> Living Beings > Bacterium > Anabaena

Anabaena

Anabaena is a genus of filamentous, nitrogen-fixing cyanobacteria commonly found in freshwater environments.
These photosynthetic microorganisms play a crucial role in aquatic ecosystems, contributing to nutrient cycling and primary productivity.
Anabaena species are known for their ability to form specialized cells called heterocysts, which are responsible for nitrogen fixation.
The genus is of great interest to researchers studying biological nitrogen fixation, algal biofuel production, and the ecology of freshwater systems.
Optimizing research protocols for Anabaena can be enhanced through the use of AI-driven comparisons, as offered by the PubCompare.ai tool, to identify the best experimental methods and products from the scientific literature, pre-prints, and patents.
This powerful tool can simplify the research process and enhance findings, boosting reproducibility and accuracy in Anabaena studies.

Most cited protocols related to «Anabaena»

X-ray Diffraction Analysis of Protein Crystals

X-ray diffraction data sets for the native and mercury-derivatized protein crystals were collected on beamline X06SA at SLS and beamline BL32XU at SPring-8, using a 1-μm-wide, 15-μm-high microbeam³⁸. Data were indexed and scaled with the programs XDS^{39 (link)} and SCALA^{40 (link)}, or with DENZO and SCALEPACK from the HKL2000 program suite (HKL Research). Experimental phases were determined by the MAD method, using the four Hg sites identified with the program SHELX^{41 (link)}. Subsequent refinements of the heavy atom parameters and phase calculations were performed with the program SHARP⁴². The data collection and phasing statistics are shown in Supplementary Table 1. The initial model structure of C1C2 was built with the program Phyre⁴³, using the Anabaena sensory rhodopsin structure (PDB accession 1XIO) as the template. The resultant structure was manually modified to fit into the experimental electron density maps, using the program Coot^{44 (link)}. The structure was then refined with the program Phenix^{45 (link)}. Figures were prepared with Cuemol (http://www.cuemol.org).

Kato H.E., Zhang F., Yizhar O., Ramakrishnan C., Nishizawa T., Hirata K., Ito J., Aita Y., Tsukazaki T., Hayashi S., Hegemann P., Maturana A.D., Ishitani R., Deisseroth K, & Nureki O. (2012). Crystal structure of the channelrhodopsin light-gated cation channel. Nature, 482(7385), 369-374.

Publication 2012

Anabaena Electrons Microtubule-Associated Proteins Proteins Sensory Rhodopsins X-Ray Diffraction

