Protein sequences for human, mouse (Mus musculus), rat (Rattus norvegicus), chicken (Gallus gallus), pufferfish (Takifugu rubripes), zebrafish (Danio rerio) and fruitfly (Drosophila melanogaster) were retrieved from Ensembl (3 (link)). In addition, we obtained nematode (Caenorhabditis elegans and Caenorhabditis briggsae) proteins from WormBase (14 (link)), baker's yeast (Saccharomyces cerevisiae) proteins from SGD (15 (link)), fission yeast (Schizosaccharomyces pombe) proteins from GeneDB (16 (link)) and thale cress (Arabidopsis thaliana) proteins from TIGR (17 (link)). In addition to these fully sequenced species, TreeFam includes UniProt (18 (link)) proteins from animal species whose genomes have not been fully sequenced. Where multiple splice forms were available for a gene, all were downloaded, but just one splice form was chosen to represent the gene during the process of building a family (see ‘Constructing Phylogenetic Trees’ below). For TreeFam release 1.1, the Ensembl sequences were downloaded on 27th December 2004, and the other sequences in January 2005.
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Pufferfish
Pufferfish
Pufferfish, also known as blowfish or swellfish, are a group of marine and freshwater fish known for their ability to inflate their bodies when threatened.
These fascinating creatures belong to the order Tetraodontiformes and are found in tropical and subtropical waters around the world.
Pufferfish are characterized by their distinctive round, spiny bodies and their unique defense mechanism of inflating themselves with water or air to appear larger and deter predators.
They are highly sought after in some cuisines, but also contain a potent neurotoxin that can be fatal if not properly prepared.
Researchers are continually exploring the biology, behavior, and potential medicinal applications of these remarkable fish.
Whether you're studying pufferfish behavior, ecology, or pharmacology, PubCompare.ai can help you find the most accurate and reproducible protocols from the literature to enhace your pufferfish reserch.
These fascinating creatures belong to the order Tetraodontiformes and are found in tropical and subtropical waters around the world.
Pufferfish are characterized by their distinctive round, spiny bodies and their unique defense mechanism of inflating themselves with water or air to appear larger and deter predators.
They are highly sought after in some cuisines, but also contain a potent neurotoxin that can be fatal if not properly prepared.
Researchers are continually exploring the biology, behavior, and potential medicinal applications of these remarkable fish.
Whether you're studying pufferfish behavior, ecology, or pharmacology, PubCompare.ai can help you find the most accurate and reproducible protocols from the literature to enhace your pufferfish reserch.
Most cited protocols related to «Pufferfish»
Amino Acid Sequence
Animals
Arabidopsis thaliana Proteins
Arabidopsis thalianas
Caenorhabditis
Caenorhabditis elegans
Chickens
Drosophila
Drosophila melanogaster
Genes
Genome
Homo sapiens
link protein
Mice, House
Nematoda
NR4A2 protein, human
Proteins
Pufferfish
Rattus norvegicus
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Schizosaccharomyces pombe
Takifugu rubripes
Zebrafish
Adolescent
Child
Childbirth
Family Member
Households
Infant
Interviewers
Mothers
Physicians
Pufferfish
Speech
Vision
Seventeen new species have been added since TreeFam v1 (4 (link)). TreeFam v4 contains predicted protein sequences from the fully sequenced genomes of 25 animal species: human, chimpanzee, macaque, mouse, rat, cow, dog, opossum, chicken, frog, two pufferfish (Takifugu and Tetraodon), zebrafish, medaka, stickleback, sea squirts (Ciona intestinalis and C. savignyi), two fruit-flies (Drosophila melanogaster and D. pseudoobscura), two mosquitoes (Aedes aegypti and Anopheles gambiae), the flatworm Schistosoma mansoni, and the nematodes Caenorhabditis elegans, C. briggsae and C. remanei. In addition, four outgroup genomes are included: baker's yeast, fission yeast, rice and thale cress (Arabidopsis).
The C. briggsae and C. remanei proteins were downloaded from WormBase (16 (link)), D. pseudoobscura proteins from FlyBase (17 (link)), fission yeast and flatworm proteins from GeneDB (18 (link)), thale cress proteins from TIGR (19 (link)), rice proteins from the Beijing Genomics Institute (20 (link)) and the remaining sequences from Ensembl (15 (link)). In addition to these species, TreeFam includes UniProt (21 (link)) proteins from animal species whose genomes have not been fully sequenced. For TreeFam v4, all sequences were downloaded in October 2006.
