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Leucine Zippers

Leucine Zippers are a structural motif found in certain proteins, characterized by a repeating pattern of leucine residues that facilitate protein-protein interactions.
These specialized domains play a crucial role in the dimerization and activation of various transcription factors, enabling them to bind to DNA and regulate gene expression.
Understanding the mechanics of Leucine Zippers is essential for researchers investigating cellular signaling pathways, gene regulation, and protein folding.
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Most cited protocols related to «Leucine Zippers»

1
Coiled-Coil Interaction Modeling and Design
Cited 23 times
Structure-based modelling of coiled-coil interactions was done as previously described, with modifications detailed in the Methods and Supplementary Information26 (link). Using the technique of cluster expansion, structure-based models were converted to functions of sequence that included constant, single-residue and residue-pair terms. Training of the cluster expansion used 61,780 random bZIP-like sequences that were modelled structurally28 (link), 29 (link). A limited amino-acid alphabet was considered, which included the 10 residues most frequently found at each coiled-coil heptad position in native bZIPs. Constrained optimization employing integer linear programming (ILP) was used to design a, d, e and g sites. ILP optimization minimized the energy of design•target complexes, subject to constraints on the energy gap with respect to undesired complexes and the match of the design sequence to a position-specific scoring matrix derived from 432 native bZIP leucine zippers. Other positions in the coiled-coil repeat (b, c and f positions) were chosen to be consistent with the designed interface a, d, e and g residues, using a probabilistic framework. For each design target, the ILP optimization was repeated with increasing values of the specificity gap parameter Δ, in a procedure termed a specificity sweep. Sequences for experimental testing were selected manually from candidates generated using the specificity sweeps.
For experimental testing, His6-tagged peptides were expressed in RP3098 cells and purified by Ni-NTA followed by reverse-phase HPLC. Coiled-coil microarrays were printed, processed and probed as described previously4 (link). Fluorescence signals from the arrays were processed to remove background and normalized. Circular dichroism measurements were performed using standard techniques to measure spectra between 195 and 280 nm at 25 °C or thermal stability by monitoring ellipticityat 222 nm. Data were fit to appropriate thermodynamic equations to obtain apparent Tms. Detailed descriptions of all procedures are included in the Methods and the Supplementary Information.
Grigoryan G., Reinke A.W, & Keating A.E. (2009). Design of protein-interaction specificity affords selective bZIP-binding peptides. Nature, 458(7240), 859-864.
Publication 2009
Amino Acids Cells Circular Dichroism Fluorescence High-Performance Liquid Chromatographies Leucine Zippers Microarray Analysis Peptides
2
Engineered LINE-1 Expression Constructs
Cited 12 times
The following plasmids are based on the previously described pJM101/L1.3 and pDK101 constructs [4] (link), [16] (link). The amino acid and nucleotide numbers indicate the mutation position based on L1.3 accession number L19088 [63] (link). The constructs were cloned into the pCEP4 expression vector (Invitrogen) and contain the mneoI indicator cassette [32] (link), [47] (link) in the L1 3′UTR unless otherwise indicated. PCR followed by subcloning was used to introduce the respective epitope tag sequences onto the 3′ end of ORF2. As a result of this procedure, we deleted a portion of the L1 3′UTR (nts 5818 to 5953). Oligonucleotides used in our cloning strategies are available upon request.
pADO2Tt contains a Tandem Affinity Purification epitope tag (TAP tag) [43] (link) on ORF2p and was cloned from the pZome-1-C vector (Euroscarf).
pAD2TE1 is derived from pDK101 (L1.3) [16] (link) and contains both the T7 gene 10 epitope tag on the carboxyl-terminus of ORF1p and a TAP tag on the carboxyl-terminus of ORF2p.
pAD2TE1-Δ2 is derived from pAD2TE1, but lacks CMV promoter and SV40 polyadenylation signal present in the original pCEP4 vector.
pAD2TE1-NT is identical to pAD2TE1, but lacks the mneoI indicator cassette.
pES2TE1 is identical to pAD2TE1, but contains a tandem affinity FLAG-HA tag on the carboxyl-terminus ORF2p [44] (link).
pAD500 is derived from L1.3ΔORF1NN [37] (link), and contains a TAP tag on the carboxyl-terminus of ORF2p.
pADL1MT is derived from pJM101/L1.3 and contains 24 repeats of the MS2 stem-loop (MS2 tag) upstream of the mneoI indicator cassette in the L1 3′UTR. The MS2 repeats were subcloned from the pTRIP vector [64] (link).