Cpf1-based Genetic Editing Plasmids

The plasmid containing cpf1 and the native Francisella novicida CRISPR array, pY002 (pFnCpf1_min)16 (link), was obtained as a kind gift from Feng Zhang (Addgene plasmid # 69975). The cpf1 gene was amplified from pY002 with the cpf1 lac-L/cpf1-R primers (Supplementary Table 2) which also fuse a lac promoter onto cpf1. The resulting fragment was cloned into the ApaLI/EcoRI sites on pVZ32138 to replace the Cm^R cassette to generate pSL2668. Next, overlap extension PCR was used to introduce a pair of AarI sites into the first spacer in the CRISPR array of pY002 by amplifying the left and right halves using the J23119ecoL/directrepeat aarI-2 or directrepeat aarI-1/directrepeat-R primers followed by amplification using the J23119ecoL/directrepeat-R primers. The resulting PCR fragment was cloned into the EcoRI/SalI sites on pSL2668 to generate pSL2683. LacZ was amplified from the pCrispomyces-239 (link) plasmid using the lacZaarI-L/lacZaarI-R primers. The resulting fragment was then cloned into the AarI sites on pSL2683 to generate pSL2680, which served as the base plasmid for construction of editing plasmids expressing a full length pre-crRNA. Editing plasmids were constructed by cloning annealed oligos into the AarI sites on pSL2680. The following annealed oligos were ligated into the AarI sites on pSL2680: 7942nblAKOgRNAL/7942nblAKOgRNAR to yield pSL2682; 7942s264agRNAL/7942s264agRNAR to yield pSL2723; NS1gRNAL/NS1gRNAR to yield pSL2724; 6803nblAKOgRNAL/6803nblAKOgRNAR to yield pSL2726; 7120nifHgRNAL/7120nifHgRNAR to yield pSL2728; 7120nifDgRNAL/7120nifDgRNAR to yield pSL2833; and 6803isiAgRNAL/6803gRNAR to yield pSL2834. Next, PCR was used to synthesize the homology regions which were then cloned into the KpnI site on the plasmids containing the matching crRNA. The Synechococcus 7942 nblA homology region containing the deletion of nblA was synthesized from pSL247015 (link) using nblAdelRkpnI/nblAdelLkpnI and cloned into the KpnI sites on pSL2682 and pSL2684 to yield pSL2691 and pSL2689 respectively. The homology region containing the Synechococcus 7942 psbA S264A mutation was synthesized using fusion PCR with the 7942psbAL1/7942psbAR2 and 7942psbAL2/7942psbAR1 primers followed by PCR with the 7942psbAL1/7942psbAR1 primers. The resulting PCR fragment was cloned into pSL2723 to yield pSL2796. The homology region targeting eYFP to NS1 was synthesized using fusion PCR with the pAM1303NS1L1/pAM1303NS1R2, pAM1303NS1L2/pAM1303NS1R3 and pAM1303NS1L3/pAM1303NS1R1 primers followed by PCR with the pAM1303NS1L1/ pAM1303NS1R1 primers. The resulting PCR fragment was cloned into pSL2724 to yield pSL2801. The Synechocystis 6803 nblA homology region containing the deletion of nblA1A2 was synthesized using fusion PCR with the 6803nblAdelL1/6803nblAdelR2 and 6803nblAdelL2/6803nblAdel R1 primers followed by PCR with the 6803nblAdelL1/6803nblAdelR1primers. The resulting PCR fragment was cloned into pSL2726 to yield pSL2773. The Anabaena 7120 nifH homology region containing the deletion of nifH was synthesized using fusion PCR with the 7120nifHL1a/7120nifH R2 and 7120nifHL2/7120nifHR1 primers followed by PCR with the 7120nifHL1a/7120nifHR1 primers. The resulting PCR fragment was cloned into pSL2728 to yield pSL2739. The Anabaena 7120 nifD point mutation homology region was constructed in two pieced using nifDL/nifDMR or nifDML/nifDR primers. The homology template was then assembled into pSL2833 linearized with kpnI using Gibson assembly to generate pSL2839. The Synechocystis 6803 isiA point mutation homology region was constructed in two pieces using 6803isiAL/6803isiAMR or 6803isiAML/6803isiAR primers. The homology template was then assembled into pSL2834 linearized with KpnI using Gibson assembly to generate pSL2834. The homologous repair template to insert eYFP into nifH of Anabaena 7120 was synthesized as three fragments using the primers 7120eYfplgibs/7120eYFPR1 or 7120eYFPL1/7120eYFPR2 or 7120eYFPL2/7120eYFPRgibs. The three fragments were assembled into pSL2728 linearized with KpnI using Gibson assembly to generate pSL2840. The homologous repair template to insert eYFP into nblA of 6803 was synthesized as three fragments using the primers 6803eYfplgibs/6803eYFPR1 or 6803eYFPL1/6803eYFPR2 or 6803eYFPL2/6803eYFPRgibs. The three fragments were assembled into pSL2726 linearized with KpnI using Gibson assembly to generate pSL2841.

Ungerer J, & Pakrasi H.B. (2016). Cpf1 Is A Versatile Tool for CRISPR Genome Editing Across Diverse Species of Cyanobacteria. Scientific Reports, 6, 39681.