The C. briggsae and C. remanei proteins were downloaded from WormBase (16 (link)), D. pseudoobscura proteins from FlyBase (17 (link)), fission yeast and flatworm proteins from GeneDB (18 (link)), thale cress proteins from TIGR (19 (link)), rice proteins from the Beijing Genomics Institute (20 (link)) and the remaining sequences from Ensembl (15 (link)). In addition to these species, TreeFam includes UniProt (21 (link)) proteins from animal species whose genomes have not been fully sequenced. For TreeFam v4, all sequences were downloaded in October 2006.
Aedes
Amino Acid Sequence
Animals
Anopheles gambiae
Arabidopsis
Arabidopsis thaliana Proteins
Arabidopsis thalianas
Caenorhabditis elegans
Chickens
Ciona intestinalis
citrate carrier
Culicidae
Didelphidae
Drosophila
Drosophila melanogaster
Flatworms
Genome
Homo sapiens
link protein
Macaca
Mice, House
Nematoda
Oryza sativa
Oryzias latipes
Pan troglodytes
Proteins
Pufferfish
Rana
Saccharomyces cerevisiae
Schistosoma mansoni
Schizosaccharomyces pombe
Sea Squirts
Sticklebacks
Takifugu
Zebrafish
Genome annotations were produced using the MAKER47 (link)–49 (link) genome annotation pipeline, which supports re-annotation using pre-existing gene models as input. Previous Petromyzon marinus gene models (WUGSC 7.0/petMar2 assembly)50 (link) were mapped against the new genome assembly into GFF3 format and were used as prior model input to MAKER for re-annotation. Snap51 (link) and Augustus52 (link),53 (link) were also used with MAKER and were trained using the pre-existing lamprey gene models. Additional input to MAKER included previously-published mRNA-seq reads derived from lamprey embryos and testes10 (link),12 (link),13 (link) and assembled using Trinity54 (link), as well as mRNA-seq reads (NexSeq 75–100 bp paired-end) were derived from whole embryos and dissected heads at Tahara stage 20, as well as dissected embryonic dorsal neural tubes at Tahara stage 18, 20 and 21. The following protein datasets were also used: Ciona intestinalis (sea squirt)55 (link), Lottia gigantea (limpet)56 (link), Nematostella vectensis (sea anemone)57 (link), Takifugu rubripes (pufferfish)58 (link), Branchiostoma floridae (lancelet)59 (link), Callorhinchus milii (elephant shark)60 (link), Xenopus tropicalis (western clawed frog)61 (link), Drosophila melanogaster (fruit fly)62 (link), Homo sapiens (human)63 (link),64 (link), Mus musculus (mouse)65 (link), Danio rerio (zebrafish)66 (link), Hydra magnipapillata67 (link), Trichoplax adhaerens68 (link), and the Uniprot/Swiss-Prot protein database69 (link),70 (link). Protein domains were identified in final gene models using the InterProScan domain identification pipeline71 (link)–73 (link), and putative gene functions were assigned using BLASTP74 (link) identified homology to the Uniprot/Swiss-Prot protein database.
Branchiostoma floridae
Ciona intestinalis
Drosophila
Drosophila melanogaster
Elephants
Embryo
Genome
Head
Homo sapiens
Hydra
Lampreys
Lancelets
Mice, House
Mus
Operator, Genetic
Petromyzon marinus
Protein Domain
Proteins
Pufferfish
RNA, Messenger
Sea Anemones
Sharks
Takifugu rubripes
Trichoplax
Tube, Neural
Urochordata
Xenopus laevis
Zebrafish
The latest build of genome assembly of zebrafish (Zv9) and pufferfish (tetNig2) were downloaded from UCSC Genome Browser (Kuhn et al. 2009 (link)). CAGE tags were mapped using Bowtie (Langmead et al. 2009 (link)), allowing a maximum of two mismatches and only uniquely mapping tags. Since the CAGE protocol often yields an additional G nucleotide at the 5′-end of the tag, we removed the starting G when mismatching G at the first position and removed tags with an additional mismatch at the second position (affecting 1%–2% of CAGE tags; see Supplemental Table 13). The remaining unique 5′-ends were regarded as CAGE tag-defined transcriptional start sites (CTSSs). The number of CAGE tags mapping to each CTSS across different samples was normalized as in Balwierz et al. (2009) (link) to obtain the normalized number of tags per million (tpm).