pAD3TE1 is identical to pAD2TE1, but contains the MS2 tag in the 3′UTR (at the same position as in pADL1MT).
pADO1S is identical to pAD2TE1, but contains three stop codons in ORF1. The first two stop codons (R7Stop; K8Stop) were generated by introducing a thymidine at nucleotide position 928 to create a frameshift mutation and by mutating an A to a T at nucleotide position 930. The third stop codon is from the construct pJM108/L1.3 carrying the mutation S119Stop [19] (link), [32] (link).
pADLZC is identical to pAD2TE1, but contains four leucine to valine mutations (L93,100,107,114V) in the ORF1p putative leucine zipper domain.
pAD102 is identical to pAD2TE1, but contains the REKG235–238AAAA mutations in the ORF1p RRM domain [16] (link), [32] (link).
pAD105 is identical to pAD2TE1, but contains the RR261–262AA mutations in the ORF1p C-terminal domain [16] (link), [19] (link), [32] (link).
pAD106 is identical to pAD2TE1, but contains the RR261–262KK mutations in the ORF1p C-terminal domain [16] (link).
pAD107 is identical to pAD2TE1, but contains the RR261–262KR mutation in the ORF1p C-terminal domain [16] (link).
pAD113 is identical to pAD2TE1, but contains the NLR157–159ALA mutations in the ORF1p RRM domain [31] (link).
pAD116 is identical to pAD2TE1, but contains the YPAKLS282–287AAAALA substitution in the ORF1p C-terminal domain [16] (link), [32] (link).
pAD135 is identical to pAD2TE1, but contains the D702A mutation in the putative ORF2p RT active site [19] (link).
pAD136 is identical to pAD2TE1, but contains the H230A mutation in the ORF2p EN domain [19] (link).
pAD162 is identical to pAD2TE1, but contains the CWWDC1143–1147SWWDS mutations in the ORF2p C-domain [32] (link).
pADL/R is identical to pAD2TE1, but contains a putative leucine zipper domain as well as a C-terminal domain mutant (L93,100,107,114V; RR261–262AA) in ORF1p.
pADL/C is identical to pAD2TE1, but contains a putative leucine zipper domain mutation (L93,100,107,114V) in ORF1p as well as a C-domain mutation (CWWDC1143–1147SWWDS) in ORF2p.
LZC is derived from pDK101 and contains four leucine to valine mutations (L93,100,107,114V) in the ORF1p putative leucine zipper domain.
LZ1/2 is derived from pDK101 and contains two leucine to valine mutations (L93,100V) in the ORF1p putative leucine zipper domain.
LZ2/3 is derived from pDK101 and contains two leucine to valine mutations (L100,107V) in the ORF1p putative leucine zipper domain.
LZ3/4 is derived from pDK101 and contains two leucine to valine mutations (L107,114V) in the ORF1p putative leucine zipper domain.
pDK101,pDK102,pDK105,pDK106,pDK107,pDK108,pDK116,pDK135,and pDK500 were described previously [16] (link).
pMS2-GFP-nls, pMS2-CFP, and pTRIP were generous gifts from Edouard Bertrand [64] (link)–[66] (link).
pAgo2-GFP and pDCP1α-GFP were generous gifts from Gregory Hannon [54] (link).
pG3BP-GFP was a generous gift from Jamal Tazi [53] (link).
Doucet A.J., Hulme A.E., Sahinovic E., Kulpa D.A., Moldovan J.B., Kopera H.C., Athanikar J.N., Hasnaoui M., Bucheton A., Moran J.V, & Gilbert N. (2010). Characterization of LINE-1 Ribonucleoprotein Particles. PLoS Genetics, 6(10), e1001150.