Full text: Click here

Publication 2016

2',5'-oligoadenylate Anabaena CRISPR Loci CRISPR Spacers Deletion Mutation Deoxyribonuclease EcoRI Francisella tularensis subsp. novicida Genes LacZ Genes Mutation Oligonucleotide Primers Plasmids Point Mutation RNA, CRISPR Guide Synechococcus Synechocystis

Identifying CNB and GAF Domains in Plants

In order to identify the proteins which contain CNB or GAF domains, we initially used the Simple Modular Architecture Research Tool (SMART at smart.embl.heidelberg.de; [60 (link)-62 (link)]) to scan all predicted Arabidopsis proteins for CNB and GAF domains in the EMBL, TIGR or NCBI databases. Once redundancies were removed, a list of proteins was generated [see additional file 2]. In order to ensure broad coverage of possible variants, we also examined the Interpro collection of protein sequence analysis algorithms, all of which use slightly different methods [63 (link)]. As an additional method, the predicted proteins of the Arabidopsis genome were searched using the BLAST algorithm [64 (link)]. As search bait, we used several known cyclic nucleotide binding domains including those from GAF domains (human PDE2A [Swiss-Prot: O00408] and Anabaena cyaB1 [Trembl: P94181]) as well as CNB domains (human CGK2 [Swiss-Prot: Q13237], human RIIβ [Swiss-Prot: P31323], human Epac2 [Swiss-Prot: Q8WZA2], human rod CNGC [Swiss-Prot: P29973] and E. coli CAP [pir: E86000]). This yielded no new inclusions to our list of proteins, but did confirm each of our previous entries. For examination of the Oryza sativa spp. Japonica genome we performed BLAST searches using the aforementioned baits, as well as each of the Arabidopsis proteins. This search was performed using the Blast utility of the TIGR rice database [40 (link)]. The criterion for inclusion was that the CNB or GAF domain had to match the consensus motif with an E-value of less than 0.5 over the entire domain as determined by SMART. For newly identified proteins from the Orzya sativa, we named them so that they agreed best with the nomenclature of Maser et al. [37 (link)] [see additional files 1, 2, 3]. Sequence alignments were performed using the ClustalX [65 (link)] or T-COFFEE algorithms [66 (link)]and then inspected visually. Neighbor-joining trees were generated by ClustalX or PHYLIP [67 (link)], then were visualized with TreeView [68 (link)]. Trees generated using a variety of analysis methods (parsimony, distance and maximum likelihood) yielded similar results to the neighbor-joining trees.

Bridges D., Fraser M.E, & Moorhead G.B. (2005). Cyclic nucleotide binding proteins in the Arabidopsis thaliana and Oryza sativa genomes. BMC Bioinformatics, 6, 6.

Full text: Click here

Publication 2005

ALL protein, Arabidopsis Anabaena Arabidopsis Proteins Coffee Escherichia coli Genome Homo sapiens Inclusion Bodies Nucleotides, Cyclic Oryza sativa PDE2A protein, human PRKG2 protein, human Proteins Radionuclide Imaging Rice Sequence Alignment Sequence Analysis, Protein Staphylococcal Protein A Trees

