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Importins

Importins are a family of proteins that play a crucial role in the transport of macromolecules, such as proteins and RNA, across the nuclear membrane.
They act as shuttles, binding to their cargo inside the cytoplasm and then transporting them into the nucleus.
Importins recognize specific nuclear localization signals (NLS) on their cargo and facilitate their passage through the nuclear pore complex.
This process is essential for many cellular processes, including gene regulation, signal transduction, and cellular homeostasis.
Importins are divided into several subtypes, each with distinct cargo preferences and functions.
Understaning the dynamics and mechanisms of importins is crucial for researchers studying cellular trafficking, nuclear transport, and related biological pathways.
With PubCompare.ai, you can easily identify the latest protocols, preprints, and patents related to importins, optimizing your research workflow and discovering the most effective methodologies.

Most cited protocols related to «Importins»

1
Importin-α Binding Site Alignment
Cited 74 times
Based on recent studies on the binding sites of the importin-α [9 (link)], we created an alignment of our cNLS based on the major site of the importin (Figure 2). This alignment was run through HMMer [11 (link)] using HMMbuild and calibrated using HMMcalibrate. Using HMMsearch and a leave-one-out cross-validation [25 ], we assessed its predictive power. The leave-one-out cross-validation of the HMMer framework was done by removing all the characterized NLSs of one of the proteins from the alignment and then applying the above method on the protein.
Nguyen Ba A.N., Pogoutse A., Provart N, & Moses A.M. (2009). NLStradamus: a simple Hidden Markov Model for nuclear localization signal prediction. BMC Bioinformatics, 10, 202.
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Publication 2009
Binding Sites Importins Nuclear Localization Signals Proteins
2
Xenopus Egg Extracts for Nuclear Assembly
Cited 17 times

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Publication 2010
Antibodies Biotin Buffers Cell Nucleus Cycloheximide Embryo HEPES Importins Magnesium Chloride Metaphase Nuclear Import Proteins Recombinant Proteins Sperm Streptavidin Sucrose Xenopus laevis
3
SARS-CoV-2 Viral Load Quantification
Cited 13 times
Levels of SARS-CoV-2 viral load were quantified using the US CDC 2019-nCoV_N1 primers and probe set (Supplementary Table 3)36 . Virions were pelleted from respiratory secretions, swab fluids, plasma, or urine by centrifugation at approximately 21,000 × g for 2 h at 4 °C. The supernatant was removed and 750 µL of TRIzol-LS™ Reagent (ThermoFisher) was added to the pellets and then incubated on ice. Following incubation, 200 µL of chloroform (MilliporeSigma) was added and vortexed. The mixtures were separated by centrifugation at 21,000 × g for 15 min at 4 °C, and subsequently the aqueous layer was removed and treated with an equal volume of isopropanol (Sigma). GlycoBlue™ Coprecipitant (ThermoFisher) and 100 µL 3 M Sodium Acetate (Life Technologies) were added to each sample and incubated on dry ice until frozen. RNA was pelleted by centrifugation at 21,000 × g for 45 mins at 4 °C. The supernatant was discarded and the RNA was washed with cold 70% ethanol. The RNA was resuspended in diethyl pyrocarbonate-treated water (ThermoFisher).
Each reaction contained extracted RNA, 1× TaqPath™ 1-Step RT-qPCR Master Mix, CG (ThermoFisher), the CDC N1 forward and reverse primers, and probe36 . Viral copy numbers were quantified using N1 quantitative PCR (qPCR) standards in 16-fold dilutions to generate a standard curve. The assay was run in triplicate for each sample and two non-template control wells were included as negative controls. Quantification of the Importin-8 housekeeping gene RNA level was performed to determine the quality of respiratory sample collection. An internal virion control (RCAS) was spiked into each sample and quantified to determine the efficiency of RNA extraction and qPCR amplification37 (link). Concurrent analysis of results by this CDC N1 viral load assay showed high correlation with that of the Roche cobas SARS-CoV-2 ORF-1ab and E genes (Supplementary Fig. 4).
Fajnzylber J., Regan J., Coxen K., Corry H., Wong C., Rosenthal A., Worrall D., Giguel F., Piechocka-Trocha A., Atyeo C., Fischinger S., Chan A., Flaherty K.T., Hall K., Dougan M., Ryan E.T., Gillespie E., Chishti R., Li Y., Jilg N., Hanidziar D., Baron R.M., Baden L., Tsibris A.M., Armstrong K.A., Kuritzkes D.R., Alter G., Walker B.D., Yu X, & Li J.Z. (2020). SARS-CoV-2 viral load is associated with increased disease severity and mortality. Nature Communications, 11, 5493.
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Publication 2020
Biological Assay Centrifugation Chloroform Common Cold Diethyl Pyrocarbonate Dry Ice Ethanol Freezing Genes Genes, Housekeeping Importins Isopropyl Alcohol Oligonucleotide Primers Pellets, Drug Plasma Respiratory Rate Reverse Transcriptase Polymerase Chain Reaction SARS-CoV-2 Secretions, Bodily Sodium Acetate Specimen Collection Technique, Dilution trizol Urine Virion
4
Flexible Protein-Protein Docking Refinement
Cited 8 times
The FiberDock method refines soft rigid-docking solution candidates and re-ranks them in order to identify the near native models (21 (link)). The refinement takes into account both backbone and side-chain flexibility. The method combines a novel normal mode analysis (NMA) based backbone refinement with our previously developed side-chain optimization and rigid-body minimization method, FireDock (22 (link)).
The NMA is performed in a pre-processing stage. In this stage, the normal modes of the proteins are calculated using the anisotropic network model (ANM) (18 (link)).
The FiberDock algorithm, which is applied on each rigid-body solution candidate, includes four main stages:

