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Heat-Shock Proteins 70

Heat-Shock Proteins 70 (HSP70) are a family of highly conserved molecular chaperones that play a critical role in cellular proteostasis.
These proteins assist in the folding, trafficking, and degradation of other proteins, helping to maintain proper protein structure and function under normal and stressful conditions.
HSP70s are upregulated in response to a variety of cellular stressors, including heat, oxidative damage, and pathogen infection.
They are involved in a wide range of biological processes, from protein quality control to immune regulation.
Researchers studying HSP70 can leverage the PubCompare.ai platform to easily locate and compare experimental protocols from the literature, preprints, and patents, identifing the most effective approaches to enhance reproducibility and accuracy in their HSP70 research.
Explore this leading AI-powered tool to take your HSP70 studies to new hights.

Most cited protocols related to «Heat-Shock Proteins 70»

1
CRISPR-Cas9 Genome Editing in Cells
Cited 336 times
For human cells, expression vector PX330 (Addgene plasmid 42230) encoding Cas9 and chimeric guide RNA was used (11 (link)). The LBR guides were cloned into expression vector pBluescript with the sgRNA cassette of PX330 and transfected into the K562 line stably transformed with Cas9. For Drosophila cells, Cas9 expression vector pBS-Hsp70-Cas9 (Addgene plasmid 46294) was used in combination with pU6-BbsI-chiRNA construct (Addgene plasmid 45946) (12 (link)). The sgRNAs were designed using CRISPR design (http://crispr.mit.edu/) (13 (link)) and CHOPCHOP (https://chopchop.rc.fas.harvard.edu/) (14 (link)).
The following sgRNA sequences were used:
For the cloning of individual DNA fragments from the edited GFP gene, PCR products were ligated in Zero Blunt vector (Invitrogen) using standard procedures.
Brinkman E.K., Chen T., Amendola M, & van Steensel B. (2014). Easy quantitative assessment of genome editing by sequence trace decomposition. Nucleic Acids Research, 42(22), e168.
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Publication 2014
Cells Chimera Cloning Vectors Clustered Regularly Interspaced Short Palindromic Repeats Drosophila Genes Heat-Shock Proteins 70 Homo sapiens Plasmids
2
Zebrafish Ventricular Resection and Regeneration
Cited 40 times
Outbred Ekkwill strain (EK) or EK/AB mixed background zebrafish 6–12 months of age were used for ventricular resection surgeries as described previously4 (link). All transgenic strains were analyzed as hemizygotes; details of their construction are described in the separate Methods section. Animal density was maintained at ~4 fish/liter in all experiments. 4-hydroxytamoxifen (4-HT) (Sigma) dissolved with ethanol (5 mg/ml) was diluted in water to 0.5 mg/ml for intraperitoneal injections. 10% ethanol was used as a vehicle control. EGFP labeling quantification is described in the separate Methods section. Heat-shock experiments were performed as described previously27 (link), using double transgenic hsp70:dnfgfr1; cmlc2:nucDsRed2 or hsp70:dnfgfr1; gata4:EGFP animals. For BrdU incorporation experiments, 2.5 mg/ml BrdU (Sigma) was injected intraperitoneally once daily for 3 days prior to collection. Immunofluorescence, in situ hybridization, and Acid Fuchsin Orange G stains (detecting fibrin and collagen) were performed as described previously4 (link). Primary antibodies used in this study were: anti-Mef2 (rabbit; Santa Cruz Biotechnology), anti-Myosin heavy chain (F59, mouse; Developmental Studies Hybridoma Bank), anti-β-catenin (rabbit; Sigma), anti-zf Raldh2 (rabbit: Abmart), anti-BrdU (rat; Accurate), and anti-GFP (rabbit, used only for co-detection with BrdU; Invitrogen). Secondary antibodies (Invitrogen) used in this study were Alexa Fluor 594 goat anti-rabbit IgG (H+L) for anti-Mef2, Alexa Fluor 594 goat anti-mouse IgG (H+L) for F59, Alexa Fluor 594 goat anti-rat IgG (H+L) for anti-BrdU, and Alexa Fluor 488 goat anti-rabbit IgG (H+L) for anti-GFP. In situ hybridization and immunofluorescence images were taken using a Leica DM6000 microscope with a Retiga-EXi camera (Q-IMAGING), and confocal images were taken using a Leica SP2 or SP5 confocal microscope. Physiology methods are described in the separate Methods section.
