Log In Sign up
The largest database of trusted experimental protocols
> Genes & Molecular Sequences > Amino Acid Sequence > Zinc Fingers

Zinc Fingers

Zinc fingers are small protein motifs that can bind to DNA and regulate gene expression.
They are composed of a zinc ion coordinated by cysteine and histidine residues, forming a compact structure that interacts with the DNA backbone and specific nucleotide sequences.
Zinc finger proteins play crucial roles in many biological processes, including transcriptional regulation, DNA repair, and signal transduction.
Researchers can utilize PubCompare.ai's AI-driven platform to effortlessly locate protocols from literature, preprints, and patents, while using advanced comparisons to identify the best protocols and products for their zinc finger research needs.
This can enhance reproducibility and accuracy, allowing researchers to experince the future of research today.

Most cited protocols related to «Zinc Fingers»

1
Mapping Annotated Residues from Swiss-Prot to PDB
The numbered positions of annotated residues in the Swiss-Prot sequence often do not align to the same numbered positions of the sequence from the PDB structure. Therefore, a mapping of positions between the Swiss-Prot sequence and the PDB sequence must be obtained. We use a variation of the Needleman and Wunsch algorithm to identify if a sequence of a PDB structure can be found to match the sequence containing annotated residues from the Swiss-Prot database.
Specifically, every Swiss-Prot sequence containing one or more annotated residues and a link to a PDB structure was aligned to the corresponding sequence of the PDB structure. Standard annotations of Swiss-Prot used include post-translational modifications (MOD_RES), covalent binding of a lipid moiety (LIPID), glycosylation sites (CARBOHYD), post-translational formed amino acid bonds (CROSSLNK), metal binding sites (METAL), chemical group binding sites (BINDING), calcium binding regions (CA_BIND), DNA binding regions (DNA_BIND), nucleotide phosphate binding regions (NP_BIND), zinc finger regions (ZN_FING), enzyme activity amino acids (ACT_SITE) and any interesting single amino acid site (SITE). To ensure that the mapping is accurate, only alignments of two sequences with a sequence identity greater than ninety five percent were used. The annotated positions from Swiss-Prot are then transferred onto the PDB sequence, as long as the position is not aligned to a gap.
Dundas J., Ouyang Z., Tseng J., Binkowski A., Turpaz Y, & Liang J. (2006). CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Research, 34(Web Server issue), W116-W118.
Publication 2006
Amino Acids Binding Sites Calcium enzyme activity Lipid A Lipids Metals Nucleotides Phosphates Protein Biosynthesis Protein Glycosylation Sequence Alignment Zinc Fingers
2
Establishing Inference Thresholds for DNA-Binding Domains

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2014
Amino Acid Sequence ARID1A protein, human AT Rich Sequence Consensus Sequence DNA Replication DNA Sequence HSP40 Heat-Shock Proteins Protein Arrays Proteins Rosaniline Dyes Stars, Celestial Zinc Fingers
3
Clustering Transcription Factor Binding Sites
Transcription factors can be classified according to structural characteristics of DNA binding domains (Figure 2). It is often the case that TFs belonging to the same structural classes share similar DNA binding profiles, such that distinct TFs of the same class may bind to similar sequence patterns. If a given class contains numerous TFs with almost identical consensus sequences, oPOSSUM-3 analysis results can be dominated by subsets of profiles that are nearly identical. In such cases, it is useful to condense the redundant results to allow the user to identify independent enriched profiles. It is not suitable to combine the results simply based on the TF class, as the extent of the binding sequence similarity is variable among the different classes. Although some classes are defined by a characteristic consensus sequence, other classes, such as zinc fingers, have low profile similarities among the member TFs. Thus, it is necessary to divide each structural class into clusters based on profile similarity. Figure 2 illustrates the idea behind TFBS clustering and its application to oPOSSUM-3.