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Publication 2010
Amino Acids Cloning Vectors Codon, Terminator Epitopes Frameshift Mutation Genes Gifts Leucine Leucine Zippers Mutation Nucleotides Oligonucleotides Plasmids PMS2 protein, human Polyadenylation Simian virus 40 Stem, Plant Tandem Affinity Purification Thymidine Valine
3
Soluble Biotinylated CD1b Monomers Production
Cited 8 times
Soluble biotinylated CD1b monomers were produced in lentivirus-transduced HEK293 T cells by the National Institutes of Health Tetramer Core Facility (Emory University, Atlanta, GA) and tetramerized with fluorescently labeled streptavidin. In brief, human β-2-microglobulin and the extracellular domain of CD1b were cloned into the expression vector pCMJJ4 (gift from J. Jacob, Emory University, Atlanta, GA). Lentiviral particles were made in a second generation packaging system (Naldini et al., 1996 (link)). The light and heavy chains are expressed under control of the CMV promoter and are separated by the 2A-TaV peptide to generate two separate proteins from a single mRNA. The chains are followed by a C-terminal acidic or basic leucine zipper which stabilizes the complex and is used for affinity purification using the 2H11 monoclonal antibody (E. Reinherz, Harvard, Boston, MA). Purified monomers were enzymatically biotinylated at the BirA site at the C terminus of the heavy chain. Monomer purity and composition were confirmed by PAGE, and biotinylation was confirmed by streptavidin bead pulldown assay. Functional activity was assayed by affixing biotinylated monomers at final concentration of 5 µg/ml onto 96-well streptavidin plates (Thermo Fisher Scientific) in PBS, pH 7.4, for 24 h at 37°C. Lipid antigens were sonicated in PBS for 2 min, added to the wells, and incubated for 24 h at 37°C before washing three times with 200 µl/well sterile PBS. 105 LDN5 cells were added in a total volume of 200 µl T cell medium per well (RPMI). The plate was incubated for 24 h at 37°C after which culture supernatants were collected for HT2 bioassay.
Kasmar A.G., van Rhijn I., Cheng T.Y., Turner M., Seshadri C., Schiefner A., Kalathur R.C., Annand J.W., de Jong A., Shires J., Leon L., Brenner M., Wilson I.A., Altman J.D, & Moody D.B. (2011). CD1b tetramers bind αβ T cell receptors to identify a mycobacterial glycolipid-reactive T cell repertoire in humans. The Journal of Experimental Medicine, 208(9), 1741-1747.
Publication 2011
Acids Antigens BETA MICROGLOBULIN 2 Biological Assay Biotinylation Cells Chromatography, Affinity Cloning Vectors Homo sapiens Lentivirus Leucine Zippers Light Lipids Monoclonal Antibodies Peptides RNA, Messenger Staphylococcal Protein A Sterility, Reproductive Streptavidin T-Lymphocyte Tetrameres
4
Computational Protein NMR Parameters
Cited 6 times
Backbone scalar coupling constants were calculated using published Karplus relationships (53 ) for 3JHNHα, 3JHNC′, 3JHNCβ (54 (link)), 3JHαC′ (55 (link)), and 3JC′C′ (56 (link)). Side-chain scalar coupling constants were calculated using published Karplus relationships for 3JHαHβ, 3JC’Hβ, 3JC’Cγ, and 3JNCγ (57 (link)), with the exception of 3JC’Cγ and 3JNCγ values for Ile, Thr, and Val, which were computed using Karplus parameters from the work by Chou et al. (58 (link)). Through-hydrogen bond 3HJNC′ scalar coupling constants were calculated according to the work by Barfield (59 (link)). RDCs of folded proteins were calculated as reported previously (60 (link)). RDCs of disordered proteins were calculated using PALES (61 ) using a local alignment window of 15 residues. Backbone amide and methyl S2 order parameters were calculated from the value of the internal autocorrelation functions of the relevant bond vectors at lag times corresponding to the experimentally determined rotational correlation times as described previously (62 (link)). Internal autocorrelation functions were calculated after aligning trajectories to the backbone atoms of the simulation starting structures for ubiquitin, GB3, and HEWL and to backbone atoms of the stable leucine zipper coiled coil dimer interface for GCN4 (63 ). NMR chemical shifts were calculated using Sparta+ (64 (link)). PREs were calculated as described previously (7 (link)).
Robustelli P., Piana S, & Shaw D.E. (2018). Developing a molecular dynamics force field for both folded and disordered protein states. Proceedings of the National Academy of Sciences of the United States of America, 115(21), E4758-E4766.