Kikuchi K., Holdway J.E., Werdich A.A., Anderson R.M., Fang Y., Egnaczyk G.F., Evans T., MacRae C.A., Stainier D.Y, & Poss K.D. (2010). Primary contribution to zebrafish heart regeneration by gata4+ cardiomyocytes. Nature, 464(7288), 601-605.
Publication 2010
acid-fuchsin afimoxifene ALDH1A2 protein, human Alexa594 alexa fluor 488 Animals Animals, Transgenic anti-IgG Antibodies Bromodeoxyuridine Collagen CTNNB1 protein, human Ethanol Fibrin Fishes Fluorescent Antibody Technique Goat Heart Ventricle Heat-Shock Proteins 70 Heat-Shock Response Hemizygote Hybridomas Injections, Intraperitoneal In Situ Hybridization Mice, House Microscopy Microscopy, Confocal Myosin Heavy Chains Operative Surgical Procedures Orange G physiology Rabbits Staining Strains Zebrafish
3
PCR Verification of RMCE Integration
Cited 37 times
For PCR verification of RMCE integration events, DNA was extracted from 10 to 15 adult flies using the PureLink™ Genomic DNA Mini Kit (Invitrogen). PCR was performed with tag-specific primers and MiMIC specific primers. Tag-specific primers (Tag-F and Tag-R) are mCherry-Seq-F and mCherry-Seq-R for mCherry, EGFPdo-Seq-F and EGFPdo-Seq-R for EGFP, EBFP2do-Seq-F and EBFP2do-Seq-R for EBFP2, TagRFPdo-Seq-F and TagRFPdo-Seq-R for TagRFP, Hrpdo-Seq-F and Hrpdo-Seq-R for HRP, Dendrado-Seq-F and Dendrado-Seq-R for Dendra, Killerreddo-Seq-F and Killerreddo-Seq-R for Killerred, GAL4-1R and GAL4-5F for GAL4, FLP0-Seq-R and SV40pA-Long-F for Flpo, and QF-Seq-R1 and Hsp70-pA-Alt-F for QF. MiMIC specific primers are Orientation-MiL-F and Orientation-MiL-R. PCR reaction conditions were: 1 μl DNA, 1 μl primer 1, 1 μl primer 2, 2 μl 10× Buffer, 0.16 μl dNTPs (25 mM each), 0.08 μl Qiagen HotStarTaq DNA Polymerase (QIAGEN), 14.76 μl milliQ water. PCR cycling conditions in PTC-225 or DNA Engine (MJ Research) were: denaturation at 94° for 10 minutes, 40 cycles at 94° for 30 seconds, 60° for 30 seconds and 72° for 60 seconds, and post-amplification extension at 72° for 10 minutes.
For each RMCE event, 4 PCR reactions were performed: a first PCR reaction with primers Orientation-MiL-F and Tag-R, a second PCR reaction with primers Orientation-MiL-F and Tag-F, a third PCR reaction with primers Orientation-MiL-R and Tag-R, and a fourth PCR reaction with primers Orientation-MiL-R and Tag-F. Since the transposon integrates one or two orientations relative to the gene, only one in two RMCE events is productive with respect to creating a gene trap or protein trap, which is reflected in a positive PCR for reactions 1 and 4, or 2 and 3. A “1/4” PCR pattern is always desired for a productive RMCE event (for example a gene or protein trap), when the gene/transposon configuration is 1/1 or −1/−1. Conversely, a “2/3” PCR pattern is diagnostic of a productive RMCE event, when the gene/transposon configuration is 1/−1 or −1/1. The reverse holds for unproductive RMCE events (Supplementary Figure 2).