CAGE1 protein, human
CTSS protein, human
Genome
Nucleotides
Pufferfish
Transcription Initiation Site
Zebrafish
Most recents protocols related to «Pufferfish»
Fishes (n = 192) were collected in early April 2021 at Orpheus Island, GBR (18°36’44.3”S 146°28’59.4”E). All were “healthy” in that they were intact with good colour and no visible signs of disease, stress, or wasting. The vast majority were adult individuals. These included sixty-one species across sixteen reef fish families: Gobiidae (gobies) (n = 30 species), Labridae (wrasses) (n = 6), Pomacentridae (damselfishes) (n = 5), Blenniidae (blennies) (n = 5), Acanthuridae (surgeonfishes) (n = 3), Apogonidae (cardinalfishes) (n = 2), Monacanthidae (filefishes) (n = 2), Tetraodontidae (pufferfishes) (n = 1), Pseudochromidae (dottybacks) (n = 1), Chaetodontidae (butterflyfishes) (n = 1), Atherinidae (silversides, hardyheads) (n = 1), Serranidae (groupers) (n = 1), Tripterygiidae (triplefin blennies) (n = 1), Muraenidae (moray eels) (n = 1), Bythitidae (brotulas) (n = 1), and Ophichthidae (snake eels) (n = 1) (
Adult
Eels
Fishes
Gills
Liver
Oil, Clove
Pufferfish
Serranidae
SLC6A2 protein, human
Snakes
Following behavioral testing, one cohort of the Chat::Cre+ transgenic rats (N = 4 males, N = 4 females) were injected with an adeno‐associated viral vector (AAV) into the basal forebrain (BF) to induce enhanced yellow fluorescent protein (EYFP) expression in cholinergic neurons. Rats were anesthetized with isoflurane (5% for induction, 2.5% for maintenance, E‐Z Systems Palmer, PA) in oxygen, placed in a Kopf stereotaxic device (David Kopf Instruments, Tujunga CA), and body temperature was maintained using a homeothermic blanket (Harvard Apparatus, Holliston, MA). After administration of a local anesthetic (2% carbocaine, s.c.) at the incision site, the basal forebrain was targeted by drilling two holes through the skull using the following coordinates measured from Bregma with skull flat: A/P‐0.8, L/M+/− 2.4, DV ‐8.6‐8.8.46 Rats were injected bilaterally with 2 μl of rAAV5/Ef1a‐DIO‐EYFP (UNC Viral Vector Core; LOT AV4310L) using a 33‐gauge needle on a Neuros Hamilton syringe at a rate of 0.2 μl/min using a motorized injector (Stoelting QSI Stereotaxic injector Wood Dale, IL). Following injections, the viral vector was allowed to diffuse for 10 min before the needle was withdrawn. Nalbuphine (2 mg/kg, s.c.) was administered postoperatively for pain management, the diet was supplemented with bacon softies (Bio‐serve, Frenchtown, NJ) to maintain postoperative weight, and topical nitrofurazone powder (NFZ puffer, Neogen Corporation) was used for prevention of infection at the incision site. Animals were allowed 3 weeks of recovery prior to perfusion and euthanasia to determine the number of BF cholinergic neurons expressing eYFP using immunofluorescence for choline acetyltransferase (ChAT; described below).
Adeno-Associated Virus
Aftercare
Animals
BACON protocol
Basal Forebrain
Body Temperature
Carbocaine
Choline O-Acetyltransferase
Cholinergic Neurons
Cloning Vectors
Cranium
Diet
Euthanasia
Females
Immunofluorescence
Infection
Isoflurane
Local Anesthesia
Males
Management, Pain
Medical Devices
Nalbuphine
Needles
Nitrofurazone
Oxygen
Perfusion
Powder
Proteins
Pufferfish
Rats, Transgenic
Rattus
Syringes
Hemostatic factors were analyzed in citrate plasma samples collected after an overnight fast. Plasma samples were centrifuged (10 min. at 15°) immediately after collection and then aliquoted and stored at −80 °C. The separation of plasma from the other blood components was completed after 30 min. at the latest. The following hemostatic factors were analyzed: antithrombin III, D-dimers, factor VIII, fibrinogen, protein S, partial thromboplastin time (aPTT), quick value, and international normalized ratio (INR).
