Biospectrometer

Manufactured by Eppendorf

Sourced in Germany, United States, Italy, United Kingdom, Austria

The BioSpectrometer is a versatile lab equipment for measuring the absorbance of various samples across a range of wavelengths. It provides accurate and reliable spectrophotometric analysis for life science applications.

Automatically generated - may contain errors

Lab products found in correlation

Spelling variants of this product

BioSpectrometer basic (79 citations) BioSpectrometer Kinetic (26 citations) BioSpectrometer fluorescence (11 citations) BioSpectrometer spectrophotometer (5 citations) BioSpectrometer Plus (4 citations) UV-Vis BioSpectrometer (4 citations) BioSpectrometer basic system (2 citations) UV Eppendorf BioSpectrometer (2 citations) Eppendorf Spectrophotometer (UV‐Vis BioSpectrometer), (1 citations)

312 protocols using biospectrometer

Quantification of Plant Sugars and Starch

Check if the same lab product or an alternative is used in the 5 most similar protocols

Total soluble sugars were extracted from leaves with 80% ethanol and employing a modified method [9 (link),54 (link)]. Fresh leaves, each containing 0.1 g of plant tissue, were taken in triplicate. The total soluble sugar content was measured at 620 nm by a Biospectrometer (Eppendorf, Hamburg, Germany) using glucose as the standard. The contents of soluble sugars are expressed as mg g⁻¹ FW.
Glucose, fructose and sucrose were extracted from the leaves using the method in Lu and Sharkey [55 (link)]. Fresh leaves, each containing 0.1 g of plant tissue, were taken in triplicate. The sugar concentrations were measured as described Stitt et al., 1989 and a Biospectrometer [56 ] (Eppendorf, Hamburg, Germany). To analyze starch content, the resulting sediments from aqueous ethanol extractions were autoclaved for 3 h in distilled H₂O and enzymatically digested to glucose according to the method described by Walters et al. [57 (link)]. α-amylase and amyloglucosidase from the Total Starch Kit were used to digest amylose and amylopectin into glucose. (Megazyme International Ireland Ltd.,Wichlow, Ireland, K-TSTA-100A). The sugar concentrations were determined enzymatically with a method described by Stitt et al., 1989 using a Biospectrometer [56 ] (Eppendorf, Hamburg, Germany).

Kim T.L., Lim H., Chung H., Veerappan K, & Oh C. (2022). Elevated CO2 Alters the Physiological and Transcriptome Responses of Pinus densiflora to Long-Term CO2 Exposure. Plants, 11(24), 3530.

+ Open protocol

+ Expand

Enzymatic Activity Assays for Hexokinase and G6PD

Check if the same lab product or an alternative is used in the 5 most similar protocols

Samples were lysed in a non-denaturant lysis buffer (50 mM Tris-HCl, pH 7.5, 1 mM EDTA, 150 mM NaCl, 1% NP-40, 1 mM DTT, protease inhibitor cocktail) for 30 min on ice and centrifuged at 10,000×g for 20 min at 4 °C. For the hexokinase activity, 50 μg of protein lysate was added to an equal volume of reaction buffer (50 mM Tris-HCl, pH 7.5, 10 mM MgCl₂, 0.6 mM ATP, 100 mM glucose, 0.2 mM NADP⁺, 0.1 U/mL of glucose-6-phosphate dehydrogenase) for 30 min at 37 °C. The optical absorbance was measured at 340 nm every 15 s for 10 min with an Eppendorf BioSpectrometer®. HK activity was represented as changes in absorbance per minute (U) normalized on protein.
For the G6PD activity, 50 μg of protein lysate was added to an equal volume of reaction buffer containing 50 mM Tris, 1 mM MgCl₂, 100 μM NADP⁺, pH 8.1 and 200 μM glucose-6-phosphate and/or 6-phosphogluconate. G6PD activity was calculated as the difference between the combined activity of G6PD and 6-phosphogluconate dehydrogenase (for this reaction, the buffer contains both glucose-6-phosphate and 6-phosphogluconate) and the only activity of 6-phosphogluconate dehydrogenase (buffer contains only 6-phosphogluconate). The optical absorbance was measured at 340 nm every 30 s for 6 min with an Eppendorf BioSpectrometer® G6PD activity was represented as change in absorbance per minute (U) normalized on protein.