Genetic Manipulation of Anabaena PCC 7120

All plasmids were verified by Sanger sequencing and listed in Supplementary Table S2. Primers used in this study were listed in Supplementary Table S3.
Plasmid pCpf1-CT- dnaENI is constructed for making conditional mutant CT-dnaENI. To generate the repair template, a region upstream of dnaENI amplified using the primers Pall3578F940m and Pall3578R150m, a region of CT promoter (an artificial promoter with a petE promoter and a theophylline riboswitch) amplified using the primers Pall0258F475m and PV_19 from vector pCT, and a region downstream amplified using the primers Pall3578F1 and Pall3578R960 were fused by overlapping PCR using the primers Pall3578F940m and Pall3578R960. A sequence of two spacers was prepared by annealing the complementary primers cr1_all3578F23mF, cr1_all3578F23mR, cr2_all3578R32mF, and cr2_all3578R32mR. The repair template and the spacer sequence were sequentially cloned into pCpf1 at the sites of BglII/BamHI and AarI/AarI, resulting in the mutation plasmid pCpf1-CT-dnaENI.
To generate plasmid pCint2-ΔdnaA, the upstream and downstream sequences of dnaA gene as well as the kanamycin resistance cassette were amplified using specific primers listed in Supplementary Table S2. The resulting three fragments were fused by overlapping PCR using the primers Palr2009F1255m and Palr2009R2628. This repair template was then cloned into pCint2 at the sites of BglII/BamHI, resulting in the plasmid pCint2-ΔdnaA.
To construct the CT-dnaENI conditional mutant, the mutation plasmid pCpf1-CT-dnaENI was transferred into Anabaena PCC 7120 by conjugation (Cai and Wolk, 1990 (link); Elhai et al., 1997 (link)). The exconjugants were selected on BG11 plates containing 100 μg mL^–1 neomycin, 0.3 μmol CuSO₄, and 1 mM theophylline and verified by PCR and Sanger sequencing.
To construct WT/pP_hetR-gfp, TRS-polA/pP_hetR-gfp, and CT-dnaENT/pP_hetR-gfp, the replicated plasmid pP_hetR-gfp was transferred into WT, TRS-polA, and CT-dnaENT, respectively, by conjugation. The positive clones were selected on BG11 plates containing 5 μg mL^–1 spectinomycin and 2.5 μg mL^–1 streptomycin and verified by PCR.
To construct ΔdnaA, the mutation plasmid pCint2-ΔdnaA was transferred into Anabaena PCC 7120 by conjugation, and the single-crossover was selected on BG11 plates containing 100 μg mL^–1 neomycin and verified by PCR. The homologous double-crossover was selected on BG11 plates containing 8% sucrose, verified by PCR and Sanger sequencing.
To make the plasmid for transcriptional fusion of hetR, the promoter region of hetR was amplified using the primers Palr2339F915m and Palr2339R3 and subsequently cloned into pRL25N-Lgfp at the sites of BamHI/XhoI, resulting in the transcriptional fusion plasmid pP_hetR-gfp. It was then moved into the cells by conjugation.

Xing W.Y., Xie L.R., Zeng X., Yang Y, & Zhang C.C. (2020). Functional Dissection of Genes Encoding DNA Polymerases Based on Conditional Mutants in the Heterocyst-Forming Cyanobacterium Anabaena PCC 7120. Frontiers in Microbiology, 11, 1108.

Full text: Click here

Publication 2020

Anabaena Cells Cloning Vectors Genes Kanamycin Resistance Mutation Neomycin Oligonucleotide Primers Plasmids Riboswitch Spectinomycin Streptomycin Sucrose Theophylline Transcription, Genetic

Cyanobacterial Metacaspase Identification

Thirty-three species of cyanobacteria, including Prochlorococcus, Synechococcus, Synechocystis, Gloeobacter, Cyanothece, Microcystis, Trichodesmium, Acaryochloris, Anabaena and Nostoc were used in this analysis. Since sequences of 36 species had not been fully released, they were not considered in our comparisons. All of the 33 genome sequences (as of Nov. 2008) were accessed from IMG in FASTA format [41 ].
In order to identify genes that may encode metacaspases, proven metacaspases from marine diatom Thalassiosira pseudonana (Protein id: 270038, 2505, 268857, 270007, 38187 in Thalassiosira pseudonana "finished chromosomes" database v3.0 [11 (link),42 ]) were used to construct a query protein set. BLASTp (protein-protein BLAST) [22 (link),43 (link),44 (link)] was conducted locally to search all proteins from each of the 33 cyanobacteria. Proteins found by this method that fit the criteria for a genuine metacaspase were added to the query set for another round of BLASTp searches. A threshold e-value of 1e-10 was set in the first two rounds, which changed into 2e-20 subsequently. The procedure was continued until no new proteins were found.
Proteins identified by BLASTp were aligned using Clustal X (Version 1.83) program [45 (link)] with a gap opening penalty of 10, a gap extension penalty of 0.2, and Gonnet as the weight matrix. The alignment was examined by inspection of peptidase C14, caspase catalytic subunit P20 domain (COG 4249, KOG1546 in the NCBI Conserved Domain Database [23 (link),24 ]). A protein was accepted as a metacaspase if it was possible to recognize P20 domain and if the most conserved His and Cys residues known to participate in the function of metacaspases [18 (link)] were present. However, minor alterations of the conserved His and Cys residues were tolerated. Specifically, putative MCA genes encoding Tyr in place of His and Ser/Asn/Gln/Gly instead of Cys were taken into account as well. Structure analyses of the obtained metacaspases were performed using the SMART (Simple Modular Architecture Research Tool) [25 ,26 (link)] and the CDD (Conserved Domains Database) [23 (link),24 ], relying on hidden Markov models and Reverse Position-Specific BLAST separately. Sequences of the P20 domain (about 300 aa in length) used for phylogenetic tree construction were obtained from the SMART database [25 ,26 (link)]. Trees based on metacaspase P20 domain and cyanobacterial 16s rRNA were constructed using NJ methods of the MEGA package (Version 4.0) [46 (link)], and the reliability of each branch was tested by 1000 bootstrap replications. In phylogenetic analysis of MCA, putative metacaspase of Gamma proteobacterium and human caspase-3 were used as outgroups to root the tree.

