fluoride Proteins Rabbits Tissue, Membrane

Mitochondrial Function and Oxidative Stress

Cells were grown on high precision cover glass until desired confluency, fixed, permeabilized, stained with antibodies specific for cGAS and Lamin A and imaged as specified in Additional file 1: Methods.
Analysis of mitochondrial membrane potential and reactive oxygen species.
Mitochondrial membrane potential (MMP) and production of reactive oxygen species (ROS) were assessed as described in Additional file 1: Methods.

Lamsal A., Andersen S.B., Johansson I., Vietri M., Bokil A.A., Kurganovs N.J., Rylander F., Bjørkøy G., Pettersen K, & Giambelluca M.S. (2023). Opposite and dynamic regulation of the interferon response in metastatic and non-metastatic breast cancer. Cell Communication and Signaling : CCS, 21, 50.

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Publication 2023

Antibodies Cells Chromogranin A Lamin Type A Membrane Potential, Mitochondrial Reactive Oxygen Species

Immunoblotting Antibody Optimization Protocol

Immunoblotting was performed as previously described (23 (link)). The antibodies used in this study were as follows: mouse anti-GAPDH antibody (1:20,000; Santa Cruz; sc-32233), mouse anti-α-SMA antibody (1:10,000; Thermo; MS-113-P), rabbit anti-SM22α antibody (1:4000; Abcam; ab14106), rabbit anti-Col1a1 antibody (1:4,000, CST; 72,026), rabbit anti-β-actin antibody (1:4000; Proteintech; 20536-1-AP), rabbit anti-Mkl1 antibody (1:4000; Proteintech; 21166-1-AP), rabbit anti-lamin A/C antibody (1:4000; Proteintech; 10298-1-AP), rabbit anti-SOX9 antibody (1:4000; abcam; ab185230), horseradish peroxidase (HRP)-conjugated anti-FLAG primary antibody (1:10,000; Sigma Aldrich; A8592), horseradish peroxidase (HRP)- conjugated anti-HA primary antibody (1:5000; Roche; 12013819001), HRP-conjugated anti-mouse IgG secondary antibody (1:10,000; Abcam; ab6789), HRP-conjugated anti-rabbit IgG secondary antibody (1:10,000; Abcam; ab6721), HRP-conjugated anti-rabbit IgG secondary antibody (1:10,000; Santa Cruz; sc-2004), and HRP-conjugated anti-rabbit IgG secondary antibody (1:2000; CST; 7074).

Hironaka T., Takizawa N., Yamauchi Y., Horii Y, & Nakaya M. (2023). The well-developed actin cytoskeleton and Cthrc1 expression by actin-binding protein drebrin in myofibroblasts promote cardiac and hepatic fibrosis. The Journal of Biological Chemistry, 299(3), 102934.

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Publication 2023

Actins anti-c antibody anti-IgG Antibodies Antibodies, Anti-Idiotypic GAPDH protein, human Horseradish Peroxidase Immunoglobulins Lamin Type A LMNA protein, human megakaryocytic acute leukemia protein, human Mice, House Rabbits SOX9 protein, human

Immunofluorescence Staining of Cytoskeletal Proteins

Cells were fixed in 4% paraformaldehyde (Santa Cruz Biotechnology, Dallas, Texas), dissolved in PBS for 15 min, and rinsed in PBS twice. Three hundred microliters of permeabilization solution (0.1% Triton‐X‐100 in PBS) was then added to permeabilize the cells. After 15 min, the permeabilization solution was aspirated, and the cells were blocked using 10% goat serum in PBS for 30 min. Following this, the cells were incubated with either the anti‐lamin A/C primary antibody or the anti‐paxillin antibody (Abcam, Cambridge, United Kingdom) dissolved in antibody dilution buffer (0.3% Triton‐X‐100 and 1% BSA in PBS) at a ratio of either 1:200 (for lamin) or 1:500 (for paxillin) for either 2 h at 37 °C (for lamin) or 16 h at 4 °C (for paxillin). After the incubation period, the secondary antibody Alexa Fluor 647 goat anti‐mouse (Invitrogen, Carlsbad, CA) was diluted in the antibody dilution buffer at the ratio of 1:500 and added to the wells for lamin. For paxillin, the secondary antibody Alexa Fluor 488 goat anti‐rabbit (Invitrogen) was diluted in the antibody dilution buffer at a ratio of 1:350 and added to the wells. For imaging the filamentous actin for the stress fiber angle measurements, no primary antibody was added to the well. In this case, after permeabilization, rhodamine‐phalloidin (Abcam) was dissolved in the antibody dilution buffer at the ratio of 1:80 and added directly to the well. After immunochemistry, the samples were stored in a dark place for 45 min, followed by 3 PBS washes. Finally, the nuclei were counterstained with 300 nm of DAPI (Invitrogen) for 15 min. The scaffolds were kept hydrated in 2 ml of PBS and imaged using a 63× (water‐based immersion) magnification.

