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Biotin 1

Biotin 1 is a water-soluble B-complex vitamin that serves as a cofactor for carboxylase enzymes involved in critical metabolic pathways.
It plays a key role in the conversion of nutrients into energy, the synthesis of fatty acids and the metabolism of amino acids.
Biotin 1 is essential for cell growth, the development of the nervous system, and the maintainance of healthy skin and hair.
Deficiency in Biotin 1 can lead to symptoms such as skin rashes, hair loss, fatigue and neurological problems.
Resaerchers can utilize PubCompare.ai to identify the most accurate and reproducible protocols for studying Biotin 1 from the literature, preprints and patents, and compare methodolgies to optimize their experimental approaches.

Most cited protocols related to «Biotin 1»

1
Immunostaining for viral antigen detection
Cited 865 times
The streptavidin alkaline phosphatase method was adapted to detect the viral antigen using a polyclonal anti-ZIKV antibody produced at the Evandro Chagas Institute2 (link). The biotin-streptavidin peroxidase method was used for immunostaining of tissues with antibodies specific for each marker studied. First, the tissue samples were deparaffinized in xylene and hydrated in a decreasing ethanol series (90%, 80%, and 70%). Endogenous peroxidase was blocked by incubating the sections in 3% hydrogen peroxide for 45 min. Antigen retrieval was performed by incubation in citrate buffer, pH 6.0, or EDTA, pH 9.0, for 20 min at 90 °C. Nonspecific proteins were blocked by incubating the sections in 10% skim milk for 30 min. The histological sections were then incubated overnight with the primary antibodies diluted in 1% bovine serum albumin (Supplementary Table S1). After this period, the slides were immersed in 1 × PBS and incubated with the secondary biotinylated antibody (LSAB, DakoCytomation) in an oven for 30 min at 37 °C. The slides were again immersed in 1X PBS and incubated with streptavidin peroxidase (LSAB, DakoCytomation) for 30 min at 37 °C. The reactions were developed with 0.03% diaminobenzidine and 3% hydrogen peroxide as the chromogen solution. After this step, the slides were washed in distilled water and counterstained with Harris hematoxylin for 1 min. Finally, the sections were dehydrated in an increasing ethanol series and cleared in xylene.
Azevedo R.S., de Sousa J.R., Araujo M.T., Martins Filho A.J., de Alcantara B.N., Araujo F.M., Queiroz M.G., Cruz A.C., Vasconcelos B.H., Chiang J.O., Martins L.C., Casseb L.M., da Silva E.V., Carvalho V.L., Vasconcelos B.C., Rodrigues S.G., Oliveira C.S., Quaresma J.A, & Vasconcelos P.F. (2018). In situ immune response and mechanisms of cell damage in central nervous system of fatal cases microcephaly by Zika virus. Scientific Reports, 8, 1.
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Publication 2018
Alkaline Phosphatase Antibodies Antibodies, Anti-Idiotypic Antigens Antigens, Viral azo rubin S Biotin Buffers Citrates Edetic Acid Ethanol Hematoxylin Immunoglobulins Milk, Cow's Peroxidase Peroxide, Hydrogen Peroxides Proteins Serum Albumin, Bovine Streptavidin Tissues Tritium Xylene Zika Virus
2
Nextera LMP Library Construction and Adapter Trimming
Cited 156 times
Mate-pair library sequencing allows the generation of long-insert PE libraries that are useful in the scaffolding process of de novo genome assembly and in the detection of long-range genome structural variations. In the Nextera LMP library construction process, there are additional reactions called “tagmentation” and “circularization” before the normal PE library construction. The tagmentation reaction uses a specially engineered transposome to fragment the DNA sample and tag the DNA fragments by attaching a pair of biotinylated junction adapters simultaneously to the ends. Next, the tagmented DNA molecules are circularized and sheared by ultrasonics, and the sub-fragments containing the original junction parts are enriched via the biotin tag in the junction adapter.
Trimming adapters from Nextera LMP reads is like a reverse process of Nextera LMP library construction. To process Nextera mate-pair reads, the program first trims the adapters as if it is dealing with PE reads. Then, it trims junction adapters from the processed paired reads separately using the extended version of Algorithm 1.
