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Cross-Linking Reagents

Cross-Linking Reagents are chemical agents used to establish stable connections between molecules, often proteins, to study their structure, interactions, and function.
These reagents can covalently link specific amino acid residues, enabling researchers to capture transient or weak associations, and provide insights into molecular organization.
By leveraging the power of AI-driven comparisons, the PubCompare.ai platform helps scientists effortlessly locate protocols and identify the best cross-linking reagents and products for their research needs, streamlining the discovery process and enabling more informed decisions.
Unleash the power of AI to revolutionize your cross-linking studies and uncover new biological insights.

Most cited protocols related to «Cross-Linking Reagents»

Protein Cross-linking Protocol for Mass Spectrometry

Individual stock solutions of the eight model proteins (bovine catalase, rabbit creatine kinase, rabbit fructose-bisphosphate aldolase, bovine lactoferrin, chicken ovotransferrin, rabbit pyruvate kinase, bovine serotransferrin, bovine serum albumin; all obtained from Sigma-Aldrich Buchs, Switzerland) were prepared at concentrations of 5–10 mg ml⁻¹ in 20 mm HEPES/KOH buffer (pH 8.2). Samples were diluted for each protein separately to a final concentration of 2 mg ml⁻¹ in the same buffer, and 4 μl of the cross-linker solution (25 mm each of DSS-d₀ and DSS-d₁₂ (Creative Molecules, Canada) in anhydrous DMF) were added per 100 μl protein solution. Samples were incubated for 30 min at 37 °C in an Eppendorf Thermomixer (mixing speed 750 rpm). Remaining cross-linking reagent was quenched by adding aqueous NH₄HCO₃ solution to a final concentration of 50 mm, followed by incubation for further 20 min. Aliquots of the individually cross-linked protein solutions were then combined and evaporated to dryness in a vacuum centrifuge before further processing.

Leitner A., Reischl R., Walzthoeni T., Herzog F., Bohn S., Förster F, & Aebersold R. (2012). Expanding the Chemical Cross-Linking Toolbox by the Use of Multiple Proteases and Enrichment by Size Exclusion Chromatography. Molecular & Cellular Proteomics : MCP, 11(3), M111.014126.

Publication 2012

Bos taurus Buffers Catalase Chickens Conalbumin Creatine Kinase Cross-Linking Reagents Fructosediphosphate Aldolase HEPES LTF protein, human Proteins Pyruvate Kinase Rabbits Serum Albumin, Bovine Transferrin Vacuum

NR2B Surface Expression Quantification

Surface expression of NR2B was assayed using a membrane-impermeable cross-linking reagent BS³, which only cross-links proteins on the surface of live cells23 (link). Brains were removed following anesthesia and sliced (400 μm). The striatum was dissected and added to eppendorf tubes containing ice-cold artificial cerebrospinal fluid (ACSF). BS³ (Pierce, Rockford, IL) was added to 2 mM and incubated with gentle agitation for 30 min at 4°C. The cross-linking reaction was terminated by quenching with 20 mM of glycine (10 min, 4°C). The tissue was then washed four times in cold ACSF (10 min each), homogenized to obtain total protein homogenate, and analyzed directly by SDS-PAGE (4–12% Tris-glycine gels, Invitrogen).

Mao L.M., Wang W., Chu X.P., Zhang G.C., Liu X.Y., Yang Y.J., Haines M., Papasian C.J., Fibuch E.E., Buch S., Chen J.G, & Wang J.Q. (2009). Stability of NMDA receptors at the plasma membrane controls synaptic and behavioral adaptations to amphetamine. Nature neuroscience, 12(5), 602-610.