Profiles in JASPAR 2010 have been annotated for TF structural class and family. Based on these classifications, the profiles in the given family are subject to a refined clustering process in oPOSSUM-3. First, using the MatrixAligner similarity scoring program (Sandelin et al. 2003 (link)), a pairwise similarity score table is calculated for the entire set of profiles in JASPAR. Two thresholds are set: (1) cluster score threshold T, which is the MatrixAligner score above which the two matrices being compared are deemed to be similar, and (2) radius margin R, which is a secondary score threshold used to determine whether those TFs at the boundary of the cluster join the cluster (Figure 3A). The process is based on tree traversal, with nodes being the profiles and the edges being the similarity scores. One profile within a given family is randomly chosen to act as the seed node for the cluster, and a tree is constructed between this seed profile and all other profiles in the family. The nodes are traversed in sequence, and the traversed nodes are added to the cluster if (1) the similarity scores between the parent node and the child node are lower than the cluster score threshold T, and (2) the average score S between the cluster member nodes (the parent nodes that have already been included in the cluster) and the child node is below T. If the child node in question qualifies for condition 1 but not condition 2, it can still be included in the cluster if S exceeds T by less than R. A pseudocode of the clustering process is given in Figure S4. From the JASPAR 2010 database, 250 profiles from the CORE collection and 184 from the PBM collection were analyzed, along with the 4 profiles from the custom PENDING collection. A cluster score threshold of 1.8 and a radius margin of 0.1 were used. These values were selected empirically, based on the distribution of pairwise similarity scores among all available JASPAR profiles.
When a TFBS cluster-based analysis is performed, any overlapping TFBS hits that belong to the same TFBS cluster are merged to form a single cluster hit. Only the merged cluster hits are counted for TFBS over-representation calculations (Figure 3B).
Kwon A.T., Arenillas D.J., Hunt R.W, & Wasserman W.W. (2012). oPOSSUM-3: Advanced Analysis of Regulatory Motif Over-Representation Across Genes or ChIP-Seq Datasets. G3: Genes|Genomes|Genetics, 2(9), 987-1002.
Full text: Click here
Publication 2012
Child Consensus Sequence Didelphidae Parent Radius Transcription Factor Trees Zinc Fingers
4
Mapping African-enriched Recombination Hotspots
We assembled SNP array data from 29,589 unrelated people and 222 nuclear families genotyped at 490,000–910,000 SNPs from the Candidate Gene Association Resource (CARe), studies at the Children’s Hospital of Philadelphia (CHOP), the African American Breast Cancer Consortium, the African American Prostate Cancer Consortium and the African American Lung Cancer Consortium. To build a recombination map, we used HAPMIX to localize candidate crossover positions15 (link), and implemented a Markov Chain Monte Carlo (MCMC) that used the probability distributions for the positions of the filtered crossovers to infer recombination rates for each of 1.3 million inter-SNP intervals. We also implemented a second MCMC that models each individual’s set of crossovers as a mixture of a Shared (S) Map similar to the European deCODE Map and an African-enriched (AE) Map, and then assigns each individual an “AE phenotype” corresponding to the proportion of their newly detected crossovers assigned to the AE Map. We imputed genotypes at up to three million HapMap2 SNPs8 using MaCH26 (link), and then tested each of these SNPs for association with the AE phenotype and other recombination-related phenotypes. We identified 2,454 candidate African-enriched hotspots with increased recombination rates in the YRI vs. CEU maps, and in the AE vs. S maps, and searched for motifs enriched at these loci, thus identifying a degenerate 17-bp motif. To study the structure of PRDM9, we measured the length of the PRDM9 zinc finger array and genotyped rs6889665 in YRI, CEU and the CARe nuclear families; we also carried out imputation based on 1000 Genomes Project short read data10 (link) to infer the alleles individuals carry, among 29 previously characterized in a sequencing study of PRDM99 (link).
Hinch A.G., Tandon A., Patterson N., Song Y., Rohland N., Palmer C.D., Chen G.K., Wang K., Buxbaum S.G., Akylbekova M., Aldrich M.C., Ambrosone C.B., Amos C., Bandera E.V., Berndt S.I., Bernstein L., Blot W.J., Bock C.H., Boerwinkle E., Cai Q., Caporaso N., Casey G., Cupples L.A., Deming S.L., Diver W.R., Divers J., Fornage M., Gillanders E.M., Glessner J., Harris C.C., Hu J.J., Ingles S.A., Isaacs W., John E.M., Kao W.H., Keating B., Kittles R.A., Kolonel L.N., Larkin E., Le Marchand L., McNeill L.H., Millikan R.C., Murphy A., Musani S., Neslund-Dudas C., Nyante S., Papanicolaou G.J., Press M.F., Psaty B.M., Reiner A.P., Rich S.S., Rodriguez-Gil J.L., Rotter J.I., Rybicki B.A., Schwartz A.G., Signorello L.B., Spitz M., Strom S.S., Thun M.J., Tucker M.A., Wang Z., Wiencke J.K., Witte J.S., Wrensch M., Wu X., Yamamura Y., Zanetti K.A., Zheng W., Ziegler R.G., Zhu X., Redline S., Hirschhorn J.N., Henderson B.E., Taylor HA J.r., Price A.L., Hakonarson H., Chanock S.J., Haiman C.A., Wilson J.G., Reich D, & Myers S.R. (2011). The landscape of recombination in African Americans. Nature, 476(7359), 170-175.