De Falco P., Lazzarino G., Felice F., Desideri E., Castelli S., Salvatori I., Ciccarone F, & Ciriolo M.R. (2022). Hindering NAT8L expression in hepatocellular carcinoma increases cytosolic aspartate delivery that fosters pentose phosphate pathway and purine biosynthesis promoting cell proliferation. Redox Biology, 59, 102585.

+ Open protocol

+ Expand

Nuclear and Whole Tissue Protein Extraction

Check if the same lab product or an alternative is used in the 5 most similar protocols

Three mice livers collected at each zeitgeber time point were pooled together to extract nuclear protein and whole-tissue protein.
Nuclear extractions: 0.3 g pooled tissues were homogenized with 800 μl Cytoplasmic Extraction Reagent I (CER I) buffer (NE-PER™ kit Thermo Fisher Scientific), and 8 μl protease inhibitor (Pierce™, Thermo Fisher Scientific). Nuclear proteins were extracted following the protocol provided by the manufacturer. Protein concentrations were measured using Bradford method (Eppendorf Biospectrometer).
Whole-tissue protein extractions: An aliquot of 0.1 g pooled tissues were lysed with 400 μl urea lysis buffer (8 M urea, 100 mM Tris-HCl pH 8.0), 4 μl protease inhibitor (Pierce™, Thermo Fisher Scientific) was added to protect protein from degradation and protein concentrations were measured using Bradford method (Eppendorf Biospectrometer).
KCs protein extractions: In total, 100 μl cell pellets were lysed with 400 μl urea lysis buffer (8 M urea, 100 mM Tris-HCl pH 8.0), 4 μl protease inhibitor (Pierce™, Thermo Fisher Scientific) was added to protect protein from degradation and protein concentrations were measured using Bradford method (Eppendorf Biospectrometer).

Wang Y., Song L., Liu M., Ge R., Zhou Q., Liu W., Li R., Qie J., Zhen B., Wang Y., He F., Qin J, & Ding C. (2018). A proteomics landscape of circadian clock in mouse liver. Nature Communications, 9, 1553.

+ Open protocol

+ Expand

RNA Isolation and Sequencing from Plant Tissues

Check if the same lab product or an alternative is used in the 5 most similar protocols

The harvested samples were pulverized, and total RNA was isolated from 200 mg of homogenized tissue. RNA was isolated according to a previously described method for plants with substantial amounts of polysaccharides and polyphenolic compounds [75 (link)]. RNA integrity was evaluated by chipbased capillary gel electrophoresis using a Bioanalyzer system (Agilent Technologies). RNA concentration was determined by absorbance at 260 nm using a UV spectrophotometer (BioSpectrometer Eppendorf). A sample of 500 ng of RNA was used as input material for the cDNA library preparation. One library for each plant organ was prepared using standard TruSeq RNA Sample Preparation Kit (Illumina) and sequenced using the Illumina NextSeq500 platform to obtain 150-bp paired-end reads. Files containing sequence reads and quality scores were deposited in the Short Read Archive (SRA) of the National Center for Biotechnology Information (NCBI). Accession number SRP156345.

Canedo-Téxon A., Ramón-Farias F., Monribot-Villanueva J.L., Villafán E., Alonso-Sánchez A., Pérez-Torres C.A., Ángeles G., Guerrero-Analco J.A, & Ibarra-Laclette E. (2019). Novel findings to the biosynthetic pathway of magnoflorine and taspine through transcriptomic and metabolomic analysis of Croton draco (Euphorbiaceae). BMC Plant Biology, 19, 560.