Jiang H., Lei R., Ding S.W, & Zhu S. (2014). Skewer: a fast and accurate adapter trimmer for next-generation sequencing paired-end reads. BMC Bioinformatics, 15, 182.
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Publication 2014
Biotin DNA DNA Library Genome Genomic Structural Variation Ultrasonics
3
Optimizing Cardiac Differentiation of Pluripotent Stem Cells
Cited 139 times
Both hiPSCs and hESCs (>p20) were split at 1:10 or 1:12 ratios, using EDTA as above and grown for 4 days, at which time they reached ~85% confluence. Medium was changed to CDM3, consisting of RPMI 1640 (11875, Life Technologies), 500 µg/mL Oryza sativa-derived recombinant human albumin (A0237, Sigma-Aldrich, 75 mg/mL stock solution in WFI H2O, stored at −20 °C), and 213 µg/mL L-ascorbic acid 2-phosphate (Sigma-Aldrich, 64 mg/mL stock solution in WFI H2O, stored at −20 °C). Medium was changed every other day (48 h). For d0-d2, medium was supplemented with 6 µM CHIR99021 (LC Laboratories). On d2, medium was changed to CDM3 supplemented with 2 µM Wnt-C59 (Selleck Chemicals). Medium was changed on d4 and every other day for CDM3. Contracting cells were noted from d7.
Other additions to cardiac differentiation media tested were 10.7 µg/mL recombinant human transferrin, 14 µg/mL sodium selenite, 1 µg/mL linoleic acid, 1 µg/mL linolenic acid, 2 ng/mL triiodo-l-thyronine, 2 µg/mL L-carnitine, 1 µg/mL D,L-alpha-tocopherol acetate, 100 ng/mL retinol acetate, 1 µg/mL ethanolamine, 20 ng/mL corticosterone, 9 ng/mL progesterone, 47 ng/mL lipoic acid, 100 ng/mL retinol, 1 µg/mL D,L-alpha-tocopherol, 100 ng/mL biotin, 2.5 ug/mL catalase, 2.5 µg/mL glutathione, 2.5 µg/mL superoxide dismutase, 2 µg/mL L-carnitine, 15 µg/mL D(+)-galactose, 16.1 µg/mL putrescine, 450 µM 1-thioglycerol, 55 µM 2-mercaptoethanol, and 64 µg/mL L-ascorbic acid 2-phosphate (all from Sigma-Aldrich).
Basal media assessed were DMEM (catalogue #11965), DMEM/F12 (11330), IMDM (12440), IMDM/F12 (12440/11765), RPMI 1640 (11875), McCoy’s 5A (16600), M199 (with Earle’s Salts, 11150), MEMα (with Earle’s Salts, no nucleosides, 12561), and MEM (with Earle’s Salts, 11095) (all from Life Technologies). RPMI 1640 media assessed were RPMI 1640 with L-glutamine (catalogue number 11875), RPMI 1640 with L-glutamine and HEPES (22400), RPMI 1640 with GlutaMAX (61870), and RPMI with GlutaMAX and HEPES (72400) (all from Life Technologies).
Albumin sources assessed were human serum albumin (A1653, Sigma-Aldrich), Oryza sativa-derived recombinant human albumin (A0237, Sigma-Aldrich), Saccharomyces cerevisiae-derived recombinant Albucult (Novozymes Biopahrma/A6608, Sigma Aldrich), Oryza sativa-derived recombinant Cellastim (Invitria/A9731, Sigma Aldrich), and embryo-grade bovine serum albumin (A3311, Sigma Aldrich).
Wnt inhibitors assessed were IWP-2, IWR-1 (both Sigma-Aldrich), XAV-939, ICG-001 (Selleck Chemicals), IWP-4 (Stemgent), and Wnt-C59 (Selleck Chemicals). GSK3B inhibitors assessed were CHIR99021 (LC Laboratories), BIO, TWS119 (Selleck Chemicals), 1-azenkenpaullone, TDZD-8, ARA014418, and 3F8 (all Sigma-Aldrich). Inhibitors used for pathway analysis were PD173074, SB203580, LDN193189, SB431542 (all Selleck Chemicals), SU5402, Dorsomorphin, A83-01 (all Tocris), ALK5 inhibitor (Stemgent), and ITD-1 (Xcessbio). All small molecules were resuspended to 10 mM in dimethyl sulfoxide (DMSO) and used at 5 µM except for Wnt-C59 which was used at 2 µM.