Side-chain optimization: The side-chain flexibility of interface residues of both proteins is modeled by a rotamer library. The optimal combination of rotamers is found by an integer linear programming (ILP) technique (23 ).

NMA-based backbone refinement: The refinement performs up to 20 iterations which consist of the following steps: (i) The van der Waals (vdW) forces that the proteins apply on each other are calculated. (ii) The 10 normal modes with the best correlation to these forces are identified, and the backbone conformation of the proteins are minimized along these normal modes. (iii) Monte Carlo (MC) rigid-body minimization is performed. (iv) A score is calculated for the current result and the result is saved if it is better than the previous results.

Rigid-body MC minimization: The rigid-body orientation of the ligand is optimized by a MC technique, and a BFGS quasi-Newton minimization is performed in each MC cycle (24 ,25 ).

Ranking according to binding energy: This stage attempts to identify near-native solutions among the entire set of refined complexes. The calculated binding energy includes a variety of energy terms, such as desolvation energy [atomic contact energy(ACE)], vdW interactions, partial electrostatics, hydrogen and disulfide bonds, π-stacking, aliphatic interactions, and more.

The method was tested on a set of 20 protein–protein complexes in which the receptor's interface RMSD, between its bound and the unbound conformation, varies in the range of 0.59–6.08Å. The results showed that the method successfully models backbone movements that occur during molecular interactions, and that the inclusion of the backbone refinement stage improves both the accuracy and the ranking of near-native docking solution candidates (21 (link)). Figure 1 shows the FiberDock results of refining two docking models (from our test set) that are composed of an unbound conformation of the receptor and a bound conformation of a ligand, placed in a near-native orientation. The figure shows that in both cases FiberDock correctly models the backbone movement that is essential for generating a high-accuracy docking model with no steric-clashes.

FiberDock results of refining two docking models of complexes: (A) HIV-1 neutralizing antibody in complex with its V3 loop peptide antigen, PDB-ID: 1GGI and (B) Ran-Importin β, PDB-ID: 1IBR, which are composed of an unbound conformation of the receptor and a bound conformation of a ligand, placed in a near-native orientation. The unbound structure of the receptor (the starting conformation of the refinement) is colored in red and the bound complex structure is in blue. The predicted complex structure by FiberDock is in green. In both cases FiberDock correctly modeled the backbone movement (marked by arrows) that is essential for generating a high-accuracy docking model with no steric clashes. This image was produced using the UCSF Chimera package (26 (link)).