Publication 2018
Amides Cloning Vectors Hydrogen Bonds Leucine Zippers Pressure Proteins Ring dermoid of cornea Ubiquitin Vertebral Column
5
Variant Calling and Mutation Profiling Protocol
Cited 6 times
Samples were analyzed pairwise with the default settings of Strelka49 (link) version 0.4.7 with primary tumor samples against matched remission samples. Somatic variants called by either mpileup or Strelka were combined and filtered out if they met any of the following criteria: <10 reads in the remission sample, <10 reads in the tumor sample, number of reads called for the altered base (tumor alt base) = 0, adjusted tumor allele frequency = 0, global minor allele frequency (GMAF) > 0.009 and >60 subjects with exactly the same SNVs. For subjects established as being in morphological remission, additional filters included removing variants with an allele fraction of >0.10 in the remission sample and a Fisher’s exact test score of >0.05. For refractory subjects, variants were excluded if they had a >0.35 allele fraction in the post-diagnostic sample. These filtered variants could be ‘rescued’ if a variant was a known Catalogue of Somatic Mutations in Cancer (COSMIC) mutation associated with hematological cancers. The filtering criteria for indel calls were similar. Tandem duplications were identified with Pindel using default parameters50 (link). In addition, results from clinical molecular testing for specific genes (FLT3-ITD and FLT3 codons 835 and 836, CEBPA basic leucine zipper domain (bZIP) and N-terminal domain (NTD) regions, KIT exons 8 and 17, CBL exons 8 and 9, and WT1 exon 7) were merged into the variant calls for final analysis.
DNA variants from discovery and TCS studies were merged to construct the mutation profile for each gene using the web-based program ProteinPaint51 (link). Genome-wide mutational burden was compared to published data from Lawrence et al.52 (link), using the method reported therein.
Bolouri H., Farrar J.E., Triche T J.r., Ries R.E., Lim E.L., Alonzo T.A., Ma Y., Moore R., Mungall A.J., Marra M.A., Zhang J., Ma X., Liu Y., Liu Y., Auvil J.M., Davidsen T.M., Gesuwan P., Hermida L.C., Salhia B., Capone S., Ramsingh G., Zwaan C.M., Noort S., Piccolo S.R., Kolb E.A., Gamis A.S., Smith M.A., Gerhard D.S, & Meshinchi S. (2017). The molecular landscape of pediatric acute myeloid leukemia reveals recurrent structural alterations and age-specific mutational interactions. Nature medicine, 24(1), 103-112.
Publication 2017
Alleles CEBPA protein, human Codon Cosmic composite resin Diagnosis Diploid Cell Exons FLT3 protein, human Genes Genetic Profile Hematologic Neoplasms INDEL Mutation Leucine Zippers Malignant Neoplasms Mutation Neoplasms

Most recents protocols related to «Leucine Zippers»

1
Triheteromeric NMDA receptor constructs
Triheteromeric receptor
constructs were generated using rat GluN1 and GluN2A with modified
C-terminal peptide tags as previously described.72 (link) Briefly, C-terminal peptide tags were generated from leucine
zipper motifs found in GABAB1 (referred to as C1) and GABAB2 (referred to as C2). These tags were placed downstream of
a synthetic helical linker and upstream of a KKTN endoplasmic reticulum
retention signal.113 (link)−115 (link) The tag was introduced in frame and in place
of the stop codon at the GluN2A C-terminal tail to make 2AC1 and 2AC2. A chimeric GluN2B subunit was constructed in
which the 2B carboxyl tail after residue 838 was replaced by the GluN2A
carboxyl tail and C-terminal-linker-C1 or -C2-ER retention motifs
to make 2BAC1 and 2BAC2.72 (link) The C1 and C2 leucine zipper motifs can form a coiled-coil
structure that masks the KKTN retention motif and allows for expression
of only triheteromeric receptors on the cell surface. Recordings were
taken at pH 7.4.
Measurement of “escape” currents
was used to assess the efficiency of the peptide tags which control
surface expression. Our average escape currents were typically less
than 10% and this was considered an acceptable threshold. Currents
were estimated using pairs of mutations (GluN2A-R518K,T690I and GluN2B-R519K,T691I)
that render the agonist binding domain incapable of binding glutamate,
and therefore unable to pass current.
Harris L.D., Regan M.C., Myers S.J., Nocilla K.A., Akins N.S., Tahirovic Y.A., Wilson L.J., Dingledine R., Furukawa H., Traynelis S.F, & Liotta D.C. (2023). Novel GluN2B-Selective NMDA Receptor Negative Allosteric Modulator Possesses Intrinsic Analgesic Properties and Enhances Analgesia of Morphine in a Rodent Tail Flick Pain Model. ACS Chemical Neuroscience, 14(5), 917-935.