For control treatments (0 µM) 0.1% DMSO was used. Comparisons of differentiation media were made to RPMI+B27-ins consisting of RPMI 1640 (11875) supplemented with 2% B27 without insulin (0050129SA, Life Technologies), and StemPro-34 (Life Technologies) supplemented as shown in Supplementary Table 1. LI-APEL low insulin medium and Xeno-free Differentiation Medium were made as described2 (link), 9 (link), 48 (link). For optimization of cardiac differentiation conditions, cells were differentiated in 12-well plates and samples were analyzed at day 15 of differentiation after dissociation with TrypLE Express for 10 min at 37 °C.
Burridge P.W., Matsa E., Shukla P., Lin Z.C., Churko J.M., Ebert A.D., Lan F., Diecke S., Huber B., Mordwinkin N.M., Plews J.R., Abilez O.J., Cui B., Gold J.D, & Wu J.C. (2014). Chemically Defined and Small Molecule-Based Generation of Human Cardiomyocytes. Nature methods, 11(8), 855-860.
Publication 2014
4
Curated CLIP-Seq Data Analysis
Cited 121 times
In cases where raw high-throughput data were available, curators obtained the relevant data sets, commented each library with extensive metadata and marked them for reanalysis in order to maintain optimal quality standards for all identified interactions. Specifically, data available from online repositories or supplemental materials of 1 CLASH, 31 PAR-CLIP and 122 HITS-CLIP libraries were analyzed and included in the database.
The CLIP-Seq analysis has been performed using an in-house developed pipeline. Regions formed by at least five overlapping reads were included to the analysis. For PAR-CLIP data, peaks containing adequate T-to-C (sense strand) or A-to-G (antisense strand) incorporation were selected. At least two transitions in the same position for peaks with less than 50 reads were required, while for the remaining regions we applied the threshold of >5%, as indicated by Hafner et al. (11 (link)). For all CLIP-Seq data sets having replicates, a peak had to be present in at least two replicates in order to be considered as valid. Where available, top expressed miRNAs were retrieved from the original publication. In all other instances, we analyzed publically available small-RNA-Seq libraries derived from the relevant cell lines. miRNA:gene interactions were inferred using a CLIP-peak-guided MRE search algorithm considering the miRNA:mRNA binding type, binding free energy, MRE conservation and AU flanking content.
Changes over 50% were utilized as a threshold for microarray and biotin pull-down experiments. In cases where replicates were available, an interaction had to be present in at least two replicates, in order to be included to the database.
Vlachos I.S., Paraskevopoulou M.D., Karagkouni D., Georgakilas G., Vergoulis T., Kanellos I., Anastasopoulos I.L., Maniou S., Karathanou K., Kalfakakou D., Fevgas A., Dalamagas T, & Hatzigeorgiou A.G. (2014). DIANA-TarBase v7.0: indexing more than half a million experimentally supported miRNA:mRNA interactions. Nucleic Acids Research, 43(Database issue), D153-D159.
Publication 2014
Biotin cDNA Library Cell Lines Clip Cross-Linking and Immunoprecipitation Followed by Deep Sequencing Genes High-Throughput Sequencing of RNA Isolated by Crosslinking Immunoprecipitation Lanugo Microarray Analysis MicroRNAs RNA, Messenger RNA-Seq
5
Quantifying Cysteine Reactivity with isoTOP-ABPP
Cited 103 times
Our approach, termed isoTOP-ABPP (isotopic Tandem Orthogonal Proteolysis – Activity-Based Protein Profiling), has four features to enable quantitative analysis of native cysteine reactivity (Fig. 1a): [1] an electrophilic iodoacetamide (IA) probe to label cysteine residues in proteins that also has [2] an alkyne handle for “click chemistry” conjugation of probe-labeled proteins19 (link) to [3] an azide-functionalized TEV-protease recognition peptide containing a biotin group for streptavidin-enrichment of probe-labeled proteins20 (link) and [4] an isotopically-labeled valine for quantitative mass spectrometry (MS) measurements of IA-labeled peptides across multiple proteomes (Supplementary Fig. 1). Following tandem on-bead proteolytic digestions with trypsin and TEV protease15 (link),20 (link), probe-labeled peptides attached to isotopic tags are released and analyzed by liquid chromatography-high-resolution MS to identify IA-modified cysteines and quantify their extent of labeling based on MS2 and MS1 profiles, respectively. An isoTOP-ABPP ratio, R, is generated for each identified cysteine that reflects the difference in signal intensity between light and heavy tag-conjugated proteomes.