Jiang Q., Qin S, & Wu Q.Y. (2010). Genome-wide comparative analysis of metacaspases in unicellular and filamentous cyanobacteria. BMC Genomics, 11, 198.

Full text: Click here

Publication 2010

Anabaena CASP3 protein, human Caspase Catalytic Domain Chromosomes Cyanobacteria Cyanothece cysteinylglycine Diatoms DNA Replication Gamma Rays Genes Genome glutaminyl-glycine Homo sapiens Marines Microcystis Nostoc Peptide Hydrolases Plant Roots Prochlorococcus Proteins Protein Subunits RNA, Ribosomal, 16S Staphylococcal Protein A Synechococcus Synechocystis Trees Trichodesmium

Most recents protocols related to «Anabaena»

Cyanobacterial Nitrogen Fixation and Carbon Assimilation

¹⁵N₂ incubation was performed according to our previous work (26 (link)). Briefly, an aliquot of 20 mL of BG11₀ medium was filled into a 120-mL crimp-top vial and inoculated with 500 μL of Anabaena sp. PCC 7120 or R. raciborskii XM1 solution. The vials were sealed, and air in the headspace was replaced with Ar gas after 10 min of continual aeration. Then, a gas mixture consisting of N₂ and O₂ (4:1 v/v) was aerated into the vials to achieve different volume percentages of ¹⁵N₂ (¹⁵N₂/(¹⁵N₂ + ¹⁴N₂)). Considering that ¹⁵N content is 0.36% in natural abundance and 99% in commercial areas, the absolute atmospheric ¹⁵N abundances in the incubations were calculated as 0.36, 10.22, 25.02, 49.68, 74.52, and 99.36%. To temporally track N₂ fixation and transfer, cyanobacteria were incubated in the prepared ¹⁵N₂-containing atmosphere and harvested after 6 or 12 h time intervals.
In parallel incubation experiments, to perform ¹³C labeling, BG11₀ medium without NaHCO₃ was aerated with Ar gas to remove dissolved CO₂. Premixed ¹²C and ¹³C-NaHCO₃ solutions with ¹³C percentages (¹³C/(¹³C + ¹²C)) of 1.11, 10.90, 25.58, 50.06, 74.53, and 99.00% (calculated after considering the ¹³C natural abundance) were immediately added to the medium. The vials were sealed, and air in the headspace was replaced with Ar gas after 10 min of continual aeration. Then, a mixture gas consisting of N₂ (as a sole source of nitrogen) and O₂ (4:1 v/v) was aerated into the vials. After inoculating 500 μL of Anabaena sp. PCC 7120 or R. raciborskii XM1 solution, cyanobacteria were cultured in these media and harvested at 6 or 12 h time intervals.

Cui L., Xin Y., Yang K., Li H., Tan F., Zhang Y., Li X., Zhu Z., Yang J., Kao S.J., Ren B., Zhu Y.G., Musat F, & Musat N. (2023). Live tracking metabolic networks and physiological responses within microbial assemblages at single-cell level. PNAS Nexus, 2(3), pgad006.