Venken K.J., Schulze K.L., Haelterman N.A., Pan H., He Y., Evans-Holm M., Carlson J.W., Levis R.W., Spradling A.C., Hoskins R.A, & Bellen H.J. (2011). MiMIC: a highly versatile transposon insertion resource for engineering Drosophila melanogaster genes. Nature methods, 8(9), 737-743.
Publication 2011
Adjustment Disorders Adult Buffers Diagnosis Diptera DNA-Directed DNA Polymerase Gene Order Genes Genome Heat-Shock Proteins 70 Jumping Genes Mental Orientation Oligonucleotide Primers Proteins
4
Versatile Dual-Reporter Transgenic Fly Lines
Cited 30 times
Synthetic double stranded oligonucleotides, carrying four high affinity AP-1 or Nrf2 binding sites or a mutant control (4×ARE, 4×TRE and 4×mRE, see Fig. 1B) were inserted into modified pGL3-Basic, a plasmid that includes Drosophila Hsp70 minimal promoter driving the expression of firefly luciferase gene [42] (link) (kindly provided by Dr. Michael Boutros) to generate cell-based reporter plasmids. The in vivo reporter plasmids were generated in multiple steps. 4×ARE was transferred into the pGreen H-Pelican vector to generate pGreen-ARE. The attB sequence from piB-GFP [43] (link) plasmid was inserted into pBSKS vector to generate pBSKS-attB plasmid. The ARE-eGFP cassette along with the flanking gypsy insulators was amplified by PCR and inserted into pBSKS-attB to generate pB-ARE-green. The 4×ARE promoter element and eGFP reporter gene of this plasmid was replaced with other promoter elements (e.g., 4×TRE, 4×mRE) and other reporter genes (e.g., DsRed.T4), respectively, to generate plasmids with different combinations of promoters and reporters.
ΦC31 recombinase-mediated site-directed transgenesis was used to generate transgenic fly lines (service provided by Genetic Services Inc, MA). Individual reporter fly lines were then recombined with other reporter fly lines to facilitate the simultaneous study of two different promoter elements in the same organism. For overexpression or RNAi experiments in which genetic effects on reporter activity were analyzed, the reporter lines were also recombined with different driver lines (e.g, arm-Gal4, tubGS-Gal4).
Plasmids maps and sequence files are included as Text S1.
Chatterjee N, & Bohmann D. (2012). A Versatile ΦC31 Based Reporter System for Measuring AP-1 and Nrf2 Signaling in Drosophila and in Tissue Culture. PLoS ONE, 7(4), e34063.
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Publication 2012
Animals, Transgenic Binding Sites Cells Cloning Vectors Drosophila GA-Binding Protein Transcription Factor Gene Expression Genes, Reporter Gypsies Heat-Shock Proteins 70 Luciferases, Firefly Microtubule-Associated Proteins Oligonucleotides Paragangliomas 3 Plasmids Recombinase Reproduction RNA Interference Service, Genetic
5
Gene-Trap Cassette Construction for Lineage Tracing
Cited 28 times
A gene-trap cassette incorporating the Mhc intron 18 SA site51 (link) was PCR amplified from pP-GC (gift of Xavier Morin and William Chia)15 (link) with primers SA-XbaI-F and SA-PstI-R. The resulting PCR fragment was cut with XbaI and PstI and subcloned into pBS-KS-attB1-2, cut with XbaI and PstI, resulting in the mini gene-trap plasmid, pBS-KS-attB1-2-GT-SA. The SA is followed by a multiple cloning site (PstI, EcoRI, XhoI, BamHI and HindIII).