We first verified the accuracy of isoTOP-ABPP by labeling varying amounts of a mouse liver proteome (1X, 2X, 4X) with the IA-probe followed by click chemistry conjugation with either the heavy- or light-variants of the azide-TEV-biotin tag. The observed signals for labeled cysteines closely matched the expected proteome ratios (R1:1 ≈ 1, R2:1 ≈ 2, or R4:1 ≈ 4, respectively; Supplementary Fig. 2). A representative MS/MS profile of an IA-labeled peptide from our proteomic experiments is provided in Supplementary Fig. 3.
In contrast to traditional cysteine-alkylating protocols for proteomics that use millimolar concentrations of IA to stoichiometrically modify all cysteines in denatured proteins21 (link), we hypothesized that, by applying low (micromolar) concentrations of the IA-probe to native proteomes, differences in the extent of alkylation would reflect differences in cysteine reactivity, rather than abundance. This hypothesis predicts that the reactivity of cysteines can be measured on a proteome-wide scale in isoTOP-ABPP experiments that compare low versus high concentrations of IA-probe, where hyperreactive cysteines would be expected to label to completion at low probe concentrations (generating isoTOP-ABPP ratios with R[high]:[low] ≈ 1) and less reactive cysteines should show concentration-dependent increases in IA-probe labeling (generating isoTOP-ABPP ratios with R[high]:[low] >> 1) (Supplementary Fig. 4). We tested this idea by performing four parallel isoTOP-ABPP experiments with the soluble proteome of the human breast cancer cell line MCF7 using pair-wise IA-probe concentrations of 10:10 μM, 20:10 μM, 50:10 μM and 100:10 μM (light:heavy). More than 800 probe-labeled cysteines were identified on 522 proteins, the vast majority of which exhibited escalating isoTOP-ABPP ratios (Fig. 1b) expected for reactions that did not reach completion over the tested probe concentration range. In contrast, a small subset of cysteines (< 10%) showed nearly identical ratios at all probe concentrations tested (R1:1 ≈ R2:1 ≈ R5:1 ≈ R10:1 ≈ 1, Fig. 1b, shaded blue box). An expanded analysis of multiple human cancer line (Supplementary Fig. 5 and Supplementary Table 1) and mouse tissue (Supplementary Fig. 6 and Supplementary Table 2) proteomes treated with low (10 μM) and high (100 μM) IA-probe concentrations revealed consistent isoTOP-ABPP ratios for individual cysteine residues, indicating that the propensity of a cysteine to display high IA reactivity is an intrinsic property of the residue (and presumably its local protein environment), and not, in general, contingent on features specific to a particular cell or tissue. Additionally, isoTOP-ABPP ratios showed no correlation with either protein abundance or peptide ion intensity (Supplementary Fig. 7), indicating that they were independent of potential MS-based ionization sources for saturation. Finally, we confirmed that similar isoTOP-ABPP ratios were obtained for cysteines in reactions where time rather than the concentration of probe was varied (Supplementary Fig. 8 and Supplementary Table 3), confirming that low isoTOP-ABPP ratios reflect rapid reaction kinetics (hyperreactivity), rather than saturable binding interactions (see Supplementary Discussion).
Weerapana E., Wang C., Simon G.M., Richter F., Khare S., Dillon M.B., Bachovchin D.A., Mowen K., Baker D, & Cravatt B.F. (2010). Quantitative reactivity profiling predicts functional cysteines in proteomes. Nature, 468(7325), 790-795.