Publication 2011
African American Alleles Europeans Genes Genome Lung Cancer Malignant Neoplasm of Breast Microtubule-Associated Proteins Negroid Races Phenotype Prostate Cancer Recombination, Genetic Single Nucleotide Polymorphism Zinc Fingers
5
Zinc Finger Protein Binding Sites
Single ZFP-binding sites—Individual zinc finger modules can be linked together to form multi-finger arrays that recognize specific sequences in double-stranded genomic DNA (Figure 2a). These multi-finger arrays can be fused to other protein domains, such as transcriptional activation or repression domains, in order to target them to specific locations within large genomes (1–4 ). Because a single ZF recognition helix typically binds three contiguous nucleotides in DNA, most binding sites for single ZF proteins (which we designate'single ZF array binding sites’) have lengths that are multiples of three base pairs. However, certain ZF modules containing aspartic acid in the +2 position of the DNA recognition helix appear to recognize four nucleotides. This can result in ‘target site overlap’ between adjacent ZF modules or, if the Asp-containing module occurs in the amino-terminal position of an array, the requirement for an additional 3' nucleotide in the ZF array binding site (19 (link)).
Dimeric zinc finger nuclease sites—Zinc finger nucleases (ZFNs) consist of a zinc finger array fused to a non-specific dsDNA nuclease (e.g. the nuclease domain of the Type IIS restriction enzyme FokI) (5 (link),6 (link),8 (link),10 (link)). ZFNs made with FokI nuclease are catalytically active only as dimers (20 (link)). Thus, a full ZFN target site consists of two ZF ‘half-sites’ on complementary DNA strands, separated by a ‘spacer’ of five or six base pairs, as shown in Figure 2b (6 (link),21 (link)). In this article, we designate the two ‘half-sites’ together with the spacer as a ‘dimeric ZF nuclease site.’
Sander J.D., Zaback P., Joung J.K., Voytas D.F, & Dobbs D. (2007). Zinc Finger Targeter (ZiFiT): an engineered zinc finger/target site design tool. Nucleic Acids Research, 35(Web Server issue), W599-W605.
Publication 2007
Aspartic Acid Binding Proteins Binding Sites DNA, Complementary DNA, Double-Stranded DNA Restriction Enzymes Fingers Genome Helix (Snails) Nucleotides Protein Domain Repression, Psychology Transcriptional Activation Zinc Fingers

Most recents protocols related to «Zinc Fingers»

1
Synthetic Promoters for Recombinant Protein Expression
The DNA fragments MMV FLt (-193 to +63 bp), MMV Sgt (-306 to -125 bp), and FMV Sgt (-270 to -63 bp) were chemically synthesized (Gene Universal, Inc., Newark, USA) (Supplemental Table 1). The FM′M promoter was first synthesized as a single DNA fragment. Subsequently, each domain was amplified by PCR using the specific primers MMFg-F, MMSg-F, FsMf-F, FsMf-R, M′FM-R, M′FM-F, and FM′M-R (Supplemental Table 2). To insert the UAS×4 motif and/or the single or double zinc finger binding motifs into the FM′M promoter, the primers FM′M-U-F and FM′M-R or FM′M-US-F and FM′M-US-R or FM′M-UD-F and FM′M-UD-R were used for overlapping PCR (Supplemental Table 2). All promoter fragments were digested with PstI and XbaI, and ligated into pCAMBIA1300, digested with the same restriction endonucleases. The BiP : GFP:HDEL recombinant construct (Islam et al., 2020 (link)) was ligated to each of the hybrid promoters following digestion with the restriction endonucleases XbaI and XhoI. The reporter gene encoding BiP : RBD:SD1:6×His : HDEL (Bangaru et al., 2020 (link)) was digested with the restriction endonucleases XbaI and XhoI, and ligated to the FM′M-UD or CaMV 35S promoters that had previously been digested with the same restriction endonucleases. The recombinant construct, BiP : MP:CBM3:bdSUMO:hIL6:HDEL (Islam et al., 2019 (link)), was ligated to the FM′M-UD or CaMV 35S promoters following digestion with XbaI and XhoI restriction endonucleases. All these constructs contained the RD29B terminator from Arabidopsis thaliana RD29B (D.13044.1) or the recombinant 3PR terminator (Supplemental Table 1). The 3PR terminator sequence was chemically synthesized (Gene Universal, Inc., Newark, United States). These terminators were ligated into the constructs after digestion with restriction endonucleases XhoI and EcoRI. The DNA fragments encoding the transcription factors GAL4:VP16, GAL4:TAC3d2, and ZinC7:TAC3d2 were chemically synthesized (Gene Universal, Inc., Newark, United States), and contained XbaI and XhoI restriction endonuclease sites. The MacT promoter and RD29B terminator were used for the expression of these transcription factors. All the primer sequences used in this study are listed in Supplemental Table 2.