Mashiach E., Nussinov R, & Wolfson H.J. (2010). FiberDock: a web server for flexible induced-fit backbone refinement in molecular docking. Nucleic Acids Research, 38(Web Server issue), W457-W461.
Publication 2010
Anisotropy Antibodies, Neutralizing Antigens cDNA Library Chimera Disulfides Electrostatics HIV-1 HIV Antibodies Human Body Hydrogen Importins Ligands Movement Muscle Rigidity Nuclear Energy Peptides Proteins SET protein, human Vertebral Column
5
Plasmid Constructs for Skp2, Akt, and Related Proteins
Cited 8 times
FLAG.Skp2, HA.Skp2 and HA.Myr.Akt1 plasmids were described previously5 (link),45 (link). HA.Myr.Akt2 plasmid was purchased from Addgene. The first 90 amino acids of human Skp2 protein was fused in frame with the GST protein to create the pGEX.WT.human.Skp2 construct. Mouse Skp2 cDNA was amplified from a mouse cDNA library (kind gift from Dr. Ronald Depinho) using the Pfu polymerase (Stratagene). Full-length mouse Skp2 cDNA was subcloned into the pCMV-FLAG vector (Sigma) to create the FLAG.mouse.Skp2 construct and the first 90 amino acids of mouse Skp2 was fused in frame with the GST protein to create the pGEX.WT.mouse.Skp2 construct. Skp2 mutants were generated using the QuikChange XL Site-Directed Mutagenesis Kit (Stratagene). HA.Cdh1 construct was obtained from Dr. Peter Jackson. HA.S6K.CA and HA.S6K.KD constructs were obtained from Dr. John Blennis. HA.SGK.CA construct was a kind gift from Dr. Sussanne Conzen. The importin α1, importin α5 and importin α7 plasmids were obtained from the DF/HCC DNA Resource Core.
Gao D., Inuzuka H., Tseng A., Chin R.Y., Toker A, & Wei W. (2009). Phosphorylation by Akt1 Promotes Skp2 Cytoplasmic Localization and Impairs APC/Cdh1-mediated Skp2 Destruction. Nature cell biology, 11(4), 397-408.
Publication 2009
Acids AKT1 protein, human AKT2 protein, human Amino Acids CDH1 protein, human cDNA Library Cloning Vectors DNA, Complementary Homo sapiens Importins Mice, Laboratory Mutagenesis, Site-Directed Pfu DNA polymerase Plasmids Proteins Reading Frames SKP2 protein, human

Most recents protocols related to «Importins»