Publication 2010

Most recents protocols related to «Biotin 1»

1
Biotin-tagged miRNA and rRNA Synthesis
The DNAs containing T7 RNA polymerase promoter and pri-miR-9-1 (137nt and 413nt) or pri-miR-29b-1 (144nt) (T7-RNA-polymerase-promoter-pri-miR-9-1/-pri-miR-29b-1) and helix 45 of 18S-rRNA (50nt) (T7-RNA-polymerase-promoter-18S-rRNA-45h) were separately amplified by PCR (Supplementary Table S1) from CD513B-pri-miR-9-1, CD513B-pri-miR-29b-1 and total RNA reverse transcribed cDNA. The 18S-rRNA-45h, pri-miR-9-1 and pri-miR-29b-1 RNAs were internally tagged with biotin by using Bio-16-UTP as well as ATP, UTP, CTP and GTP through T7 RNA polymerase transcription. Meanwhile, ac4C-pri-miR-9-1, ac4C-pri-miR-29b-1 and ac4C-18S-rRNA-45h RNAs were transcribed with ATP, UTP, GTP and N4-actylcytidine triphosphate (ac4CTP) as well as internally tagged with biotin by using Bio-16-UTP through T7 RNA polymerase transcription. Finally, all the transcribed RNAs were further purified from 8 M Urea/ 15% PAGE gel.
Zhang H., Lu R., Huang J., Li L., Cao Y., Huang C., Chen R., Wang Y., Huang J., Zhao X, & Yu J. (2024). N4-acetylcytidine modifies primary microRNAs for processing in cancer cells. Cellular and Molecular Life Sciences: CMLS, 81(1), 73.
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Publication 2024
2
PMP Biotinylation in CHO Cells
Not available on PMC !
The cells were cultured in 100 mm dishes under standard culture conditions, maintaining a temperature of 37°C with 5% CO 2 and appropriate humidity, following the guidelines recommended by ATCC. For the PMP biotinylation, the cells were washed three times with PBS to eliminate FBS (Fetal Bovine Serum) and other medium additives. The cells were then covered with growth medium containing 0.25 µM of either TurboID or TurboID-START, along with 1 mM ATP, 3 mM MgCl2, and 500 µM biotin. The biotinylation reaction was allowed to proceed for 30 minutes at 37°C. To stop the biotinylation reaction, the cells were transferred onto ice and washed ve times with PBS. The chemical biotinylation of PMPs was achieved using a commercially available EZ-link Sulfo-NHS-LC-Biotinylation kit (Thermo Scienti c, USA), following the instructions. CHO cells that were not biotinylated by TurboID, TurboID-START, or the chemical method were used as the negative control.
Sarihan M., Kasap M, & Akpinar G. (2024). Streamlined Biotinylation, Enrichment and Analysis for Enhanced Plasma Membrane Protein Identification Using TurboID and TurboID-Start Biotin Ligases. The Journal of membrane biology, 257(1-2).
Publication 2024
3
Multiparametric Flow Cytometry Analysis of MDSCs
Single-cell suspensions were stained with surface antibodies in cold FACS buffer (containing 1 × PBS supplemented with 1% FBS and 2 mM EDTA) for 30 min at 4°C, and red cells were removed using ACK lysing buffer. Flow cytometric analysis was performed by a CytoFLEX flow cytometer (Beckman Coulter). Flow cytometric sorting was performed by a MoFlo Astrios EQs flow cytometer cell sorter (Beckman Coulter). Data were analyzed by FlowJo V10 (TreeStar). Mouse MDSCs (CD11b+Gr1+), PMN-MDSCs (CD11b+Ly6G+Ly6Clo), and M-MDSCs (CD11b+Ly6G−Ly6Chigh) were analyzed by flow cytometer. After surface staining, LIVE/DEAD staining (Thermo Fisher) was used to exclude the dead cells. The following antimouse antibodies were purchased from eBioscience: biotin antimouse CD3 (clone 145-2C11), biotin antimouse CD4 (clone GK1.5), biotin antimouse CD8 (clone 53-6.7), biotin antimouse Gr1 (clone RB6-8C5), biotin antimouse CD11b (clone M1/70), biotin antimouse Ter119 (clone TER-119), biotin antimouse B220 (clone RA3-6B2), biotin antimouse NK1.1 (clone PK136), and APC streptavidin. The following antimouse antibodies were purchased from BioLegend: APC antimouse CD4 (clone GK1.5), APC/Cyanine7 antimouse CD8a (clone 53-6.7), FITC antimouse CD11b (clone M1/70), Brilliant Violet 421 antimouse CD11b (clone M1/70), PE antimouse Ly6G (clone 1A8), APC antimouse Ly6C (clone HK1.4), Percp-cy5.5 antimouse Ly6C (clone HK1.4), and PE antimouse Ly-6G/Ly-6C (Gr-1) (clone RB6-8C5).