Yun A., Kang J., Lee J., Song S.J, & Hwang I. (2023). Design of an artificial transcriptional system for production of high levels of recombinant proteins in tobacco (Nicotiana benthamiana). Frontiers in Plant Science, 14, 1138089.
Full text: Click here
Publication 2023
Arabidopsis thalianas Deoxyribonuclease EcoRI Digestion DNA Restriction Enzymes endodeoxyribonuclease XhoI Genes Genes, Reporter Hybrids Oligonucleotide Primers Terminator Regions, Genetic Transcription Factor VP-16 Zinc Fingers
2
Reannotation and Phylogenetic Analysis of Barley CCT Genes
We reannotated barley CCT genes by blasting CCT domains from HvCMF4 (301 to 345 residues) and Pfam database (http://pfam.xfam.org/) (PF06203) against barley Morex V2 proteome (e value: 0.005). Full-length protein sequences from the retrieved genes were domain-annotated with hmmscan under Pfam database to identify additional domains such as B-box–type zinc finger domain (PF00643), response regulator receiver domain (PF00072), GATA zinc finger (PF00320), or tify domain (PF06200). Gaps present in ≥80% of the aligned sequences were removed. Phylogenetic trees were built with RAxML (64 (link)). We carried out rapid bootstrapping and best­scoring ML tree searching in the same run (-f a) with an extended majority rule (-# autoMRE). The resultant tree was visualized with Evolview v3 (65 (link)). During the analysis, we noticed two CMFs (HvCMF4L1 and HvCMF4L2) with high amino acid sequence identity (~95%) compared with HvCMF4, which may indicate gene duplication. To ascertain this, we aligned the genomic sequences from HvCMF4L1/L2 against a ~5.5-kb genomic sequence surrounding HvCMF4 under the Sequence Alignment Viewer (https://ncbi.nlm.nih.gov/projects/msaviewer/) and found that both HvCMF4L1 and HvCMF4L2 arose from a partial duplication (~2 kb, with ~97% identity) of the HvCMF4 locus. We blasted the ~2-kb genomic sequences from both HvCMF4L1 and HvCMF4L2 against the remaining 19 barley reference genomes (16 (link)). While HvCMF4L1 was present in all of the 19 reference genomes assayed, for HvCMF4L2, only 14 (including Golden Promise) of the 19 barley reference genomes showed a hit in the syntenic region. Notably, no hits were found in syntenic regions of wheat and rye genomes for both genes (HvCMF4L1/L2), suggesting that these duplication events happened after the divergence of these Triticeae species and that the HvCMF4L2 duplication is younger than HvCMF4L1.
To construct a HvCMF4-specific phylogenetic tree, its full-length protein sequence was queried against proteomes from 14 species downloaded from Phytozome v12.1 (https://phytozome-next.jgi.doe.gov/), which included eight grasses and six eudicots. E value cutoff was set as 1 × 10−10, which retrieved 195 genes. After filtering genes without CCT domain or with the additional domains mentioned above, 186 were retained for building the tree. We followed the same procedure mentioned above to construct and visualize the tree. To ascertain true homology relationships with HvCMF4 inferred from the tree, we blasted back genes from the HvCMF4 clade against barley proteome.