1
Generation and Characterization of NOSIP Constructs
Plasmids pEGFP-GST-NOSIP, pcDNA3.1(+)-NOSIP-HA and pMal-His-NOSIP-MBP (18 (link)), pMal-c2-TNPO1 (FL [aa 1–890],ΔC [aa 1–517], ΔN [aa 518–890]), pTYB2-S-His-importin β (ΔC [aa 1–396], ΔN [aa304–876]), pGEX-KG-GST-IBB and pGEX-4T1-GST-M9 (32 (link)), RanWT (42 (link)), pQE80-His-importin 13 (19 (link)), pQE80-RanQ69L (1–180) (43 (link)), pQE80-His-importin 7 (Xenopus laevis, obtained from R. Ficner (44 (link)), pQE32-His-TNPO1 (45 (link)), pQE60-His-CRM1 (46 (link)), pRSETb-His-importin α (47 (link)), pET30a-His-importin β (48 (link)), pXGmLnt-Rev-GR-GFP (21 (link)), pEGFP-c1-GFP-M9M and pEGFP-c1-GFP-Bimax2 (49 (link)), pEGFP-c1-Rev(47–116)-GFP2-cNLS (50 (link)) and pcDNA3-NES-mTagBFP2-cNLS (51 (link))) were described before.
The plasmid pEGFP-c1-GR(511–795)2-GFP2-MCS was generated by inserting two copies of the hormone-responsive fragment of rat glucocorticoid receptor via NotI and XhoI and XhoI and BcuI in front of GFP. A second GFP was inserted via BglII and Eco32I.
NOSIP fragments (aa 1–110, 1–160, 1–240, 111–240, 111–301, 75–102, 75–140, 75–180, 75–200) were amplified by PCR using pcDNA3.1(+)-NOSIP-HA as template and cloned via Gibson assembly into the pEGFP-GST vector. For tagged versions of NOSIP K78AK79A, site-directed mutagenesis was performed using oligonucleotides 5′-GTACATTCTGCACCAGGCGGCGGAGATTGCCCGGCAG and 5′-CTGCCGGGCAATCTCCGCCGCCTGGTGCAGAATGTAC using the corresponding wildtype plasmids as template. The coding sequence of NOSIP was amplified by PCR using NOSIP-HA as a template and cloned into pGEX-6P-1 via EcoRI and XhoI to generate GST-NOSIP, in pQLink-His via HindIII and NotI to obtain His-NOSIP and in pEGFP-C1-GR(511–795)2-GFP2-MCS using BglII and SalI and thereby replacing one GFP to obtain GR(511–795)2-GFP-NOSIP. pcDNA3-NES-mTagBFP2-M9 was generated by amplifying NES-mTagBFP2 by PCR using pcDNA3-NES-mTagBFP2-cNLS as template (51 (link)) and cloning it into pcDNA3 via EcoRI and EcoRV. The oligonucleotides 5′-AAAGATATCATGGGGAATTACAACAATCAGTCTTC and 5′-AAACTCGAGTCAATAGCCACCTTGGTTTCGTG were used to amplify the M9-sequence of hnRNPA1 and inserting it via EcoRV and XhoI into pcDNA3-NES-mTagBFP2 to obtain pcDNA3-NES-mTag-BFP2-M9. Plasmids coding for RFP-M9M and RFP-Bimax2 were obtained from Dr Dorothee Dormann (49 (link)).
Pörschke M., Rodríguez-González I., Parfentev I., Urlaub H, & Kehlenbach R.H. (2023). Transportin 1 is a major nuclear import receptor of the nitric oxide synthase interacting protein. The Journal of Biological Chemistry, 299(3), 102932.
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Publication 2023
Cloning Vectors Deoxyribonuclease EcoRI Importins Mutagenesis, Site-Directed NR3C1 protein, human Oligonucleotides Open Reading Frames Plasmids TNPO1 protein, human Xenopus laevis
2
Purification and complex formation of NTRs
For complex formation, His-NOSIP and purified NTRs were incubated in TPB at a molar ratio of 1:1 (except His-importin β:His-importin 7:His-NOSIP and His-importin α:His-importin β:NOSIP with a ratio of 1:1:3) in the presence or absence of a 3-fold molar excess of RanQ69L1−180-GTP for 1 to 2 h at 4 °C. Samples were cleared by centrifugation at 4 °C at 16,100g for 20 min and subjected to size exclusion chromatography using a Superdex S200 analytical increase 10/300 GL column (Cytiva) equilibrated in TPB. Fractions were analyzed by SDS-PAGE followed by Coomassie staining.
Pörschke M., Rodríguez-González I., Parfentev I., Urlaub H, & Kehlenbach R.H. (2023). Transportin 1 is a major nuclear import receptor of the nitric oxide synthase interacting protein. The Journal of Biological Chemistry, 299(3), 102932.
Full text: Click here
Publication 2023
Centrifugation Importins Molar Molecular Sieve Chromatography SDS-PAGE
3
Binding Assays for MBP and GST Proteins
For binding assays with MBP proteins, 100 pmol His-NOSIP-MBP or MBP was immobilized on 10 μl amylose beads (NEB Biotechnologies, E8022L) equilibrated in transport buffer containing 10 mg/ml ovalbumin or bovine serum albumin (Sigma) for 1 h at 4 °C under gentle agitation. After three washing steps with TPB containing 10 mg/ml ovalbumin, the beads were incubated with 100 pmol of purified NTR in the presence or absence of 300 pmol RanQ69L1−180-GTP for 3 h at 4 °C under gentle agitation in a total volume of 500 μl. To remove unbound proteins, beads were washed three times with TPB. Bound proteins were eluted in 4× SDS-sample buffer at 95 °C and analyzed by SDS-PAGE (4–12% NuPAGE, Invitrogen).
Binding assays using GST proteins were performed as described above, using 100 pmol GST, GST-IBB, GST-M9, or GST-NOSIP, immobilized on 10 μl glutathione Sepharose beads (Cytiva) and 100 pmol of respective proteins, as indicated.
For competition assays, 100 pmol His-S-importin β was immobilized on 10 μl S-protein beads (Cytiva) and incubated with 100 pmol His-NOSIP and increasing amounts of His-importin α (0, 100, 300, 1000 pmol) or the other way around. For assays with NTRs competing for binding sites on NOSIP, 100 pmol His-NOSIP-MBP was immobilized on amylose beads and incubated with 100 pmol of one and increasing amounts of the other NTR.
For binding assays with HeLa-cytosol, 600 pmol His-NOSIP-MBP was immobilized on 62.5 μl MBP-selector beads (Nanotag Biotechnologies) in TPB containing 10 mg/ml bovine serum albumin (BSA, Sigma) and 1 μg/ml each of leupeptin, pepstatin, and aprotinin (Sigma). After washing the beads 3 times with buffer, immobilized His-NOSIP-MBP was incubated with 200 μl HeLa-cytosol (Ipracell; 14,3 mg/ml) in the presence or absence of 2000 pmol RanQ69L1−180-GTP for 6 h at 4 °C under gentle rotation, followed by four washing steps with TPB. Bound proteins were eluted in 4× SDS-sample buffer at 95 °C and analyzed by SDS-PAGE (4–12% NuPAGE, Invitrogen) followed by Western blotting using the Odyssey system (LI-COR).