Lin− cells are remaining cells in the bone marrow (BM) after exclusion of CD3, CD4, CD8, Gr1, CD11b, Ter119, B220, and NK1.1 positive cells [16 (link)]. The flow cytometric analysis and sorting for lin− cell in the BM from neonatal mice were performed: BM cells were stained with primary antibodies (biotin antimouse CD3, biotin antimouse CD4, biotin antimouse CD8, biotin antimouse Gr1, biotin antimouse CD11b, biotin antimouse Ter119, biotin antimouse B220, and biotin antimouse NK1.1) for 30 min at 4°C, and cells were then washed and restained with APC Streptavidin for 30 min at 4°C. Subsequently, cells were analyzed and sorted by flow cytometer.
Chen Y., Li H., Zhu L., Yang Q, & Zhou J. (2024). β-Glucan Subverts the Function of Myeloid Cells in Neonates. Journal of Immunology Research, 2024, 2765001.
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Publication 2024
4
Biotin Labeling of ACE2 Protein
Not available on PMC !
In biotin labeling studies, an amine-specific biotinylated agent, biotin N-hydroxyl-succinimide ester (NHS-Biotin; Sigma, USA), was dissolved in DMSO. Before adding biotin, the pH of the ACE2 protein solution was adjusted to 9 with 0.1 M carbonate buffer. 1 mg of ACE2 protein and 125 µg of biotin were combined and incubated at room temperature for 4 h. By overnight dialyzing against PBS, unreacted biotin was removed from the mixture.
Kılıç G., Demirkan E, & Yücel F. (2024). Development of Anti-idiotypic Monoclonal Antibody Mimicking SARS-CoV-2 Receptor Binding Domain. Molecular biotechnology.
Publication 2024
5
Delineate Innate Lymphoid and Macrophage Subsets
Stained cells underwent analysis utilizing FACS Canto II, and the resultant data were processed utilizing FlowJo version 10 software (Ashland, OR, USA). The following antibodies procured from eBioscience (Thermo Fisher Scientific, Waltham, MA, USA) were employed for the delineation of innate lymphoid cells: Biotin-CD3e (100304; clone: 145-2C11; 1/200), Biotin-CD45R/B220 (103204; clone: RA3–6B2; 1/200), Biotin-Gr-1 (108404; clone: RB6-8C5; 1/200), Biotin-CD11c (117304; clone: N418; 1/200), Biotin-CD11b (101204; clone: M1/70; 1/200), Biotin-Ter119 (116204; clone: TER-119; 1/200), Biotin-FceRIa (134304; clone: MAR-1; 1/200), FITC-Streptavidin (405202; 1/500), PE-Cy7-CD127 (135014; clone: A7R34; 1/100), Pacific Blue-CD45 (103116; clone: 30-F11; 1/100), PE-GATA-3 (clone: TWAJ; 1/50), APC-RORγ (clone: AFKJS-9; 1/50), and Fixable Viability Dye eFluor 780 (1/400) [20 (link),21 (link)]. Additionally, the following antibodies (eBioscience, San Diego, CA, USA) were utilized for the discrimination of M1 and M2 macrophages: APC-CD45.2 (17045482; clone: 104; 1/50), PE-F4/80 (12480182; clone: BM8; 1/50), APC-Cy7-CD11b (47011282; clone: M1/70; 1/50), FITC-CD206 (MA516870; clone: MR5D3; 1/50), and PE-Cy7-CD11c (25011482; clone: N418; 1/50) [22 (link)].
Hosomi Y., Okamura T., Sakai K., Yuge H., Yoshimura T., Majima S., Okada H., Senmaru T., Ushigome E., Nakanishi N., Satoh T., Akira S., Hamaguchi M, & Fukui M. (2024). IL-33 Reduces Saturated Fatty Acid Accumulation in Mouse Atherosclerotic Foci. Nutrients, 16(8), 1195.