Publication 2009

Anesthesia Brain Cerebrospinal Fluid Cold Temperature Cross-Linking Reagents Gels Glycine GRIN2B protein, human Membrane Proteins Proteins SDS-PAGE Striatum, Corpus Tissue, Membrane Tissues Tromethamine

Chromatin Immunoprecipitation and Sequencing of BldM and WhiI Regulators

For each strain, two flasks containing 35 ml of MYM were inoculated with spores (or mycelium in case of the ΔbldM mutant) to give an OD₆₀₀ ∼0.35 after 8 h of growth. The crosslinking reagent formaldehyde was added to a final concentration of 1% (v/v) to the cultures at 16 h of growth and incubated at 30°C with shaking for 30 min before glycine was added to a final concentration of 125 mM to quench the crosslinking reaction. The samples were incubated at room temperature for 5 min and washed twice in PBS buffer pH 7.4 (Sigma). Mycelial pellets were resuspended in 0.5 ml lysis buffer (10 mM Tris-HCl pH 8, 50 mM NaCl, 15 mg/ml lysozyme, 1x protease inhibitor) and incubated at 37°C for 20 min. The lysate was resuspended in 0.5 ml IP buffer (100 mM Tris- HCl pH 8, 250 mM NaCl, 0.1% Triton-X-100, 1x protease inhibitor) and the lysate was kept on ice for 2 min before sonication. The samples were subjected to seven cycles of sonication, 15 s each, at 10 microns, to shear the chromosome into fragments ranging in size from 300–1000 bp. The sample was then centrifuged twice at top speed, 4°C for 15 minutes to clear cell extracts. To pre-clear non-specific binding, 90 µl protein A sepharose (Sigma) was added to cell lysate (about 900 µl) and incubated for 1 h at 4°C with mixing. The beads were cleared by centrifugation at top speed for 15 min. 100 µl BldM or WhiI antibodies were added to the corresponding cell lysates overnight at 4°C with mixing. 100 µl Protein A Sepharose 1∶1 suspension was added to immunoprecipitate antibody-BldM or WhiI chromatin complexes and incubated for 4 h at 4°C with mixing. The samples were centrifuged at 3500 rpm for 30 s and the beads were washed four times with IP buffer. The pellets were eluted in 150 µl IP elution buffer (50 mM Tris-HCl pH 7.6, 10 mM EDTA, 1% SDS) overnight at 65°C to reverse crosslink. The samples were centrifuged at top speed for 5 min to remove the beads and the pellets were re-extracted with 50 µl TE buffer (10 mM Tris-HCl pH 7.4, 1 mM EDTA). The supernatants were combined and incubated with 3 µl 10 mg/ml proteinase K (Roche) for 2 h at 55°C. The samples were extracted twice with phenol-chloroform to remove protein followed by chloroform extraction to remove traces of phenol and purified with Qiaquick columns (Qiagen). The IP DNA was eluted in 50 µl EB buffer (Qiagen). Sequencing libraries were generated and the IP DNA was sequenced as described previously [20] (link). The BayesPeak package was used to identify significantly enriched regions and the default parameters were applied [56] (link).

Al-Bassam M.M., Bibb M.J., Bush M.J., Chandra G, & Buttner M.J. (2014). Response Regulator Heterodimer Formation Controls a Key Stage in Streptomyces Development. PLoS Genetics, 10(8), e1004554.

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Publication 2014

Antibodies Buffers Cell Extracts Cells Centrifugation Chloroform Chromatin Chromosomes Cross-Linking Reagents Edetic Acid Endopeptidase K Formaldehyde Glycine Immunoglobulins Muramidase Mycelium Pellets, Drug Phenol Protease Inhibitors Proteins Sodium Chloride Spores Staphylococcal protein A-sepharose Strains Triton X-100 Tromethamine