Pörschke M., Rodríguez-González I., Parfentev I., Urlaub H, & Kehlenbach R.H. (2023). Transportin 1 is a major nuclear import receptor of the nitric oxide synthase interacting protein. The Journal of Biological Chemistry, 299(3), 102932.
Full text: Click here
Publication 2023
Amylose Aprotinin Binding Proteins Binding Sites Biological Assay Buffers Cytosol Glutathione HeLa Cells Importins leupeptin Ovalbumin pepstatin Proteins SDS-PAGE Sepharose Serum Albumin, Bovine spike protein, SARS-CoV-2
4
Purification of Nuclear Transport Proteins
His-NOSIP was expressed in JM109 cells grown in LB medium and induced at an A600nm of 0.7 with 1 mM IPTG for 18 h at 18 °C. His-importin 13 was expressed in JM109 cells grown in 2× YT medium containing 30 mM K2HPO4 and 2% glycerol and induced at an A600nm of 0.7 with 0.5 mM IPTG for 16 to 18 h at 18 °C. His-Imp13 and His-NOSIP were purified using buffer A (50 mM Tris pH 7.4; 500 mM NaCl; 10 mM Mg(OAc)2; 5% glycerol; 10 mM β-mercaptoethanol; 1 μg/ml each of leupeptin, pepstatin, and aprotinin; and 0.1 mM PMSF) over Ni-NTA agarose (Qiagen), followed by size exclusion chromatography over a HiLoad 16/600 Superdex 200 prepgrade column (Cytiva) equilibrated in size exclusion chromatography buffer (50 mM Tris pH 7.4, 200 mM NaCl, 2 mM DTT). His-NOSIP-MBP was expressed in JM109 cells grown in LB medium to an A600nm of 0.7 and induced with 0.5 mM IPTG at 18 °C for 18 h. The protein was purified using Ni-NTA agarose beads (Qiagen), eluted with buffer A with 300 mM imidazole and further enriched over amylose resin (New England Biolabs) using buffer A containing 20 mM maltose for elution and dialyzed overnight at 4 °C against size exclusion chromatography buffer.
GST-NOSIP was expressed in JM109 cells grown in LB medium and induced with 0.5 mM IPTG at an A600nm of 0.7 for 4 h at 30 °C. Bacteria were lysed in buffer B (50 mM Na2HPO4/NaH2PO4, pH 8.0, 300 mM NaCl, 5 mM MgCl2, 10% glycerol, 10 mM β-mercaptoethanol) containing 1% Triton-X 100; 1 μg/ml each of leupeptin, pepstatin, and aprotinin; and 0.1 mM PMSF and purified over glutathione Sepharose beads using buffer B containing protease inhibitors as above, followed by size exclusion chromatography with a HiLoad 26/600 Superdex 200 prepgrade column (Cytiva) equilibrated in 20 mM Tris pH 7.4, 100 mM NaCl, and 2 mM DTT.
MBP-TNPO1 FL/ΔC/ΔN was expressed in BL21DE3 cells grown in LB medium for 3 h at 37 °C and induced at an A600 of 0.7 with 0.5 mM IPTG. MBP proteins were purified using amylose resin (New England Biolabs) in MBP buffer (20 mM Tris pH 7.5; 200 mM NaCl; 5% glycerol; 2 mM DTT; 1 μg/ml each of leupeptin, pepstatin, and aprotinin; and 0.1 mM PMSF) and separated by a HiLoad 26/600 Superdex 200 prepgrade column using an Äkta system (Cytiva) in transport buffer TPB; (20 mM Hepes, pH 7.3, 110 mM KOAc, 2 mM Mg(OAc)2, 1 mM EGTA, 2 mM DTT).
His-TNPO1 (45 (link)), His-CRM1 (46 (link), 52 (link)), His-Importin α (47 (link)), S-His-importin β (48 (link)), GST-M9 (32 (link)), RanQ69L1-180 (52 (link)), Ubc9 (53 (link)), and RanWT (42 (link)) were purified as described. RanQ69L (aa 1–180) was loaded with GTP as described (54 (link)). His-importin 5 was a gift from Achim Dickmanns.
Pörschke M., Rodríguez-González I., Parfentev I., Urlaub H, & Kehlenbach R.H. (2023). Transportin 1 is a major nuclear import receptor of the nitric oxide synthase interacting protein. The Journal of Biological Chemistry, 299(3), 102932.
Full text: Click here
Publication 2023
2-Mercaptoethanol Amylose Aprotinin Bacteria Buffers Cells Egtazic Acid Glutathione Glycerin HEPES imidazole Importins Isopropyl Thiogalactoside leupeptin Magnesium Chloride Maltose Molecular Sieve Chromatography pepstatin potassium phosphate, dibasic Protease Inhibitors Proteins Resins, Plant Sepharose Sodium Chloride TNPO1 protein, human Triton X-100 Tromethamine
5
Reconstituting Nuclear Import Reactions
Nuclear import reactions in permeabilized cells were essentially performed as described (59 (link)). Briefly, HeLa cells grown on poly-L-lysine (Sigma Aldrich)-coated coverslips were permeabilized with 0.005% digitonin in TPB containing 1 μg/ml each of leupeptin, pepstatin, and aprotinin for 5 min on ice. Transport reactions contained an ATP-regenerating system (1 mM ATP, 5 mM creatine phosphate, 20 U/ml creatine phosphokinase), 2 mg/ml BSA, 500 nM His-NOSIP-MBP, 4 μM RanWT, and 1 μM purified NTR (His-Importin 13, His-TNPO1, His-Importin 7, His-Importin β/7, His-importin β, or His-Importin α/β) or 1.4 mg/ml cytosol in a total volume of 40 μl. Reactions were incubated for 30 min at 30 °C or 4 °C in a humidity chamber, followed by three washing steps for 3 min each with ice-cold TPB and fixation with 3.7% formaldehyde in TPB for 10 min at 4 °C. His-NOSIP-MBP was visualized by indirect immunofluorescence with an antibody against MBP. After immunostaining, cells were mounted in Mowiol containing DAPI and analyzed by confocal microscopy using a 100× Plan-Neofluar 1.3 NA oil objective. Images were processed using Fiji and cell profiler (60 (link)) (version 4.2.1.).
Pörschke M., Rodríguez-González I., Parfentev I., Urlaub H, & Kehlenbach R.H. (2023). Transportin 1 is a major nuclear import receptor of the nitric oxide synthase interacting protein. The Journal of Biological Chemistry, 299(3), 102932.
Full text: Click here
Publication 2023
Aprotinin Cells Cold Temperature Creatine Kinase Cytosol DAPI Digitonin Formaldehyde HeLa Cells Humidity Immunoglobulins Importins Indirect Immunofluorescence leupeptin Lysine Microscopy, Confocal Nuclear Import pepstatin Phosphocreatine Poly A TNPO1 protein, human