Huang Y., Kamal R., Shanmugaraj N., Rutten T., Thirulogachandar V., Zhao S., Hoffie I., Hensel G., Rajaraman J., Moya Y.A., Hajirezaei M.R., Himmelbach A., Poursarebani N., Lundqvist U., Kumlehn J., Stein N., von Wirén N., Mascher M., Melzer M, & Schnurbusch T. (2023). A molecular framework for grain number determination in barley. Science Advances, 9(9), eadd0324.
Full text: Click here
Publication 2023
Amino Acid Sequence CMF regimen Gene Duplication Genes Genome Hordeum Poaceae Proteome Sequence Alignment Strains Synteny Trees Triticum aestivum Youth Zinc Fingers
3
Conformational Dynamics of Zinc Finger Protein ZNF410
The AlphaFold protein structure database (24 (link)) was used to predict the model of the full length ZNF410. The crystal structure of the zinc fingers ZF1–ZF5 in complex with 17-bp DNA (PDB ID: 6WMI) was superposed and compared to the predicted model. The AlphaFold model was used as a template to perform rigid body modeling. Minimal molecular dynamic simulations were performed on the flexible regions within the structure so as to explore the conformational space adopted by FL and individual constructs of ZNF140 using BILBOMD (25 ). In BILBOMD every ∼100 ps one conformational state is stored for further SAXS fitting. We record 10 000 conformers in total, varying in Rg and Dmax values for consequent SAXS fitting and multistate validation (26 (link)). Because of the dynamic and flexible character of ZNF410, a minimal ensemble search method was used to identify the multi-state model (27 (link)) required to best fit the experimental data. The scattering profile from all 10 000 models was first computed and subsequent genetic algorithm-selection operators were performed to shortlist the best models. The experimental scattering profiles from each construct were then compared with the theoretical scattering profile of the shortlisted best atomistic models generated by BILBOMD, using FOXS followed by multistate model selection by MULTIFOXS (27 (link)).
Kaur G., Ren R., Hammel M., Horton J.R., Yang J., Cao Y., He C., Lan F., Lan X., Blobel G.A., Blumenthal R.M., Zhang X, & Cheng X. (2023). Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410–DNA interaction using small angle X-ray scattering. Nucleic Acids Research, 51(4), 1674-1686.
Publication 2023
Character Human Body Muscle Rigidity Operator, Genetic Zinc Fingers
4
In Vivo Gene Editing for PiZ Mutation
To generate a dsDNA break in the genomic regions flanking the PiZ mutation, 2 rAAVs (AAV2/8, containing AAV2 ITRs and AAV8 capsid) were generated to express ZFNs from a hepatocyte-specific promoter consisting of the apolipoprotein E locus control region, human AAT promoter, a portion of intron-A of human coagulation factor IX, 3′-untranslated region, and a bovine growth hormone polyadenylation signal.21 ZFNs were designed with Fok1 nuclease monomer fused at the carboxy terminals of the zinc-finger proteins. When the 2 ZFN molecules home at their respective DNA sequence recognition sites on the 2 complementary DNA strands, the Fok1 monomers dimerize, generating an active nuclease (Figure 1A). For homology-directed correction of the pathogenic mutation on exon-7 of SA1-ATZ, rAAV-TI was designed by replacing the AAV2 genome with a segment of the wild-type human SERPINA1 gene consisting of left and right homology arms, ~1 kb each, flanking the mutation site, between the AAV2 ITRs. Two silent mutations were inserted into the homologous recombination donor to prevent recleavage by ZFN.
Li Y., Guha C., Asp P., Wang X., Tchaikovskya T.L., Kim K., Mendel M., Cost G.J., Perlmutter D.H., Roy-Chowdhury N., Fox I.J., Conway A, & Roy-Chowdhury J. (2023). Resolution of hepatic fibrosis after ZFN-mediated gene editing in the PiZ mouse model of human α1-antitrypsin deficiency. Hepatology Communications, 7(3), e0070.