Measurement of AMPAR Subunit Levels

Cell surface and intracellular AMPAR subunit levels were determined using a protein crosslinking assay. Rats were taken directly from home cages and killed. A 2mm coronal section containing the NAc was obtained using a brain matrix (ASI Instruments, Inc., Warren, MI). A tissue punch was used to obtain the core (final diameter ~1.75mm) and then a scalpel was used to cut a crescent-shaped piece of tissue (shell) medial to the core punch (see Fig. 3B for a schematic of the dissection). Tissue samples were quickly minced with a scalpel and then incubated for 30 min at 4 ° C with 2mM bis(sulfosuccinimidyl)suberate (BS³; Pierce Biotechnology, Rockford, IL). BS³ is a bifunctional crosslinking reagent that does not cross membranes. Therefore, it selectively modifies surface-expressed proteins, increasing their apparent molecular weight and enabling them to be separated from unmodified intracellular proteins by SDS-PAGE and quantified by immunoblotting (see Ferrario et al., 2010 (link) for detailed procedures). Blots were processed exactly as described previously using primary antibodies to GluA1 (PA1-37776; Affinity Bioreagents, Rockford, IL), GluA2 (AB1768; Millipore, Billerica, MA) or GluA3 (3437; Cell Signaling Technology, Danvers, MA) and chemiluminescence detection. Values (diffuse densities) for surface, intracellular and total (surface + intracellular) protein levels were normalized to a loading control (GADPH; CB1001; Calbiochem, La Jolla, CA). For each of these measures (surface, intracellular and total protein) in each experiment, values from the cocaine group are expressed as percent of the mean value for a saline group run in parallel and killed on the same day.

McCutcheon J.E., Wang X., Tseng K.Y., Wolf M.E, & Marinelli M. (2011). Calcium-Permeable AMPA Receptors Are Present in Nucleus Accumbens Synapses after Prolonged Withdrawal from Cocaine Self-Administration But Not Experimenter-Administered Cocaine. The Journal of Neuroscience, 31(15), 5737-5743.

Publication 2011

Antibodies Biological Assay Brain Cells Chemiluminescence Cocaine Cross-Linking Reagents Dissection GRIA3 protein, human Membrane Proteins Proteins Protein Subunits Protoplasm Rattus norvegicus Saline Solution SDS-PAGE Staphylococcal Protein A Tissue, Membrane Tissues

Immunoblotting and Immunoprecipitation for Protein Analysis

Cells were collected and lysed in M2 buffer (20 mM Tris, pH 7, 0.5% NP40, 250 mM NaCl, 3 mM EDTA, 3 mM EGTA, 2 mM DTT, 0.5 mM phenylmethylsulphonyl fluoride, 20 mM glycerol phosphate, 1 mM sodium vanadate and 1 μg ml⁻¹ leupeptin). Cell lysates were separated by SDS–PAGE and analysed by immunoblotting. For non-reducing gel analysis, cells were lysed in M2 buffer without DTT and separated by SDS–PAGE without β-mercaptoethanol. The dilution ratio of the antibodies used for western blotting is 1:1,000. The proteins were visualized by enhanced chemiluminescence, according to the manufacturer’s (Amersham) instructions.
For immunoprecipitation, lysates were precipitated with antibody (1 μg) and protein G-agarose beads by incubation at 4 °C overnight. Beads were washed four to six times with 1 ml M2 buffer, and the bound proteins were removed by boiling in SDS buffer and resolved in 4–20% SDS–polyacrylamide gels for western blot analysis.
For TRPM7 endogenous immunoprecipitation, crosslinking of cellular proteins was performed before the cell lysis. Cells were washed three times with ice-cold PBS solution and incubated with a crosslinking reagent (DSP, 2 mM) in PBS for 30 min at room temperature, followed by incubation in 10 mM Tris, pH 7.5, buffer for 15 min to quench the reaction. Then, cells were lysed in RIPA buffer containing 0.1% SDS and the samples were used in regular immunoprecipitation procedure as described above. All western data are representative of two or three independent experiments.

Cai Z., Jitkaew S., Zhao J., Chiang H.C., Choksi S., Liu J., Ward Y., Wu L.G, & Liu Z.G. (2013). Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nature cell biology, 16(1), 55-65.