+ Open protocol

+ Expand

Antioxidant Activity Evaluation of AgNPs

Check if the same lab product or an alternative is used in the 5 most similar protocols

Antioxidant activity of AgNPs was determined using the previously reported protocol^{10 (link)}. Briefly, different concentrations (25–100 ppm) of synthesized AgNPs were prepared and 1.5 ml of these prepared concentrations was added to 1.5 ml of 0.25 mM DPPH solution. Mixtures were incubated in dark for 30 min and colour fading was observed. Absorbance was taken at 517 nm using Bio Spectrometer Eppendorf, Germany (Department of Zoology, DEI, Agra). Ascorbic acid was used as standard. Percent antioxidant activity for each sample was determined using the following formula

Percent radical scavenging activity = [A_{DPPH} - A_{S} {/A}_{DPPH}]

where, A_S = absorbance of DPPH solution with nanoparticles; A_DPPH = absorbance of DPPH solution without nanoparticles.

Yadav R, & Preet S. (2023). Comparative assessment of green and chemically synthesized glutathione capped silver nanoparticles for antioxidant, mosquito larvicidal and eco-toxicological activities. Scientific Reports, 13, 8152.

+ Open protocol

+ Expand

Minocycline Release from Chitosan Nanoparticles

Check if the same lab product or an alternative is used in the 5 most similar protocols

The CCM membrane (15 mm in diameter) and 5 μg of minocycline-loaded chitosan nanoparticles were incubated in 1 mL of PBS (pH 7.4) in a constant temperature oscillator (100 rpm) at 37 °C to determine the release of minocycline. At each time intervals (1, 3, 5, and 7 days), the supernatant was collected, and ultraviolet spectrophotometry (BioSpectrometer, Eppendorf, Germany) was used to measure the amount of minocycline released at 348 nm (n = 3). Then, all the PBS was collected and replaced with a fresh one. The concentrations of minocycline was calculated through comparisons with a standard curve.

Ma S., Adayi A., Liu Z., Li M., Wu M., Xiao L., Sun Y., Cai Q., Yang X., Zhang X, & Gao P. (2016). Asymmetric Collagen/chitosan Membrane Containing Minocycline-loaded Chitosan Nanoparticles for Guided Bone Regeneration. Scientific Reports, 6, 31822.

+ Open protocol

+ Expand

Transcriptome Analysis of Aging Rat Spinal Cord

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

All work conformed to the National Institutes of Health Guidelines for the Care and Use of Laboratory Animals and were approved by the Stony Brook University Institutional Animal Care and Use Committee and conducted under protocol #203692-23. Three-month and 17-month old Fisher 344 rats were were euthanized and transcardially perfused with heparinized saline-buffered with 5 mM H₂NaPO₄ to pH 7. LSC were rapidly removed and immediately frozen on dry ice and stored at -80 °C. Total RNAs were extracted from LSC using Qiazol extraction, and further purified with RNeasy spin columns following the manufacturer’s directions and as described previously [14 (link)]. Briefly, frozen tissues were placed on ice, Qiazol lysis reagent (Qiagen) was added immediately along with three or six 2.3 mm silica/zirconia beads (DRG and LSC, respectively), and homogenized in a BioSpec mini bead beater for 1.5 min and allowed to stand on ice for 5 min. Chloroform was added to comprise 1/5 of the total volume, and samples were mixed vigorously for 2 min and allowed to settle for 2 min before being centrifuged at 12,000 X g for 15 min at 4 °C. The upper aqueous phase was saved, mixed 1:1 with 70% ethanol, and subjected to RNeasy spin column purification (Qiagen). Final concentrations and 230/260/280 ratios were determined by nanodrop absorbancy using an Eppendorf BioSpectrometer.

Galbavy W., Lu Y., Kaczocha M., Puopolo M., Liu L, & Rebecchi M.J. (2017). Transcriptomic evidence of a para-inflammatory state in the middle aged lumbar spinal cord. Immunity & Ageing : I & A, 14, 9.