Mukherjee A., Ron J.E., Hu H.T., Nishimura T., Hanawa‐Suetsugu K., Behkam B., Mimori‐Kiyosue Y., Gov N.S., Suetsugu S, & Nain A.S. (2023). Actin Filaments Couple the Protrusive Tips to the Nucleus through the I‐BAR Domain Protein IRSp53 during the Migration of Cells on 1D Fibers. Advanced Science, 10(7), 2207368.

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Publication 2023

alexa fluor 488 Alexa Fluor 647 anti-c antibody Antibodies, Anti-Idiotypic Buffers Cell Nucleus Cells DAPI F-Actin Goat Immunoglobulins Lamins Lamin Type A LMNA protein, human Mus paraform PXN protein, human Rabbits rhodamine-phalloidin Serum Stress Fibers Submersion Technique, Dilution Triton X-100

Subcellular Protein Fractionation and Analysis

Nuclear and Cytoplasmic fractions extracted from each cell using the ProteoExtract Subcellular Proteome Extraction Kit (Calbiochem, San Diego, CA, USA) were appreciated by immunoblotting, as reported previously (6 (link)). The following primary antibodies were used: anti-HIF-1α antibody (#3716), anti-phospho-ABL1 antibody (#2865), anti-ABL1 antibody (#2862), anti-phospho-MET antibody (#3126), anti-MET antibody (#4560), anti-phospho-JNK antibody (#3073), anti-JNK antibody (#9252), anti-phospho-Akt antibody (#9271), anti-Akt antibody (#9272), anti-phospho-ERK1/2 antibody (#3073), anti-ERK1/2 antibody (#4370) (Cell Signaling Technology, Beverly, MA, USA), anti-β-actin antibody (A2228, clone AC-74) (Sigma-Aldrich, St Louis, MO, USA), and anti-Lamin A/C antibody (sc-7293) (Santa Cruz Biotechnologies, CA, USA).

Tsubaki M., Takeda T., Matsuda T., Kimura A., Tanaka R., Nagayoshi S., Hoshida T., Tanabe K, & Nishida S. (2023). Hypoxia-inducible factor 1α inhibitor induces cell death via suppression of BCR-ABL1 and Met expression in BCR-ABL1 tyrosine kinase inhibitor sensitive and resistant chronic myeloid leukemia cells. BMB Reports, 56(2), 78-83.

Publication 2023

Actins anti-c antibody Antibodies Antibodies, Anti-Idiotypic Clone Cells Cytoplasm Lamin Type A LMNA protein, human Mitogen-Activated Protein Kinase 3 Proteome

Top products related to «Lamin Type A»

Lamin a by Santa Cruz Biotechnology

Sourced in United States

Lamin A is a protein that is a structural component of the cell nucleus. It plays a role in the organization and maintenance of the nuclear envelope. Lamin A is involved in various cellular processes, including DNA repair, chromatin organization, and gene expression regulation.

Lamin a by Abcam

Sourced in United States, United Kingdom

Lamin A is a structural protein that is a component of the nuclear lamina, a fibrous layer on the inner side of the nuclear envelope of eukaryotic cells. It provides mechanical support and organization to the nucleus.

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.

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.

Fetal bovine serum (fbs) by Thermo Fisher Scientific

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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.

Ab26300 by Abcam

Sourced in United Kingdom, United States

Ab26300 is a laboratory equipment product. It serves a core function in scientific research, but a detailed description cannot be provided while maintaining an unbiased and factual approach.