Publication 2013

2-Mercaptoethanol Antibodies Buffers Cells Chemiluminescence Cold Temperature Cross-Linking Reagents Edetic Acid Egtazic Acid G-substrate Glycerophosphates Immunoglobulins Immunoprecipitation leupeptin Phenylmethylsulfonyl Fluoride polyacrylamide gels Proteins Radioimmunoprecipitation Assay SDS-PAGE Sepharose Sodium Chloride Sodium Vanadate Technique, Dilution Tromethamine TRPM7 protein, human Western Blot

Most recents protocols related to «Cross-Linking Reagents»

Crosslinking Decellularized Liver Scaffolds

For crosslinking dECM scaffolds, 50 mL of each crosslinking reagent (PBS; negative control, 0.625% glutaraldehyde, 1 μg/mL, 5 μg/mL and 10 μg/mL of NGOs) was perfused via both bile duct and portal vein of liver scaffolds for 24 h at 4 °C. The crosslinked scaffolds discs (r = 6 mm) were fabricated using skin biopsy punch (P1250, Acuderm Inc., USA). To visualize the distribution of NGOs within the dECM scaffolds and determine the efficiency of NGO incorporation, biotinylated NGOs were perfused into the scaffolds and probed with fluorescent streptavidin. For characterization, lyophilized powers of crosslinked scaffolds were subjected to ATR-FTIR analysis (VERTEX800v, Bruker, USA). Raman spectra of the whole dried scaffold discs were recorded by using 532 nm laser. The weight of scaffold discs was measured before and after drying overnight and the swelling ratio of each scaffold was calculated as below.
Swelling ratio (%) = (W_s – W_d) / W_d X 100 (W_s: Swollen weight, W_d: Dried weight)

Kim D.H., Kim M.J., Kwak S.Y., Jeong J., Choi D., Choi S.W., Ryu J, & Kang K.S. (2023). Bioengineered liver crosslinked with nano-graphene oxide enables efficient liver regeneration via MMP suppression and immunomodulation. Nature Communications, 14, 801.

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Publication 2023

Biopsy Cross-Linking Reagents Duct, Bile Glutaral Skin Spectroscopy, Fourier Transform Infrared Streptavidin Veins, Portal

Cyclic RGD Peptide-Conjugated Nanocarriers

Cyclic RGD peptide-conjugated nanocarriers were prepared to employ sulfo-SMCC and Traut’s Reagent as crosslinking reagents. Briefly, 5 mL of cyclic RGD peptide solution, at a concentration of 1 mg/mL in borate buffer (pH 8, containing 2 mM EDTA), was mixed with 30 μL of Traut’s reagent (2 mg/mL), and the reaction was allowed to proceed for 60 min at room temperature (RT), to prepare cyclic RGD peptide-SH. At the same time, 250 μL of Sulfo-SMCC solution (5 mg/mL, dissolved in PBS) was added to a 5 mL NH₂-SPIO@MSN suspension (10 mg/mL), and the reaction was allowed to proceed for 30 min at RT, to obtain sulfo-SMCC-SPIO@MSN.

Zhao X., Liu C., Wang Z., Zhao Y., Chen X., Tao H., Chen H., Wang X, & Duan S. (2023). Synergistic Pro-Apoptotic Effect of a Cyclic RGD Peptide-Conjugated Magnetic Mesoporous Therapeutic Nanosystem on Hepatocellular Carcinoma HepG2 Cells. Pharmaceutics, 15(1), 276.

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Publication 2023

Borates Buffers Cross-Linking Reagents cyclic arginine-glycine-aspartic acid peptide Cyclic Peptides Edetic Acid ferric oxide Peptides sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate

Immunostaining and Expansion Microscopy

Atto643 (NHS-Atto643, Atto-Tec) was conjugated to goat anti-rabbit IgG (Sigma) in 100 mM NaHCO₃ using 5-fold molar excess of dye for 2 h at RT, purified using Zeba Spin desalting columns with 40 MWCO (Thermo Fisher Scientific) and stored in PBS containing 0.2 % sodium azide. Goat anti-rabbit CF568 (Biotium, 10 µg/ml) and goat anti-mouse Atto643 (custom labeled, 10 µg/ml) were applied to samples in blocking buffer for 2 h at RT. Following washing in PBS (3x, 10 min each), immunostained samples were reacted with crosslinking reagent AcX (Thermo Fisher Scientific) dissolved at a concentration of 1 μg/ml in PBS overnight at RT. After washing away excess AcX (3x, 10 min each, PBS) samples were gelled as previously described^{61 (link),62 (link)}. Briefly, coverslips were flipped on 120 µl proExM monomer solution (8.55% sodium acrylate, 2.5% acrylamide, 0.15% bis-acrylamide, 0.2% ammonium persulfate, 0.2% tetramethylethylenediamine) pipetted on parafilm and gelled in a humidified atmosphere at 37 °C for 2 h. Gels were cut to a SIM card shape for the identification of gel orientation and subjected to digestion with 8 U/ml Proteinase K (Thermo Fisher Scientific) in proExM digestion buffer (50 mM Tris pH 8.0, 1 mM EDTA, 0.5% Triton X-100, 0.8 M guanidine HCl) in a 6-well cell culture chamber (3 ml volume) overnight at RT. Digested gels were expanded to the final size by repeated incubations (5-6 times, 15 min each) in double distilled water. Samples were transferred to imaging chambers coated with Poly-D lysine (Merck, high precision glass bottom, 1.5#). Imaging was performed on a LSM700 laser scanning confocal microscope (Zeiss) using a 63X 1.2 NA water objective, equipped with 561 nm and 640 nm DPSS laser lines. Z-Stacks were corrected for chromatic aberration applying elastic transformations based on images of Tetraspeck beads acquired under the same imaging conditions. Image brightness and contrast were linearly adjusted. Confocal images were acquired with ZEN 12.0.1.362 (Zeiss).

Jobin M.L., Siddig S., Koszegi Z., Lanoiselée Y., Khayenko V., Sungkaworn T., Werner C., Seier K., Misigaiski C., Mantovani G., Sauer M., Maric H.M, & Calebiro D. (2023). Filamin A organizes γ‑aminobutyric acid type B receptors at the plasma membrane. Nature Communications, 14, 34.

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Publication 2023

Acrylamide acrylate ammonium peroxydisulfate anti-IgG Atmosphere Bicarbonate, Sodium Buffers Cell Culture Techniques Cross-Linking Reagents Digestion Edetic Acid Endopeptidase K Gels Goat Guanidine Lysine Microscopy, Confocal Molar Mus Poly A Rabbits Sodium Sodium Azide tetramethylethylenediamine Triton X-100 Tromethamine

Staphylococcal Cell Morphology under APLss

Reference strains of staphylococci, including MSSA 25923 and MRSA 33591 were examined by SEM to determine the effect of APLss on cell morphology and ultrastructure as described previously [30 ]. Briefly, staphylococcal suspensions were incubated with 0.5× and 1× MIC of APLss for 12 h at 37 °C before being collected and resuspended in PBS (pH 7.4). Bacterial cells were first fixed with a mixture of 2.5% glutaraldehyde and 4% paraformaldehyde for 4 h, and then with a cross-linking reagent, 1% osmium tetraoxide, for 1 h. The specimens were then dehydrated with varying ethanol concentrations, critical point dried with carbon dioxide, stacked on a stub, and sputter-coated with gold. The specimens were examined with a JEOL JSM 6400 SEM (JEOL Ltd., Tokyo, Japan).

Yue Y., Chen K., Sun C., Ahmed S, & Ojha S.C. (2023). Antimicrobial peptidase lysostaphin at subinhibitory concentrations modulates staphylococcal adherence, biofilm formation, and toxin production. BMC Microbiology, 23, 311.

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Publication 2023

Bacteria Carbon dioxide Cells Cross-Linking Reagents Ethanol Glutaral Gold Methicillin-Resistant Staphylococcus aureus Osmium Tetroxide paraform Staphylococcus Strains