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Publication 2024

Top products related to «Biotin 1»

1
Lightshift chemiluminescent emsa kit by Thermo Fisher Scientific
Sourced in United States, China, Germany
The LightShift Chemiluminescent EMSA Kit is a laboratory tool designed to detect and analyze protein-DNA interactions. It uses chemiluminescent detection to visualize and quantify the binding of proteins to specific DNA sequences.
2
Vectastain elite abc kit by Vector Laboratories
Sourced in United States, United Kingdom, Canada, Germany, France, Japan, Switzerland
The Vectastain Elite ABC kit is a specialized laboratory equipment used for the detection and visualization of target proteins or antigens in biological samples. It utilizes an avidin-biotin complex (ABC) system to amplify the signal, enabling researchers to achieve high sensitivity and consistent results in their immunohistochemical or immunocytochemical analyses.
3
Vectastain abc kit by Vector Laboratories
Sourced in United States, Canada, United Kingdom, Germany, Japan, France
The Vectastain ABC kit is a product by Vector Laboratories that is used for the detection of specific target antigens in tissue or cell samples. The kit includes reagents necessary for the avidin-biotin complex (ABC) method of immunohistochemistry. The core function of the Vectastain ABC kit is to provide a reliable and sensitive tool for the visualization of target molecules within a sample.
4
Streptavidin agarose bead by Thermo Fisher Scientific
Sourced in United States, China
Streptavidin agarose beads are a type of affinity chromatography resin. They consist of streptavidin, a protein that binds to biotin, immobilized on agarose beads. These beads are commonly used for the purification and immobilization of biotinylated molecules.
5
Bovine serum albumin (bsa) by Merck Group
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
6
Biotin rna labeling mix by Roche
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Biotin RNA Labeling Mix is a reagent used for the incorporation of biotin labels into RNA molecules during in vitro transcription or reverse transcription reactions. It enables the detection and analysis of labeled RNA samples through various downstream applications, such as northern blotting, microarray hybridization, or pull-down experiments.
7
3 3 diaminobenzidine (dab) by Merck Group
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3,3'-diaminobenzidine is a chemical compound commonly used as a chromogenic substrate in various laboratory techniques, such as immunohistochemistry and enzyme-linked immunosorbent assays (ELISA). It is a sensitive and specific reagent that can be used to detect the presence of target proteins or enzymes in biological samples.
8
Ez link sulfo nhs lc biotin by Thermo Fisher Scientific
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EZ-Link Sulfo-NHS-LC-Biotin is a water-soluble, amine-reactive biotinylation reagent. It is used to label proteins and other macromolecules with biotin, enabling detection and purification.
9
Rneasy mini kit by Qiagen
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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.

More about "Biotin 1"

Biotin, also known as vitamin B7 or vitamin H, is a crucial water-soluble B-complex vitamin that plays a vital role in various metabolic processes.
As a cofactor for carboxylase enzymes, Biotin is essential for the conversion of nutrients into energy, the synthesis of fatty acids, and the metabolism of amino acids.
It is crucial for cell growth, the development of the nervous system, and the maintenance of healthy skin and hair.
Deficiencies in Biotin can lead to symptoms such as skin rashes, hair loss, fatigue, and neurological problems.
Researchers can utilize tools like PubCompare.ai to identify the most accurate and reproducible protocols for studying Biotin from the literature, preprints, and patents.
By comparing methodologies side-by-side, researchers can optimize their experimental approaches and ensure the reliability of their findings.
This can be particularly useful when working with related techniques and products, such as the LightShift Chemiluminescent EMSA Kit, Vectastain Elite ABC kit, Vectastain ABC kit, Streptavidin agarose beads, Bovine serum albumin, Biotin RNA Labeling Mix, 3,3′-diaminobenzidine, and EZ-Link Sulfo-NHS-LC-Biotin.
The RNeasy Mini Kit is another valuable tool for researchers studying Biotin, as it provides a reliable and efficient way to extract and purify RNA from various samples.
By incorporating these insights and products into their research, scientists can unlock the full potential of Biotin and advance our understanding of its critical role in human health and metabolism.