+ Open protocol

+ Expand

Analyzing PI3K/AKT Signaling in Cervical Cancer

Check if the same lab product or an alternative is used in the 5 most similar protocols

The p53 protein and proteins involved in the PI3K/AKT signaling pathway, including AKT, p-AKT(473), P13K and p-PI3K, were analyzed by Western blot. Transfected SiHa and CaSki cervical cancer cell lines were used for protein extraction using cOmplete™ Lysis-M EDTA-free (Roche, Sigma Aldrich, St. Louis, MO, USA), and protein concentration was measured by using a nanodrop spectrophotometer (Eppendorf BioSpectrometer^®, Macquarie Park, Australia, basic). The samples (200 µg) were loaded and separated using 10% SDS-polyacrylamide gel and transferred to a nitrocellulose membrane (BioRAD). The membranes were blocked with a 3% BSA solution. Each membrane was incubated with a specific antibody, including LAMB3 antibody (ab97765, 1:1000, Abcam, Cambridge, UK), PI3K antibody (p110 4255, 1:1000, cell signaling technology), pPI3K antibody (p-p85 4228, 1:1000, cell signaling technology), p53 antibody (p53 9282, 1:1000, cell signaling technology), and GAPDH antibody (sc-47724, 1:200, Santacruz Biotechnology). Secondary HRP-conjugated rabbit anti-mouse (ab205719) and HRP-conjugated anti-rabbit IgG (ab205718) antibodies (Abcam) were used. The protein was determined using a chemiluminescent detection method using the ChemiDoc XRS+ System (BIO-RAD). The intensity of the protein band was assessed using Image LabTM 6.0 software.

Wattanathavorn W., Seki M., Suzuki Y., Buranapraditkun S., Kitkumthorn N., Sasivimolrattana T., Bhattarakosol P, & Chaiwongkot A. (2024). Downregulation of LAMB3 Altered the Carcinogenic Properties of Human Papillomavirus 16-Positive Cervical Cancer Cells. International Journal of Molecular Sciences, 25(5), 2535.

+ Open protocol

+ Expand

LDH Cytotoxicity Assay for Cell Viability

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

LDH release was measured using an LDH Cytotoxicity Assay kit (cat. no. C0017; Beyotime Institute of Biotechnology) as previously described (42 (link)). Supernatants from Control, NC and OE-GAS5 MRC-5 cells were collected and 10% (vol/vol) LDH release reagent was added. LDH release was measured at an optical density of 490 nm using the Eppendorf BioSpectrometer fluorescence. Cytotoxicity was calculated as % × (experimental LDH release-cell spontaneous LDH release)/(maximum LDH release-cell spontaneous LDH release).

Mo R., Li J., Chen Y, & Ding Y. (2022). lncRNA GAS5 promotes pyroptosis in COPD by functioning as a ceRNA to regulate the miR-223-3p/NLRP3 axis. Molecular Medicine Reports, 26(1), 219.

+ Open protocol

+ Expand

Extracting RNA from Insect Antennae

Check if the same lab product or an alternative is used in the 5 most similar protocols

Around 10 mg of tissues (mixed antennae) were extracted by AG RNAex Pro Reagent (AG21102, Accurate Biotechnology, Hunan, Co., Ltd). The extracted RNA was first analyzed by gel electrophoresis on 1% (w/ V) agarose gel to detect the integrity of RNA, and then the concentration of RNA was measured by spectrophotometer (Eppendorf Bio Spectrometer). Solexa sequencing using an Illumina HiSeq 2000 was performed by Shenzhen Huada Gene Research Institute.

Zhang Y., Feng K., Mei R., Li W, & Tang F. (2022). Analysis of the Antennal Transcriptome and Identification of Tissue-specific Expression of Olfactory-related Genes in Micromelalopha troglodyta (Lepidoptera: Notodontidae). Journal of Insect Science, 22(5), 8.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!