A mutagenic GAL4 gene-trap cassette, encompassing the GAL4 coding sequence and Hsp70 polyadenylation signal, was obtained from plasmid pChs-GAL4 (Drosophila Genomics Resource Center)55 (link), and PCR amplified with primers GAL4-Hsp70-EcoRI-F and GAL4-Hsp70-BamHI-R. A mutagenic QF gene-trap cassette, encompassing the QF coding sequence and Hsp70 polyadenylation signal, was obtained from plasmid pattB-QF-Hsp70 (Addgene)30 (link), and PCR amplified with primers QF-SV40-EcoRI-F and QF-SV40-BamHI-R. A mutagenic Flp fate mapping gene-trap cassette, encompassing the FLPo56 (link) coding sequence and SV40 polyadenylation signal, was obtained from plasmid pQUAS-DSCP-Flpo (Addgene)30 (link), and PCR amplified with primers Flpo-SV40-EcoRI-F and Flpo-SV40-BamHI-R. The resulting PCR fragments were cut with EcoRI and BamHI and subcloned into pBS-KS-attB1-2-GT-SA, cut with EcoRI and BamHI, resulting in the plasmids pBS-KS-attB1-2-GT-SA-GAL4-Hsp70, pBS-KS-attB1-2-GT-SA-Flp-SV40, and pBS-KS-attB1-2-GT-SA-QF-Hsp70 respectively.
Venken K.J., Schulze K.L., Haelterman N.A., Pan H., He Y., Evans-Holm M., Carlson J.W., Levis R.W., Spradling A.C., Hoskins R.A, & Bellen H.J. (2011). MiMIC: a highly versatile transposon insertion resource for engineering Drosophila melanogaster genes. Nature methods, 8(9), 737-743.
Publication 2011
Deoxyribonuclease EcoRI Drosophila Genes Heat-Shock Proteins 70 Introns morin Mutagenesis Oligonucleotide Primers Open Reading Frames Plasmids Polyadenylation Salvia hispanica seed Simian virus 40

Most recents protocols related to «Heat-Shock Proteins 70»

1
Protein Expression Analysis in Cells
The cells of each group were lysed in lysis buffer. Determine the quality of the harvested protein by used BCA kit. Then, 20 μg of total proteins was separated in SDS-PAGE gels and transferred to PVDF membrane. The membranes were blocked for 1 h at room temperature and incubated overnight at 4 °C with the relevant antibodies: anti-ALP antibody (1:1000, Abcam, USA), anti-OCN antibody (1:1000, Abcam, USA), anti-RUNX2 antibody (1:1000, Abcam, USA), anti-SLIT2 antibody (1:1000, Abcam, USA), anti-CD63 antibody (1:1000, Abcam, USA), anti-TSG101 antibody (1:1000, Abcam, USA), anti-HSP70 antibody (1:1000, Abcam, USA) and anti-GAPDH antibody (1:10,000, Abcam, USA). Membranes were rinsed and incubated for 1 h with secondary antibodies (Abcam, USA). After three times of washing, membranes were exposed with the ECL kit. Bands were analyzed using ImageJ software (version 1.6 NIH) to analyze the relative expression levels of the above markers.
Su H., Yang Y., Lv W., Li X, & Zhao B. (2023). Bone marrow mesenchymal stem cell-derived exosomal microRNA-382 promotes osteogenesis in osteoblast via regulation of SLIT2. Journal of Orthopaedic Surgery and Research, 18, 185.