Publication 2023

Anabaena Atmosphere Bicarbonate, Sodium Culture Media Cyanobacteria Nitrogen Nitrogen Fixation

Diazotrophic cyanobacteria N2 fixation analysis

Two types of heterocyst-forming diazotrophic cyanobacteria i.e. Anabaena sp. and R. raciborskii were used in this study. A model strain Anabaena sp. PCC 7120 was obtained from the Freshwater Algae Culture Collection of the Institute of Hydrobiology, China. The bloom-forming cyanobacterium of R. raciborskii XM1 was isolated in a Xiamen reservoir during a summer bloom in 2018 (33 (link)). To further confirm the N₂ fixation potential of these strains, dinitrogenase reductase genes (nifH) were amplified and visualized on agarose gels. Briefly, extracted cyanobacterial DNAs were polymerase chain reaction amplified with primers nifH1 (5′-TGYGAYCCNAARGCNGA-3′) and nifH2 (5′-ADNGCCATCATYTCNCC-3′). The appearance of nifH at around 359 bp in agarose gel electrophoresis is shown in Fig. S2a. These two cyanobacterial strains were cultured in BG11 or N-free BG11 (BG11₀) medium at ∼28°C and 90 rpm under constant light condition. They were cultured in BG11₀ to ensure heterocyst formation before isotope labeling. N₂-fixing A. chroococcum (ACCC10096) and E. coli MG1655 were purchased from the Guangdong Culture Collection Center of Microbiology, China, and cultured in N-free azotobacter media and Luria−Bertani broth, respectively before co-culture. All culture medium recipes are provided in Supplementary information.
The chemicals used for stable isotope incubation included ¹⁵N-NaNO₃ (98 atom% ¹⁵N, Sigma−Aldrich, United Kingdom), ¹³C-NaHCO₃ (99 atom%; Cambridge Isotope Laboratories, Inc., UK), and ¹⁵N₂ (99 atom%; Aladdin, China). Unless otherwise stated, all chemicals were purchased from Sinopharm Chemical Reagent Co., China.

Publication 2023

Anabaena Azotobacter Bicarbonate, Sodium Coculture Techniques Culture Media Cyanobacteria Dinitrogenase Reductase DNA Electrophoresis, Agar Gel Escherichia coli Gels Genes Isotopes Light Nitrogen Fixation Oligonucleotide Primers Polymerase Chain Reaction Sepharose Strains

Isotope Labeling of Cyanobacteria for Bulk Analysis

Isotope ratio mass spectrometry was used to measure the bulk isotope contents of ¹⁵N or ¹³C in Anabaena sp. PCC 7120 was incubated with various percentages of ¹⁵N₂ or ¹³C-NaHCO₃. For ¹⁵N or ¹³C measurement, 0.01–0.03 mg of lyophilized ¹⁵N- or ¹³C-labeled Anabaena sp. PCC 7120 and 0.05–0.17 mg of urea (standards) were mixed in a tin capsule. About 0.10–0.20 mg of non-labeled lyophilized Anabaena sp. PCC 7120 used as control groups were placed in tin capsules. The samples were analyzed with an elemental analyzer (Flash HT 2000 Thermo Fisher) coupled via a ConFlo IV device to the IRMS (Delta V advantage). The bulk isotope contents were calculated using the equation below:
where At ¹⁵N% (At ¹³C%) is the percentage of ¹⁵N (¹³C) relative to the total N (C) measured by IRMS; M_urea and M₇₁₂₀ are the weights of urea and lyophilized cyanobacteria, respectively; 0.36% (1.11%) is the natural abundance of ¹⁵N (¹³C) in the urea; 46.67 and 11.3% (19.98 and 51.4%) are the total N (C) contents in urea and cyanobacteria, respectively; and ¹⁵N% (¹³C%) is the abundance of ¹⁵N (¹³C) in cyanobacteria that needs to be calculated.