Publication 2023
3' Untranslated Regions Apolipoproteins E Arm, Upper Capsid Dimerization DNA DNA, Complementary DNA, Double-Stranded Exons Factor IX Genes Genome Genome, Human growth hormone, bovine Homologous Recombination Homo sapiens Introns Locus Control Region Mutation NOS2A protein, human Pathogenicity Polyadenylation Proteins SERPINA1 protein, human Silent Mutation Tissue Donors Zinc Fingers
5
Genome-Wide Comparative Analysis of Cotton HD2 Protein Family
The whole-genome protein sequence dataset for G. arboreum, G. barbaense, and G. hirsutum was downloaded from the CottonGen database (https://www.cottongen.org/), and the dataset for G. raimondii was obtained from Phytozome, version 12 (https://phytozome.jgi.doe.gov/pz/portal.html) (Nordberg et al., 2014 (link)). Total protein sequences for other plant species from different taxonomic groups were downloaded from the website of the National Center for Biotechnology Information (NCBI) (http://www.ncbi.nlm.nih.gov/). A total of 58 HD2 protein sequences from 42 plant species were obtained from the NCBI and utilized to construct Hidden Markov model (HMM) profiles. This profile of the HD2 domains (the HD2 label and the catalytic, regulatory, and zinc- finger domains) was employed as a query to identify HD2 gene family members using HMMER (V3.0) (Finn et al., 2015 (link)). Protein sequences and CDSs for G. arboreum, G. raimondii, G. hirsutum, and G. barnadense were also downloaded from the CottonGen database (https://www.cottongen.org/) (Yu et al., 2014 (link)). All hits were queried in the Pfam (http://pfam.xfam.org/) and InterProScan (http://www.ebi.ac.uk/interpro/search/sequence-search/) databases to verify the presence of conserved domains. The ProtParam (http://web.expasy.org/protparam/) tool offered by Expasy was used to estimate the physicochemical parameters of Gossypium HD2 proteins. The ProtParam tool was also used to estimate biophysical and biochemical properties, such as number of amino acids, molecular weight, grand average hydropathy (GRAVY), theoretical isoelectric point (pI), aliphatic index, and instability index. The cotton HD2 gene subfamilies were named as per the orthologous HD2 members in the A. thaliana genome.
Bano N., Fakhrah S., Lone R.A., Mohanty C.S, & Bag S.K. (2023). Genome-wide identification and expression analysis of the HD2 protein family and its response to drought and salt stress in Gossypium species. Frontiers in Plant Science, 14, 1109031.
Full text: Click here
Publication 2023
Amino Acids Amino Acid Sequence Catalysis Family Member Genes Genome Gossypium Plants Proteins Triglyceride Storage Disease with Ichthyosis Zinc Fingers

Top products related to «Zinc Fingers»

1
Dual luciferase reporter assay system by Promega
Sourced in United States, China, Germany, United Kingdom, Switzerland, Japan, France, Italy, Spain, Austria, Australia, Hong Kong, Finland
The Dual-Luciferase Reporter Assay System is a laboratory tool designed to measure and compare the activity of two different luciferase reporter genes simultaneously. The system provides a quantitative method for analyzing gene expression and regulation in transfected or transduced cells.
2
Trizol reagent by Thermo Fisher Scientific
Sourced in United States, China, Japan, Germany, United Kingdom, Canada, France, Italy, Australia, Spain, Switzerland, Netherlands, Belgium, Lithuania, Denmark, Singapore, New Zealand, India, Brazil, Argentina, Sweden, Norway, Austria, Poland, Finland, Israel, Hong Kong, Cameroon, Sao Tome and Principe, Macao, Taiwan, Province of China, Thailand
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.
3
Fetal bovine serum (fbs) by Thermo Fisher Scientific
Sourced in United States, China, United Kingdom, Germany, Australia, Japan, Canada, Italy, France, Switzerland, New Zealand, Brazil, Belgium, India, Spain, Israel, Austria, Poland, Ireland, Sweden, Macao, Netherlands, Denmark, Cameroon, Singapore, Portugal, Argentina, Holy See (Vatican City State), Morocco, Uruguay, Mexico, Thailand, Sao Tome and Principe, Hungary, Panama, Hong Kong, Norway, United Arab Emirates, Czechia, Russian Federation, Chile, Moldova, Republic of, Gabon, Palestine, State of, Saudi Arabia, Senegal
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.
4
Lipofectamine 3000 by Thermo Fisher Scientific
Sourced in United States, China, Germany, Japan, United Kingdom, France, Canada, Italy, Australia, Switzerland, Denmark, Spain, Singapore, Belgium, Lithuania, Israel, Sweden, Austria, Moldova, Republic of, Greece, Azerbaijan, Finland
Lipofectamine 3000 is a transfection reagent used for the efficient delivery of nucleic acids, such as plasmid DNA, siRNA, and mRNA, into a variety of mammalian cell types. It facilitates the entry of these molecules into the cells, enabling their expression or silencing.