Nisin Peptide Conjugation on SPEEK-GO Substrate

The necessary quantity (0.5 wt.%) of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC, Sigma Aldrich, St. Louis, MO, USA) was first dissolved in DI water and stirred well. In this work, the nisin A peptide [ITSISLCTPGCKTGALMGCNMKTATCHCSIHVSK] was obtained from Sigma Aldrich and used as received. The nisin peptide (1 wt.%) was separately dissolved in DI water and stirred to obtain a homogeneous solution. Both the EDC and nisin solutions were slowly mixed together and continuously stirred for 40 min at ambient temperature. The SPEEK-GO plate was soaked in the nisin/EDC solution and kept in a dark atmosphere for 48 h at room temperature. Through amide linkage, the nisin peptide was conjugated to the GO using the coupling chemistry between the –NH₂ group of the nisin and the –CO₂H group of GO via the cross-linking reagent of EDC [32 (link)]. The SPEEK-GO-nisin was softly taken out of the nisin solution and washed with DI water to remove the residual reagents. The SPEEK-GO-nisin was then dried overnight at 40 °C in a vacuum oven. The sample was stored in a dark atmosphere at room temperature for further experiments. The nisin conjugation on a three-dimensional porous SPEEK-GO sample from a pure PEEK substrate is shown in the schematic illustration (Figure 8).

Kumar S.R., Hu C.C., Vi T.T., Chen D.W, & Lue S.J. (2023). Antimicrobial Peptide Conjugated on Graphene Oxide-Containing Sulfonated Polyetheretherketone Substrate for Effective Antibacterial Activities against Staphylococcus aureus. Antibiotics, 12(9), 1407.

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Publication 2023

Amides Atmosphere Carbodiimides Cross-Linking Reagents nisin A Peptides polyetheretherketone Vacuum

Top products related to «Cross-Linking Reagents»

Bs3 cross linking reagent by Thermo Fisher Scientific

Sourced in United States

The BS3 cross-linking reagent is a homobifunctional N-hydroxysuccinimide (NHS) ester that can be used to covalently link primary amine groups. It is a versatile tool for the study of protein-protein interactions, protein complex formation, and protein structure.

Dynabeads protein g by Thermo Fisher Scientific

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

Dynabeads Protein G is a magnetic bead-based product used for the purification and isolation of immunoglobulins (Ig) and other proteins that bind to Protein G. It provides a reliable and efficient method for the capture and separation of target proteins from complex samples.

Dynabead by Thermo Fisher Scientific

Sourced in United States, Norway, Germany, United Kingdom, France, China, Japan, Switzerland, Belgium, Canada, Italy, Australia

Dynabeads are magnetic beads used in various laboratory applications. They are designed to efficiently capture and isolate target molecules, such as proteins, nucleic acids, or cells, from complex samples. The magnetic properties of Dynabeads allow for easy separation and manipulation of the captured targets.

4 6 diamidino 2 phenylindole (dapi) by Thermo Fisher Scientific

Sourced in United States, Germany, United Kingdom, Japan, China, Canada, Italy, Australia, France, Switzerland, Spain, Belgium, Denmark, Panama, Poland, Singapore, Austria, Morocco, Netherlands, Sweden, Argentina, India, Finland, Pakistan, Cameroon, New Zealand

DAPI is a fluorescent dye used in microscopy and flow cytometry to stain cell nuclei. It binds strongly to the minor groove of double-stranded DNA, emitting blue fluorescence when excited by ultraviolet light.

Cplaygtw by Proteintech

CPLAYGTW is a lab equipment product offered by Proteintech. It serves as a tool for researchers and scientists in their laboratory work. The core function of this product is to facilitate specific tasks within the laboratory setting.

Recombinant cd59 by R&D Systems

Recombinant CD59 is a purified protein produced in a mammalian cell expression system. CD59 is a glycosylphosphatidylinositol (GPI)-anchored membrane protein that inhibits the formation of the membrane attack complex (MAC) of the complement system.

Protease inhibitor cocktail by Roche

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

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.

Bis sulfosuccinimidyl suberate bs3 by Thermo Fisher Scientific

Sourced in United States

Bis(sulfosuccinimidyl)suberate (BS3) is a water-soluble, homobifunctional N-hydroxysulfosuccinimide (NHS) ester cross-linker. It is used for the covalent attachment of primary amino groups in proteins and other biomolecules.

N ethylmaleimide nem by Merck Group

Sourced in United States, China, Italy

N-ethylmaleimide (NEM) is a chemical compound commonly used as a laboratory reagent. It is a colorless crystalline solid that is soluble in organic solvents. NEM is primarily used as a blocking agent for sulfhydryl groups in proteins, which can aid in the study of protein structure and function.