Publication 2023

Anabaena Bicarbonate, Sodium Capsule Cyanobacteria Dietary Fiber Isotopes Mass Spectrometry Medical Devices Nitrogen-15 Urea

Cultivation of Anabaena PCC7120 for Research

Anabaena PCC7120 was grown axenically in BG-11 medium (Rippka et al., 1979 ) buffered with 4-(2-hydroxyethyl)-1-piperazine-ethanesulfonic acid (HEPES) buffer (1.2 g L^–1) at pH 7.5 in Erlenmeyer flask of capacity 250 ml containing 100 ml of culture at 24 ± 2^oC under a day light fluorescent tube emitting 72 μmol m^–2 s^–1 photosynthetically active radiation (PAR) light intensity and a photoperiod of 14:10 h. The flasks were plugged with non-absorbent cotton and were shaken 2–3 times daily for proper aeration. All experiments were performed under an exponentially growing culture.

Srivastava R., Kanda T., Yadav S., Singh N., Yadav S., Prajapati R., Kesari V, & Atri N. (2023). Salinity pretreatment synergies heat shock toxicity in cyanobacterium Anabaena PCC7120. Frontiers in Microbiology, 14, 1061927.

Full text: Click here

Publication 2023

Anabaena Buffers ethane sulfonate Gossypium HEPES Light Piperazine Radiation

Anabaena Growth on Saline Agar

Exponentially growing Anabaena containing 10⁴ cells mL^–1 was aseptically spread on agar plates supplemented with various concentrations of NaCl (50–250 mM).

Full text: Click here

Publication 2023

Agar Anabaena Cells Sodium Chloride

Top products related to «Anabaena»

Sybr safe by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Australia, Canada, France, Germany, China, Denmark

SYBR Safe is a sensitive nucleic acid stain used for detecting DNA or RNA in agarose gels. It exhibits low toxicity and can be used in place of traditional ethidium bromide staining.

Bacto agar by BD

Sourced in United States, Germany, France, Japan, Switzerland, Netherlands, United Kingdom

Bacto agar is a solidifying agent used in microbiology and cell culture applications. It is derived from red seaweed and provides a solid growth medium for the cultivation of microorganisms and cell lines.

Quantitec reverse transcription kit by Qiagen

Sourced in Germany, United States, Canada, Italy

The QuantiTec Reverse Transcription Kit is a reagent system designed for the conversion of RNA to cDNA. It enables the synthesis of first-strand cDNA from total RNA or poly A+ RNA templates.

Gel doc 2000 image analyzer by Bio-Rad

Sourced in United States

The Gel Doc 2000 Image Analyzer is a compact and versatile imaging system designed for the documentation and analysis of DNA and protein gels. It captures high-quality images of electrophoresis gels and blots using a CCD camera and advanced imaging software.

5 methoxy uridine by TriLink

5-methoxy uridine is a nucleoside analogue with a methoxy group at the 5-position of the uracil base. It is a chemical compound used in research and laboratory applications.

Sybr safe dna gel stain by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Spain, Germany, Brazil, Canada, France, Sweden, China

SYBR Safe DNA gel stain is a nucleic acid stain used for the detection and visualization of DNA in agarose gels. It is a sensitive and environmentally friendly alternative to traditional DNA stains.

Pgem t easy vector by Promega

Sourced in United States, China, Germany, United Kingdom, Japan, France, Italy, Australia, Switzerland, Spain, Israel, Canada

The pGEM-T Easy Vector is a high-copy-number plasmid designed for cloning and sequencing of PCR products. It provides a simple, efficient method for the insertion and analysis of PCR amplified DNA fragments.

Orca er camera by Hamamatsu Photonics

Sourced in Japan, Germany, United States, United Kingdom

The ORCA-ER camera is a high-performance, scientific-grade digital camera designed for a wide range of imaging applications. It features a large active area, high quantum efficiency, and low readout noise, making it suitable for various microscopy techniques, including fluorescence, bioluminescence, and low-light imaging.

Cfx96 by Bio-Rad

Sourced in United States, China, Japan, Germany, France, United Kingdom, Canada, Singapore, Italy, Sweden, Estonia, Israel

The CFX96 is a real-time PCR detection system manufactured by Bio-Rad. It is designed for quantitative gene expression analysis and nucleic acid detection. The system includes a thermal cycler and an optical detection module to enable real-time monitoring of PCR reactions.