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Publication 2023
Antibodies Antibodies, Anti-Idiotypic Buffers GAPDH protein, human Gels Heat-Shock Proteins 70 polyvinylidene fluoride Proteins RUNX2 protein, human SDS-PAGE Tissue, Membrane TSG101 protein, human
2
Western Blotting of Cellular and Exosomal Proteins

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Publication 2023
Actins Antibodies Chemiluminescence CTSK protein, human Exosomes Heat-Shock Proteins 70 Immunoglobulins Milk, Cow's Proteins SDS-PAGE Tissue, Membrane
3
Quantifying Mucosal HIF1α and HSP70 Levels
To quantify the mucosal protein level of HIF1α, an enzyme linked immunosorbent assay (ELISA) was performed. For this purpose, mucosal tissue sections from each sample were snap frozen in liquid nitrogen, and stored at −80°C until further processing. The mucosal tissue was then homogenized in a lysis buffer (NP40 lysis buffer: 150 mM NaCl, 1.0 % NP-40 (Nonidet P40, Boehringer Mannheim, Mannheim, Germany, #1332473), 50 mM Tris pH 8.0, 5 mM EDTA, 1× Protease inhibitor mix, SIGMA-Aldrich, St. Louis, MO, USA, #P8340) using a high-speed homogenisator (FastPrep-24™ 5G, MP Biomedicals Germany GmbH, Eschwege, Germany). Protein content of each individual homogenized sample was assessed by performing a Bradford assay, as described previously (31 (link)). A commercial ELISA Kit (Horse hypoxia inducible factor 1, alpha subunit ELISA Kit, MyBioSource, San Diego, California, United States) was performed in accordance with the manufacturer's instructions. Only a small alteration in the protocol was made, diluting the HIF protein standard 1:1 in NP40 buffer, to correct for the presences of this buffer in the samples. Optical density was measured using a microplate reader set to 450 nm (Multiscan GO, Thermo Fisher Scientific GmbH, Dreiech, Germany). The accompanying software (SkanIt Software 6.0.2 for Microplate Readers RE, ver. 6.0.2.3) was used to plot the concentration curves, with r > 0.97 considered acceptable. The measured values were within the detection limit and standard range of the kit. To correct for differences in protein content between the individual samples after homogenisation, the HIF protein level was expressed in pg per mg protein in the sample.
To ensure that the HIF protein levels in the samples were not decreased due to generalized protein degradation in the sample, the housekeeping protein Heat Shock Protein 70 (HSP-70) was also determined in the same samples with a commercial ELISA kit (Horse Heat Shock Protein 70 ELISA Kit, MyBioSource, San Diego, California, United States). This was performed in accordance with the manufacturer's instructions using the same small alteration as described above for the HIF ELISA, as well as the same measurement and calculation.
Verhaar N., de Buhr N., von Köckritz-Blickwede M., Dümmer K., Hewicker-Trautwein M., Pfarrer C., Dengler F, & Kästner S. (2023). Hypoxia signaling in the equine small intestine: Expression and distribution of hypoxia inducible factors during experimental ischemia. Frontiers in Veterinary Science, 10, 1110019.
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Publication 2023
Biological Assay Buffers Edetic Acid Enzyme-Linked Immunosorbent Assay Equus caballus Freezing Glycoprotein Hormones, alpha Subunit Heat-Shock Proteins 70 Hypoxia-Inducible Factor 1 Hypoxia-Inducible Factor 1, alpha Subunit Mucous Membrane Nitrogen nonidet Nonidet P-40 Protease Inhibitors Proteins Proteolysis Sodium Chloride Tromethamine Vision
4
Investigating HSP70/HSP40 Chaperone Activity
To investigate the effect of GO‐Y030 on HSP70/HSP40‐mediated chaperone activity in the cell‐free system, we employed an HSP70/HSP40 Glow‐Fold Protein Refolding Kit (Boston Biochem, Bio‐Techne Corp.) and performed an assay in accordance with the manufacturer's protocol with modifications. In brief, Glow‐Fold Substrate protein equivalent to luciferase protein was mixed with HSP70/HSP40 complex, ATP, and the compounds to be examined or dimethylsulfoxide alone. The concentration of the HSP70 inhibitors was as: PFT‐μ, 0.8 mm; VER‐155008, 0.4 mm; and JG98, 5 μm. The reactions were exposed to 45 °C for 7 min and then placed in 30 °C to initiate refolding reactions. After the indicated times, aliquots taken from each of the reactions were mixed with luciferin reagent and luciferase activity was measured using a TECAN Infinite 200 microplate reader. Average luminescence was measured as counts per second from three independent experiments and the data are presented as a percentage of the refolding activity. The refolding activity of each sample before heat shock was set as 100%.