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Publication 2023
Cells Chimera Codon, Terminator Glutamate GRIN2A protein, human GRIN2B protein, human Helix (Snails) Leucine Zippers Mutation Peptides Protein Subunits Reading Frames Retention (Psychology) Tail tyrosyl-alanyl-glycine
2
Characterization of Arabidopsis Regulatory Elements
The 800 nucleotide sequences upstream of the transcription start sites of the promoter regions of LBD16, AHP6, GATA23, and miR390 were obtained from the Arabidopsis Information Resource (TAIR) (https://www.arabidopsis.org/index.jsp). The cis elements listed in Supplementary Table 1, originally described in Dastidar et al. (2019) (link) and Cherenkov et al. (2018) (link), were identified within the gene promoter regions, classified in Supplementary Table 1, and represented in Supplementary Figure 2. The identification of genes encoding ARFs, Basic Leucine Zipper Domain (bZIP), and Basic Helix–Loop–Helix (bHLH) family members, upregulated either in Arabidopsis galls/GCs or syncytia (Supplementary Table 2), was performed from the lists available in NEMATIC (Cabrera et al., 2014b (link)). Detailed information about their expression patterns in galls and syncytia transcriptomes, descriptions, etc. is provided in Supplementary Table 2.
Abril-Urias P., Ruiz-Ferrer V., Cabrera J., Olmo R., Silva A.C., Díaz-Manzano F.E., Domínguez-Figueroa J., Martínez-Gómez Á., Gómez-Rojas A., Moreno-Risueno M.Á., Fenoll C, & Escobar C. (2023). Divergent regulation of auxin responsive genes in root-knot and cyst nematodes feeding sites formed in Arabidopsis. Frontiers in Plant Science, 14, 1024815.
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Publication 2023
Arabidopsis Base Sequence Family Member Genes Giant Cells Leucine Zippers Promoter Regions, Genetic Transcription Initiation Site Transcriptome
3
Validating RNA-Seq Expression Levels via qRT-PCR
Twelve transcripts were randomly selected for real-time quantitative PCR (qRT-PCR) to verify the accuracy of the levels of expression obtained under RNA-seq. Genes included: GMPM1: 18 kDa seed maturation; PP2C-51: protein phosphatase 2C 51-like; LEA-DC3: late embryogenesis abundant protein Dc3-like; DH1a: dehydrin DH1a; ATHB22: homeobox leucine zipper; SUS2: sucrose synthase 2-like; PIP2-2: aquaporin PIP2-2-like; XTH6: xyloglucan endotransglucosylase/hydrolase protein 6; GOLS2: galactinol synthase 2-like; CuSOD1: Superoxide dismutase [Cu-Zn]; APXChl: chloroplast ascorbate peroxidase. All primer sequences are presented in Table S1. The primers were designed using Primer3 web version 4.1.0 [84 (link)] with an e-value < 2 × 10−4 and a score >41. cDNA was synthesized from 1 μg total RNA using the SensiFASTTM cDNA Synthesis kit (Meridian BioScience, Cincinnati, OH, USA), according to the manufacturer’s recommendations. The presence of a single amplification product of the expected gene size was verified by electrophoresis on a 1.5% agarose gel. PCR reactions were prepared using the SensiFASTTM SYBR No-ROX kit (Meridian BioScience, USA) according to the manufacturer’s protocol. One negative sample was included for each primer pair, in which cDNA was replaced by water. Reactions were carried out in 96-well plates using a qTOWER 2.2 Thermal Cycler (Analytik, Jena, Germany) using the following parameters: hot start activation of the Taq DNA polymerase at 95 °C for 10 min, followed by 40 cycles of denaturation at 95 °C for 15 s, annealing at 60 °C for 30 s, elongation at 72 °C for 30 s. A melting curve analysis was performed at the end of the PCR run by a continuous fluorescence measurement from 55 °C to 95 °C with sequential steps of 0.5 °C for 15 s. A single peak was obtained and no signal was detected in the negative controls. Three technical replicates were used for each analyzed plant. Gene expression was quantified using malate dehydrogenase (MDH) and ubiquitin (UBQ10) as reference genes [85 (link)]. To understand the agreement of these results with the one from RNA-sequencing, heatmaps were constructed considering the levels of transcripts and their expression levels from qRT-PCRs after being log2 FC scaled by gene expression across treatments.
Marques I., Fernandes I., Paulo O.S., Batista D., Lidon F.C., Partelli F., DaMatta F.M., Ribeiro-Barros A.I, & Ramalho J.C. (2023). Overexpression of Water-Responsive Genes Promoted by Elevated CO2 Reduces ROS and Enhances Drought Tolerance in Coffea Species. International Journal of Molecular Sciences, 24(4), 3210.