Antithrombin III (reference value: 83–118%) was determined by chromogenic activity assay (Innovance Antithrombin, SCS cleaner, Siemens Healthcare Diagnostics, Eschborn, Germany). D-dimers (reference value: <500 µg/dL) were measured by means of a particle-enhanced immunoturbidimetric assay (Innovance D-Dimer Kit, Siemens Healthcare Diagnostics). Factor VIII activity (reference value: 70–150%) was measured photometrically (coagulation factor VIII deficient plasma, Pathromtin SL, CaCl2, Siemens Healthcare Diagnostics), as well as quick value (reference value: 82–125%; Thromborel S, Siemens Healthcare Diagnostics), aPTT (reference value: 26–36 s; Pathromtin SL, CaCl Lösung, Actin FS, Siemens Healthcare Diagnostics), and protein S (reference value: men: 73–130%, women: 52–126%; Hemoclot protein S, OVB-Puffer, CaCl2, SCS Cleaner). Fibrinogen (reference value: 210–400 mg/dL) was measured photometrically and turbidimetrically (Multifibren U, Siemens Healthcare Diagnostics). INR (reference value: 0.9–1.15) was calculated from the prothrombin ratio (Thromborel S, Siemens Healthcare Diagnostics) by dividing the thromboplastin time of the subject by that of normal plasma squared with International Sensitivity Index (ISI) as defined by the World Health Organization [14 ]. Reference values of all hemostatic factors were taken from University Clinic Augsburg, while all other serum parameters were measured at the clinical laboratory of the University Hospital (Klinikum Großhadern) of the Ludwig-Maximilians University in Munich. Measurement procedures were performed and controlled by trained laboratory personnel according to standardized protocols.
Antithrombin III (reference value: 83–118%) was determined by chromogenic activity assay (Innovance Antithrombin, SCS cleaner, Siemens Healthcare Diagnostics, Eschborn, Germany). D-dimers (reference value: <500 µg/dL) were measured by means of a particle-enhanced immunoturbidimetric assay (Innovance D-Dimer Kit, Siemens Healthcare Diagnostics). Factor VIII activity (reference value: 70–150%) was measured photometrically (coagulation factor VIII deficient plasma, Pathromtin SL, CaCl2, Siemens Healthcare Diagnostics), as well as quick value (reference value: 82–125%; Thromborel S, Siemens Healthcare Diagnostics), aPTT (reference value: 26–36 s; Pathromtin SL, CaCl Lösung, Actin FS, Siemens Healthcare Diagnostics), and protein S (reference value: men: 73–130%, women: 52–126%; Hemoclot protein S, OVB-Puffer, CaCl2, SCS Cleaner). Fibrinogen (reference value: 210–400 mg/dL) was measured photometrically and turbidimetrically (Multifibren U, Siemens Healthcare Diagnostics). INR (reference value: 0.9–1.15) was calculated from the prothrombin ratio (Thromborel S, Siemens Healthcare Diagnostics) by dividing the thromboplastin time of the subject by that of normal plasma squared with International Sensitivity Index (ISI) as defined by the World Health Organization [14 ]. Reference values of all hemostatic factors were taken from University Clinic Augsburg, while all other serum parameters were measured at the clinical laboratory of the University Hospital (Klinikum Großhadern) of the Ludwig-Maximilians University in Munich. Measurement procedures were performed and controlled by trained laboratory personnel according to standardized protocols.
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Actins
Activated Partial Thromboplastin Time
antihemorrhagic factor
Antithrombin III
azo rubin S
Biological Assay
Blood Component Transfusion
Citrates
Clinical Laboratory Services
Diagnosis
Factor VIII
fibrin fragment D
Fibrinogen
Hypersensitivity
Immunoturbidimetric Assay
International Normalized Ratio
Laboratory Personnel
Plasma
Protein S
Prothrombin
Pufferfish
Serum
Thromboplastin
Woman
Tissue from the pathological routine diagnostics was used for histological examination. To characterize the TIME, we chose CD4 (Ventana, anti-CD4 Rabbit Monoclonal Primary Antibody, Clone SP35, dilution: 1:200) and CD8 (Ventana, anti-CD8 Rabbit Monoclonal Primary Antibody, Clone SP57, dilution: 1:200) as marker for lymphocytes, CD68 (Dako Anti-Human CD68, Clone KP1, dilution: 1:200) as a pan marker for macrophages and CD163 (Novocastra, Lyophilized Mouse Monoclonal Antibody CD163, Clone 10D6, dilution: 1:100) as a marker for M2-macrophages. First, a new hematoxylin-eosin slide was prepared, and the tumor was identified (Figure 1 A,B). All immunohistochemical stains were performed on tissue sections (4 µm thickness) prepared from formalin-fixed (4% neutral buffered formalin) paraffin-embedded tissue blocks. The procedure is part of the established routine diagnostic at our institute. Briefly, immunohistochemical staining was performed using a Roche Ventana Benchmark Ultra automated slide stainer (Ventana Medical Systems, Roche, France) with the OptiView DAB IHC Detection Kit (Roche, France). The first step of the automatic staining program includes deparaffinization and rehydrating the specimens. Then antigen retrieval was completed by heat treatment lasting for 32 min with Tris-EDTA Borat Puffer (pH 8–8.5). After incubation of the diluted primary antibodies, the nuclei were counterstained with hematoxylin.