Suzuki M., Yamamoto Y., Nishijima‐Matsunobu A., Kawasaki Y., Shibata H, & Omori Y. (2023). A curcumin analogue GO‐Y030 depletes cancer stem cells by inhibiting the interaction between the HSP70/HSP40 complex and its substrates. FEBS Open Bio, 13(3), 434-446.
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Publication 2023
Biological Assay Cell-Free System DNAJB1 protein, human Heat-Shock Proteins 70 Heat-Shock Response HSP40 Heat-Shock Proteins inhibitors Luciferases Luciferins Luminescence Molecular Chaperones Proteins Sulfoxide, Dimethyl VER 155008
5
Extracellular HSP70-1A Quantification by ELISA
An antibody‐sandwich ELISA was used for detection of extracellular HSP70‐1A in culture medium. Briefly, PC3 cells were incubated at 37 °C for 24 h in RPMI 1640 medium with or without 2 μm GO‐Y030. The conditioned medium was collected and centrifuged at 450 g at 4 °C for 10 min and the supernatant was stored. 96‐well microtiter ELISA plates (Sumitomo Bakelite Co., Ltd, Tokyo, Japan) were coated with anti‐HSP70 mouse mAb clone 4E7E5 (Proteintech, 2 μg·mL−1) in 0.1 m carbonate–bicarbonate buffer (pH 9.6) at 4 °C overnight. The wells were rinsed three times with water and coated with the blocking buffer, PBS containing 0.2% (w/v) BSA, at room temperature for 30 min. After three washes, samples were added to the wells and incubated at room temperature for 2 h. The wells were rinsed with water and incubated with 50 μL of anti‐HSP70 rabbit pAb (Proteintech) (dilution 1 ∶ 800) at room temperature for 2 h. The detection procedure is the same as the substrate‐binding activity assay.
Suzuki M., Yamamoto Y., Nishijima‐Matsunobu A., Kawasaki Y., Shibata H, & Omori Y. (2023). A curcumin analogue GO‐Y030 depletes cancer stem cells by inhibiting the interaction between the HSP70/HSP40 complex and its substrates. FEBS Open Bio, 13(3), 434-446.
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Publication 2023
bakelite Biological Assay Buffers Carbonates Clone Cells Culture Media, Conditioned Enzyme-Linked Immunosorbent Assay Heat-Shock Proteins 70 Immunoglobulins Ion, Bicarbonate Mus PC 3 Cell Line Rabbits Technique, Dilution

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HSP70 is a laboratory product that functions as a molecular chaperone. It assists in the folding and unfolding of proteins, helping to maintain their proper structure and function. HSP70 is widely used in various research applications.
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More about "Heat-Shock Proteins 70"

Heat-Shock Protein 70 (HSP70) is a highly conserved and critical molecular chaperone that plays a vital role in cellular proteostasis.
These proteins, also known as stress proteins or heat-shock proteins, assist in the folding, trafficking, and degradation of other proteins, helping to maintain proper protein structure and function under normal and stressful conditions.
HSP70s are upregulated in response to a variety of cellular stressors, including heat, oxidative damage, and pathogen infection.
They are involved in a wide range of biological processes, from protein quality control to immune regulation.
Researchers studying HSP70 can leverage the PubCompare.ai platform to easily locate and compare experimental protocols from the literature, preprints, and patents, identifying the most effective approaches to enhance reproducibility and accuracy in their HSP70 research.
Exploring the PubCompare.ai platform can help researchers optimize their HSP70 studies by providing access to a wealth of information on related techniques and products, such as PVDF membranes for Western blotting, TRIzol reagent for RNA extraction, and Lipofectamine 2000 for transfection.
Additionally, the platform can assist in the identification of reliable antibodies, such as Anti-HSP70 (Ab2787), to ensure accurate and reliable results in their HSP70 experiments.
By leveraging the insights and tools provided by PubCompare.ai, researchers can take their HSP70 studies to new heights, enhancing the reproducibility, accuracy, and impact of their work.