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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.
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3
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4
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More about "Importins"

Importins are a family of crucial transport proteins that shuttle macromolecules, like proteins and RNA, across the nuclear membrane.
They recognize nuclear localization signals (NLS) on their cargo and facilitate their passage through the nuclear pore complex, enabling essential cellular processes such as gene regulation, signal transduction, and homeostasis.
Importins are divided into subtypes with distinct cargo preferences and functions.
Researchers studying cellular trafficking, nuclear transport, and related biological pathways can leverage tools like PubCompare.ai to easily identify the latest protocols, preprints, and patents related to importins.
This can help optimize research workflows and discover the most effective importin-related methodologies.
For example, techniques involving Lipofectamine 2000, Glutathione Sepharose 4B beads, Lipofectamine 3000, and the Cary Varian spectrofluorometer may be useful for studying importin dynamics and mechanisms.
Additionally, the 7900HT Fast Real-Time PCR System could aid in quantifying importin-mediated gene expression.
Importin-binding proteins like α-tubulin and the Ab2811 antibody may also be leveraged in importin research, while size-exclusion chromatography using a Superdex 200 16/60 column can help purify and characterize importin complexes.
By incorporating these related terms and techniques, researchers can gain a more comprehensive understanding of the importin system and accelerate their studies in this crucial area of cell biology.
One typo to note is 'experince' instead of 'experience' in the metadescription.