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Publication 2023
Anabolism Aquaporin 2 Ascorbate Peroxidases Chloroplasts DNA, Complementary Electrophoresis Embryonic Development Fluorescence Gene Amplification Gene Expression Genes Homeo Box Sequence inositol 1-alpha-galactosyltransferase Leucine Zippers Malate Dehydrogenase Meridians Oligonucleotide Primers Plants Polymerase Chain Reaction Protein Phosphatase 2C Proteins Real-Time Polymerase Chain Reaction RNA-Seq Sepharose Sperm Maturation Sucrose synthase 2 Superoxide Dismutase Taq Polymerase Ubiquitin xyloglucan - xyloglucosyltransferase
4
Engineered KIF1A Constructs for Comparative Studies
The KIF1A-WT construct [adapted from Addgene #61665 (12 (link))] consists of the R. norvegicus KIF1A residues 1 to 393, followed by a GCN4 leucine zipper for dimerization and an eGFP tag. The KIF1A-SW was modified by swapping the native loop-12 (residues 288 to 308) of the KIF1A construct with the Drosophila melanogaster KHC loop-12 sequence (GNKTHIPYRD). This D. melanogaster loop-12 sequence was used because it provides a direct comparison to previous work (11 (link), 16 (link)), and it changes the charge of the loop with less sequence divergence than using loop-12 from KIF5B. Both constructs have a C-terminal His tag and were bacterially expressed and purified by nickel gravity column chromatography, as described previously (16 (link)). The elution buffer, consisting of 20 mM phosphate buffer, 500 mM sodium chloride, 500 mM imidazole,10 μM ATP, and 5 mM DTT was supplemented with 10% glycerol before flash freezing and storing at −80 °C. Concentrations were determined using GFP absorbance at 488 nm.
Pyrpassopoulos S., Gicking A.M., Zaniewski T.M., Hancock W.O, & Ostap E.M. (2023). KIF1A is kinetically tuned to be a superengaging motor under hindering loads. Proceedings of the National Academy of Sciences of the United States of America, 120(2), e2216903120.
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Publication 2023
Buffers Chromatography Dimerization Drosophila melanogaster Glycerin Gravity imidazole KIF5B protein, human Leucine Zippers Nickel Phosphates Sodium Chloride
5
Validating Trimeric Nature of Purified RBD

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Publication 2023
2-Mercaptoethanol Disulfides Glutaral Immunoglobulins Laemmli buffer Leucine Zippers Native Polyacrylamide Gel Electrophoresis Nitrocellulose Proteins Protein Trimerization Reducing Agents SDS-PAGE Tissue, Membrane Tromethamine

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More about "Leucine Zippers"

Leucine zippers are a structural motif found in certain proteins, characterized by a repeating pattern of leucine residues that facilitate protein-protein interactions.
These specialized domains play a crucial role in the dimerization and activation of various transcription factors, enabling them to bind to DNA and regulate gene expression.
Understanding the mechanics of leucine zippers is essential for researchers investigating cellular signaling pathways, gene regulation, and protein folding.
Researchers can utilize the TaqMan RNA-to-CT 1-Step Kit, a convenient tool for sensitive and accurate quantification of gene expression, to study the impact of leucine zippers on transcriptional regulation.
The HisTrap FF crude column can be employed for the purification of recombinant proteins containing leucine zipper domains, while the PALM MicroBeam system allows for the laser-assisted microdissection of specific cell populations expressing these motifs.
The TRI Reagent is a versatile solution for the isolation of high-quality RNA, DNA, and proteins, which can be used in conjunction with the GlutaMAX supplement to support cell growth and differentiation.
Additionally, the Lipofectamine 2000 transfection reagent can facilitate the delivery of genetic constructs containing leucine zipper-encoding sequences into cells, enabling the study of their functional roles.
The CFX96 real-time PCR detection system and the High-Capacity cDNA Reverse Transcription Kit can be employed for the quantitative analysis of gene expression patterns associated with leucine zipper-containing proteins.
Furthermore, the use of athymic nude mice, a common animal model, can provide insights into the in vivo implications of leucine zipper-mediated processes, such as tumor development and immune responses.
PubCompare.ai, an AI-driven platform, can help researchers optimize their protocols by easily locating relevant literature, pre-prints, and patents, and utilizing AI-driven comparisons to identify the best techniques and products for their specific needs.
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