Anti lamin a by Abcam

Sourced in United States, United Kingdom

Anti-Lamin A is a lab equipment product that is used to detect the presence of the Lamin A protein in biological samples. Lamin A is a structural protein that is an important component of the cell nucleus. Anti-Lamin A can be used in various research applications to study the expression and localization of Lamin A in cells and tissues.

Anti lamin a by Santa Cruz Biotechnology

Sourced in United States

Anti-Lamin A is a laboratory reagent produced by Santa Cruz Biotechnology. It is a monoclonal antibody that specifically binds to Lamin A, a structural protein found in the cell nucleus. The primary function of this product is to facilitate the detection and study of Lamin A in various cellular and molecular biology applications.

β actin by Merck Group

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β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.

Lamin a by Merck Group

Sourced in United States

Lamin A is a structural protein found in the cell nucleus. It is a component of the nuclear lamina, a scaffold-like structure that provides mechanical support and regulates gene expression within the nucleus.

What are the key functions of Lamin Type A in the cell nucleus?

How can researchers optimize their studies on Lamin Type A?

PubCompare.ai's AI-powered platform can help researchers studying Lamin Type A optimize their research protocols. The platform allows you to screen protocol literature more efficiently, leveraging AI to pinpoint critical insights. This can help you identify the most effective protocols related to Lamin Type A for your specific research goals, enabling you to choose the best option for reproducibility and accuracy.

Are there different variations or types of Lamin A that researchers should be aware of?

What are some common applications of Lamin Type A research?

Research on Lamin Type A is crucial for understanding a range of genetic disorders, including Progeria and various types of muscular dystrophy. By studying the dysfunctions and mutations in Lamin A, researchers can gain insights into the underlying mechanisms of these diseases and explore potential therapeutic interventions. Additionally, Lamin A's role in cellular processes like DNA repair and transcription regulation makes it an important area of study for cell biology and developmental biology.

How can PubCompare.ai help researchers streamline their Lamin Type A studies?

PubCompare.ai's AI-powered platform can greatly assist researchers studying Lamin Type A. The platform allows you to screen protocol literature more efficently, leveraging AI to pinponit critical insights. This can help you identify the most reproducible and accurate methods from literature, preprints, and patents, enabling you to choose the best protocols for your specific research goals and streamline your overall research process. The platform's intelligent comparisons can highlight key differences in protocol effectiveness, ensuring you select the optimal approach for your Lamin Type A studies.

More about "Lamin Type A"

Lamin Type A, also known as LMNA, is a crucial structural protein found within the cell nucleus.
It belongs to the lamin family, which play a vital role in maintaining the integrity and shape of the cell nucleus.
Lamin A is essential for various cellular processes, including DNA repair, transcription regulation, and cell signaling.
Dysfunctions in Lamin A have been linked to a range of genetic disorders, such as Progeria and different types of muscular dystrophy.
Researchers studying Lamin Type A can utilize PubCompare.ai's AI-powered platform to optimize their research protocols, locate the most reproducible and accurate methods from literature, preprints, and patents, and streamline their research process.
This platform can help identify the best protocols and products, improving the efficiency and accuracy of your Lamin A-related experiments.
When investigating Lamin A, researchers may also need to consider related topics such as PVDF membranes, which are commonly used for protein detection and Western blotting.
Lipofectamine 2000, a transfection reagent, can be useful for introducing genetic material into cells to study Lamin A's functions.
Additionally, fetal bovine serum (FBS) is often used as a supplement in cell culture media to support cell growth and survival.
Antibodies, such as the Anti-Lamin A antibody (Ab26300), can be employed to detect and quantify Lamin A expression in various experimental settings.
The use of β-actin as a housekeeping gene or loading control is also common in Lamin A-related studies, as it helps normalize protein expression levels.
By leveraging the insights and tools provided by PubCompare.ai, researchers can streamline their Lamin Type A studies, optimize their protocols, and uncover the most reliable and accurate methods from the available literature, preprints, and patents.
This AI-powered approach can significantly enhance the efficiency and reproducibility of your Lamin A research, ultimately leading to more robust and impactful findings.