Protease inhibitor cocktail by Roche

Sourced in United States, Switzerland, Germany, China, United Kingdom, France, Canada, Japan, Italy, Australia, Austria, Sweden, Spain, Cameroon, India, Macao, Belgium, Israel

Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.

What are some common challenges in working with Anabaena?

One of the main challenges in working with Anabaena is maintaining optimal growth and nitrogen fixation conditions. These cyanobacteria require specific nutrient balances, light exposure, and environmental parameters to thrive. Researchers must carefully control factors like temperature, pH, and the presence of essential minerals to promote robust Anabaena cultures. Additionally, the formation of specialized heterocyst cells can be sensitive to changes in the culturing environment, which can impact nitrogen fixation rates. Optimizing these variables can be time-consuming and requires extensive trial and error, highlighting the value of tools like PubCompare.ai to streamline the research process.

How can PubCompare.ai help with Anabaena research?

PubCompare.ai is a powerful tool that can greatly assist researchers working with Anabaena. The platform allows you to efficiently scren protocol literature and leverage AI to pinpoint critical insights. By comparing a wide range of published methods, pre-prints, and patents, PubCopmare.ai can help you identify the most effective protocols related to Anabaena cultivation, nitrogen fixation, and other key processes. The AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy in your Anabaena studies. This can save valuable time and resources, while boosting the quality and impact of your research findings.

Are there different variations or types of Anabaena?

Yes, the Anabaena genus encompasses a diverse range of cyanobacterial species. While they share many common characteristics, such as the ability to form heterocysts and fix nitrogen, different Anabaena species can exhibit unique morphological, physiological, and genetic traits. For example, some Anabaena species are capable of producing toxic metabolites, while others may be more suited for biofuel production or bioremediation applications. Reserchers need to be aware of these variations when selecting Anabaena strains for their specific projects and experimental goals. Understanding the differences betweens Anabaena species can help optimize research protocols and ensure the most relevant findings.

What are some key applications of Anabaena?

Anabaena cyanobacteria have a wide range of applications in various fields. In aquatic ecosystems, Anabaena plays a crucial role in nutrient cycling and primary productivity, making it an important subject of study for freshwater ecology. Some Anabaena species have also shown potential for biofuel production, as they can accumulate lipids and other energy-rich compounds. Additionally, the nitrogen-fixing capabilities of Anabaena make them valuable for agricultural applications, such as biofertilizer development. Certain Anabaena strains have even demonstrated bioremediation properties, with the ability to remove pollutants or heavy metals from contaminated water bodies. Optimizing research protocols for these diverse applications can be greatly assisted by the AI-driven comparisons offered by PubCompare.ai.

More about "Anabaena"

Anabaena is a genus of filamentous, nitrogen-fixing cyanobacteria that play a crucial role in aquatic ecosystems.
These photosynthetic microorganisms are commonly found in freshwater environments, contributing to nutrient cycling and primary productivity.
Anabaena species are known for their ability to form specialized cells called heterocysts, which are responsible for nitrogen fixation.
The genus Anabaena is of great interest to researchers studying biological nitrogen fixation, algal biofuel production, and the ecology of freshwater systems.
Optimizing research protocols for Anabaena can be enhanced through the use of AI-driven comparisons, as offered by the PubCompare.ai tool.
This powerful tool can simplify the research process and enhance findings, boosting reproducibility and accuracy in Anabaena studies.
Researchers working with Anabaena may utilize a variety of lab equipment and reagents, such as the SYBR Safe DNA gel stain, PGEM-T Easy vector, and the QuantiTec Reverse Transcription Kit, to analyze gene expression and other molecular processes.
The Gel Doc 2000 Image Analyzer and ORCA-ER camera can be used for imaging and visualization, while the CFX96 system may be employed for quantitative PCR analyses.
Protease inhibitor cocktails can help preserve protein samples during Anabaena experiments.
By leveraging the insights gained from the MeSH term description and the metadescription, and incorporating relevant scientific terms and equipment, researchers can optimize their Anabaena studies and enhance the accuracy and reproducibility of their findings.
The use of AI-driven comparisons, as offered by PubCompare.ai, can simplify the research process and lead to more efficient and effective Anabaena research.