All slides were scanned (3DHISTECH Ltd. Pannoramic slide scanner 250) and evaluated using a virtual microscopy software (3DHISTECH Ltd. Case Viewer Ver.2.2). To quantify lymphocytes, ten high power fields (HPF) were identified independently by two pathologists (A.M. & C.B.). The invasion front and tumor center were identified, and the positive cells were counted. The mean values were calculated. The CD68 reaction was used to visualize all macrophages. To evaluate the quantity of the macrophages, ten HPF of the invasion tumor front and intra-tumoral area were examined and the positive cells were counted. The mean value (confidence interval 95%) of macrophages within the tumor front and the intra-tumoral area was calculated. The macrophages were then characterized concerning their subpopulations. M2-macrophages were detected using CD163-antibody. The M2-macrophages were quantified, utilizing the same previously described procedure for quantifying CD68-positive macrophages. The number of M1-macrophages per HPF was calculated through the difference between CD68-positive-macrophages and CD163-positive-M2-macrophages.
All slides were scanned (3DHISTECH Ltd. Pannoramic slide scanner 250) and evaluated using a virtual microscopy software (3DHISTECH Ltd. Case Viewer Ver.2.2). To quantify lymphocytes, ten high power fields (HPF) were identified independently by two pathologists (A.M. & C.B.). The invasion front and tumor center were identified, and the positive cells were counted. The mean values were calculated. The CD68 reaction was used to visualize all macrophages. To evaluate the quantity of the macrophages, ten HPF of the invasion tumor front and intra-tumoral area were examined and the positive cells were counted. The mean value (confidence interval 95%) of macrophages within the tumor front and the intra-tumoral area was calculated. The macrophages were then characterized concerning their subpopulations. M2-macrophages were detected using CD163-antibody. The M2-macrophages were quantified, utilizing the same previously described procedure for quantifying CD68-positive macrophages. The number of M1-macrophages per HPF was calculated through the difference between CD68-positive-macrophages and CD163-positive-M2-macrophages.
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Antibodies
Antibodies, Anti-Idiotypic
Antigens
CD163 protein, human
Cell Nucleus
Cells
Clone Cells
Diagnosis
Edetic Acid
Eosin
Formalin
Hematoxylin
Homo sapiens
Immunoglobulins
Lymphocyte
Macrophage
Microscopy
Monoclonal Antibodies
Mus
Neoplasm Invasiveness
Neoplasms
Paraffin
Pathologists
Population Group
Pufferfish
Rabbits
Technique, Dilution
Tissues
Tromethamine
Initially, NCH421k cells (6 × 105) and U-87 MG (5 × 105) were seeded in wells of six-well plate and incubated for 24 h. Next day, anti-vimentin (Nb79) nanobody was added to final concentration 100 μg/mL and incubated for 48 h. After incubation, cells were washed with PBS three times and treated with 50 μL of RIPA puffer (ThermoFisher, Waltham, MA, USA) together with Halt protease inhibitors (ThermoFisher) and phosphatase inhibitors (ThermoFisher) for 15 min to enable cell lysis. Afterward, samples were collected to a tube and centrifuged for 15 min at 13,000 rpm. Supernatant was transferred to new microcentrifuge tubes and concentration of each cell lysate was measured on Synergy H4 Hybrid Multi-Mode Microplate Reader (BioTek, Winooski, VT, USA) using BCA Protein Assay Kit (ThermoFisher Scientific). For Western blotting, 10 μg of each sample was separated using NuPAGE 4% to 12% Bis-Tris Mini Gels (Invitrogen) and transferred to an Immobilon-P Transfer Membrane (Milipore, Burlington, MA, USA). Membrane was then blocked with 5% milk in PBS for 1 h at room temperature, and incubated with primary antibodies overnight at 4 °C. The antibodies and their working dilutions (all from Cell Signaling Technology, Danvers, MA, USA) were 1:2000 rabbit anti-ZO-1 (cat. number: 8193), 1:2000 rabbit anti-beta-catenin (cat. number: 8480), 1:2000 rabbit anti-vimentin (cat. number: 5741), 1:2000 rabbit anti-ZEB1 (cat. number: 3396). The next day, membrane was incubated with 1:5000 secondary anti-rabbit antibodies IgG, HRP-linked Antibody (cat. number: 7074, Cell Signaling Technology) for 2 h at room temperature. As a loading control, we used GAPDH (0.05 μg/mL, cat. number G8795 Sigma Aldrich, St. Louis, MO, USA). Signals were detected using SuperSignal West Pico Chemiluminescent Substrate (Thermo Scientific) and Fujifilm LAS-4000 (Tokyo, Japan). The results were analysed with the Multi Gauge version 3.2 software (FUJIFILM Manufacturing Corp., Tokyo, Japan). All the whole western blot figures can be found in the Supplementary Materials .