5
Lipofectamine 2000 by Thermo Fisher Scientific
Sourced in United States, China, Germany, United Kingdom, Canada, Japan, France, Italy, Switzerland, Australia, Spain, Belgium, Denmark, Singapore, India, Netherlands, Sweden, New Zealand, Portugal, Poland, Israel, Lithuania, Hong Kong, Argentina, Ireland, Austria, Czechia, Cameroon, Taiwan, Province of China, Morocco
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.
6
Griffonia simplicifolia isolectin ib4 ib4 lectin by Enzo Life Sciences
Griffonia simplicifolia isolectin IB4 (IB4 lectin) is a protein derived from the seeds of the Griffonia simplicifolia plant. It is a specific marker for endothelial cells and is commonly used in various research and diagnostic applications.
7
Iscript cdna synthesis kit by Bio-Rad
Sourced in United States, Germany, Italy, Canada, United Kingdom, France, Netherlands, Switzerland, Sweden, Belgium, Japan, Australia, China, India, Spain, Denmark, Austria, Norway
The IScript cDNA Synthesis Kit is a reagent kit used for the reverse transcription of RNA into complementary DNA (cDNA). The kit contains all the necessary components to perform this reaction, including a reverse transcriptase enzyme, reaction buffer, and oligo(dT) primers.
8
Puromycin by Merck Group
Sourced in United States, Germany, China, Sao Tome and Principe, United Kingdom, Macao, Canada, Japan, Italy, Switzerland, France, Israel, Australia, Spain, Belgium, Morocco, Sweden
Puromycin is a laboratory product manufactured by Merck Group. It functions as an antibiotic that inhibits protein synthesis in eukaryotic cells.
9
Spectramax m2 by Molecular Devices
Sourced in United States, United Kingdom, China, Japan, Germany, Australia, France, Canada
The SpectraMax M2 is a multi-mode microplate reader capable of absorbance, fluorescence, and luminescence measurements. It features a high-performance optical system and advanced data analysis software for accurate and reproducible results. The SpectraMax M2 is designed for a wide range of applications in life science research and drug discovery.
10
Pcdna3 by Thermo Fisher Scientific
Sourced in United States, China, United Kingdom, Germany, Japan, Canada, France, Sweden, Netherlands, Italy, Portugal, Spain, Australia, Denmark
The PcDNA3.1 is a plasmid vector used for the expression of recombinant proteins in mammalian cells. It contains a powerful human cytomegalovirus (CMV) promoter, which drives high-level expression of the inserted gene. The vector also includes a neomycin resistance gene for selection of stable transfectants.

More about "Zinc Fingers"

Zinc finger proteins, also known as ZFPs, are a class of small, versatile protein motifs that can bind to DNA and regulate gene expression.
These motifs are composed of a zinc ion coordinated by cysteine and histidine residues, forming a compact structure that interacts with the DNA backbone and specific nucleotide sequences.
Zinc fingers play crucial roles in many biological processes, including transcriptional regulation, DNA repair, and signal transduction.
Researchers can leverage a wide range of tools and techniques to study and manipulate zinc finger proteins, such as the Dual-Luciferase Reporter Assay System, TRIzol reagent, and Lipofectamine 3000 or Lipofectamine 2000 for transfection.
To enhance their zinc finger research, scientists can utilize AI-driven platforms like PubCompare.ai, which helps them effortlessly locate relevant protocols from literature, preprints, and patents.
By using advanced comparison features, researchers can identify the best protocols and products for their specific needs, improving reproducibility and accuracy.
Researchers may also employ other techniques, such as Griffonia simplicifolia isolectin IB4 (IB4 lectin) for cell labeling, the IScript cDNA synthesis kit for gene expression analysis, and puromycin for selection of transfected cells.
Specialized equipment like the SpectraMax M2 microplate reader can also be used to measure the activity of zinc finger-based systems, such as those encoded in pCDNA3.1 plasmids.
By leveraging the versatility of zinc finger proteins and the power of cutting-edge research tools and technologies, scientists can push the boundaries of their zinc finger research and experince the future of research today.