What are the different types of cross-linking reagents available?

Cross-linking reagents come in a variety of types, each with unique properties and applications. Some common categories include homobifunctional, heterobifunctional, and zero-length cross-linkers. Homobifunctional reagents have the same reactive groups on both ends, while heterobifunctional reagents have different reactive groups, allowing for more targeted and controlled cross-linking. Zero-length cross-linkers directly link two molecules without introducing any additional spacer. The choice of cross-linking reagent depends on the specific research goals and the nature of the molecules being studied.

How can I ensure the optimal use of cross-linking reagents in my experiments?

Effective use of cross-linking reagents requires careful consideration of factors like reaction time, temperature, pH, and reagent concentration. It's important to optimize these parameters to achieve the desired level of cross-linking without over-fixation or unintended side effects. Thier, it's also crucial to quench the reaction at the appropriate time to stop the cross-linking process. PubCompare.ai can help by providing access to a wealth of literature on protocol optimization, allowing you to learn from the experiences of other researchers and fine-tune your own experiments for maximum efficiency and reproducibility.

What are some common applications of cross-linking reagents in biological research?

Cross-linking reagents have a wide range of applications in biological research, including the study of protein-protein interactions, protein-nucleic acid interactions, and the identification of protein complexes. They can be used to capture transient or weak associations, enabling researchers to gain insights into molecular organization and function. Cross-linking is also valuable for structural biology studies, as it can provide information about the spatial arrangement of biomolecules within a complex. By leveraging the power of PubCompare.ai, scientists can easily identify the most effective cross-linking protocols and products for their specific research needs, streamlining the discovery process and leading to more accurate and reproducible results.

How can PubCompare.ai assist in the comparison and selection of cross-linking reagents?

PubCompare.ai is a powerful AI-driven platform that can revolutionize your cross-linking research. By efforlessly screening protocol literature from published papers, preprints, and patents, the platform can help you identify the most effective cross-linking reagents and protocols for your specific research goals. Its AI-powered analysis can highlight key differences in protocol effectiveness, enabling you to make informed decisions and choose the best option for reproducibility and accuracy. With PubCompare.ai, you can streamline your research process and unlock new biological insights by leveraging the power of AI-driven comparisons of cross-linking reagents and protocols.

More about "Cross-Linking Reagents"

Cross-linking reagents are powerful tools used in a variety of scientific research applications, from studying protein-protein interactions to unraveling the secrets of molecular structures.
These chemical agents, also known as bifunctional or multifunctional reagents, are designed to form stable covalent bonds between specific amino acid residues, enabling researchers to capture even transient or weak associations.
One of the most widely used cross-linking reagents is BS3 (Bis(sulfosuccinimidyl)suberate), which can effectively link primary amines, such as those found in lysine residues.
Other common cross-linking agents include N-ethylmaleimide (NEM), which targets sulfhydryl groups, and DAPI, which binds to DNA.
The choice of cross-linking reagent often depends on the specific research question and the nature of the biomolecules under investigation.
Dynabeads, a type of magnetic bead coated with proteins like Protein G, are frequently used in conjunction with cross-linking reagents to isolate and purify protein complexes.
These beads provide a convenient way to capture and study transient interactions, as well as to identify novel binding partners.
In addition to protein-protein interactions, cross-linking reagents can also be used to study protein-DNA and protein-RNA interactions, as well with recombinant proteins like Recombinant CD59.
The CPLAYGTW motif, for example, has been identified as a potential cross-linking site for some proteins.
To ensure the success of cross-linking experiments, researchers often employ a variety of other reagents and tools, such as protease inhibitor cocktails to prevent protein degradation, and bovine serum albumin (BSA) to block non-specific binding.
By leveraging the power of AI-driven comparisons, the PubCompare.ai platform empowers scientists to effortlessly locate relevant protocols and identify the best cross-linking reagents and products for their specific research needs.
This streamlined approach helps to accelerate the discovery process and enables more informed decision-making, ultimately unlocking new biological insights.