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anti-IgG
Antibodies
Biological Assay
Bistris
Cells
CTNNB1 protein, human
GAPDH protein, human
Gels
Hybrids
Immobilon P
Immunoglobulins
inhibitors
Milk, Cow's
Phosphoric Monoester Hydrolases
Protease Inhibitors
Proteins
Pufferfish
Rabbits
Radioimmunoprecipitation Assay
Technique, Dilution
Tissue, Membrane
Vimentin
Western Blotting
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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.
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More about "Pufferfish"
Pufferfish, also known as blowfish or swellfish, are a fascinating group of marine and freshwater fish known for their unique ability to inflate their bodies when threatened.
These remarkable creatures belong to the order Tetraodontiformes and are found in tropical and subtropical waters around the globe.
Characterized by their distinctive round, spiny bodies, pufferfish have developed a remarkable defense mechanism - they can inflate themselves with water or air to appear larger and deter predators.
This adaptation has made them highly sought-after in some cuisines, but it also means they contain a potent neurotoxin that can be fatal if not properly prepared.
Researchers are continually exploring the biology, behavior, and potential medicinal applications of these fascinating fish.
Tools like PubCompare.ai can help optimize pufferfish research by enabling users to find the most accurate and reproducible protocols from literature, preprints, and patents.
Leveraging AI-driven comparisons, this tool enhances the accuracy and reproducibility of pufferfish studies.
Whether you're studying pufferfish behavior, ecology, or pharmacology, techniques like the PcDNA3.1 expression vector, High-Capacity cDNA Reverse Transcription Kit, ATP Bioluminescence Assay Kit CLS II, and RNeasy Mini Kit can be invaluable in your research.
Uncovering the secrets of these unique creatures, from their uniqe defense mechanisms to their potential medicinal applications, could lead to groundbreaking discoveries.
So dive into the world of pufferfish research and let the power of PubCompare.ai guide you to the most accurate and reproducible protocols, enhancing your studies and contributing to our understanding of these remarkable fish.
These remarkable creatures belong to the order Tetraodontiformes and are found in tropical and subtropical waters around the globe.
Characterized by their distinctive round, spiny bodies, pufferfish have developed a remarkable defense mechanism - they can inflate themselves with water or air to appear larger and deter predators.
This adaptation has made them highly sought-after in some cuisines, but it also means they contain a potent neurotoxin that can be fatal if not properly prepared.
Researchers are continually exploring the biology, behavior, and potential medicinal applications of these fascinating fish.
Tools like PubCompare.ai can help optimize pufferfish research by enabling users to find the most accurate and reproducible protocols from literature, preprints, and patents.
Leveraging AI-driven comparisons, this tool enhances the accuracy and reproducibility of pufferfish studies.
Whether you're studying pufferfish behavior, ecology, or pharmacology, techniques like the PcDNA3.1 expression vector, High-Capacity cDNA Reverse Transcription Kit, ATP Bioluminescence Assay Kit CLS II, and RNeasy Mini Kit can be invaluable in your research.
Uncovering the secrets of these unique creatures, from their uniqe defense mechanisms to their potential medicinal applications, could lead to groundbreaking discoveries.
So dive into the world of pufferfish research and let the power of PubCompare.ai guide you to the most accurate and reproducible protocols, enhancing your studies and contributing to our understanding of these remarkable fish.