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Dimethyl pimelimidate

Dimethyl pimelimidate is a chemical compound used in various research applications.
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Most cited protocols related to «Dimethyl pimelimidate»

Purification and Characterization of HLA Complexes

Cited 13 times

For the preparation of the affinity columns, panHLA-I and panHLA-II antibodies were purified from HB95 cells and HB145 cells (ATCC, Manassas, VA), respectively. We cross-linked the antibodies to Protein-A Sepharose beads (Invitrogen, CA) with 20 mM dimethyl pimelimidate in 0.2 M sodium borate buffer pH9. Tumour amount that has been available for this research varied significantly, from about 0.1 g to 4 × 1 g in Mel15. For the purification of HLA complexes, snap-frozen melanoma tissue samples were homogenized for 10 s on ice using ULTRA-TURRAX (IKA, Staufen, Germany) in a tube containing 5–10 ml of lysis buffer and incubated at 4 °C for 1 h. The lysis buffer contained 0.25% sodium deoxycholate, 0.2 mM iodoacetamide, 1 mM EDTA, 1:200 Protease Inhibitors Cocktail (Sigma-Aldrich, MO), 1 mM PMSF, 1% octyl-β-D glucopyranoside (Sigma-Aldrich, MO) in PBS. The lysates were cleared by 20 min centrifugation at 40,000g. Lysates were passed through a column containing Protein-A Sepharose beads (Invitrogen, CA) to deplete the endogenous antibodies. Subsequently, HLA-I molecules were immunoaffinity purified from cleared lysate with the W6/32 antibody covalently bound to Protein-A Sepharose beads (Invitrogen, Camarillo, CA). HLA-II molecules were then purified by transferring the flow through onto similar affinity columns containing the HB-145 antibody. Affinity columns were washed first with 10 column volumes of 150 mM NaCl, 20 mM Tris–HCl (buffer A), 10 column volumes of 400 mM NaCl, 20 mM Tris–HCl, 10 volumes of buffer A again, and finally with seven column volumes of 20 mM Tris–HCl, pH 8.0. HLA molecules were eluted at room temperature by adding 500 μl of 0.1 N acetic acid, in total seven elutions for each sample25 .
Eluted HLA peptides and the subunits of the HLA complexes were loaded on Sep-Pak tC18 (Waters, MA) cartridges that were prewashed with 80% acetonitrile (ACN) in 0.1% trifluoracetic acid (TFA) and with 0.1% TFA. The peptides were separated from the much more hydrophobic HLA heavy chains and B2M on the C18 cartridges by eluting them with 30% CAN in 0.1% TFA. They were further purified using a Silica C-18 column tips (Harvard Apparatus, Holliston MA) and eluted again with 30% ACN in 0.1% TFA. The peptides were concentrated and the volume was reduced to 15 μl using vacuum centrifugation. Remaining immunoaffinity purified HLA heavy chains and the B2M molecules were eluted from the Sep-Pak tC18 cartridges with 80% ACN in 0.1%TFA. For western-blot detection, 1% of each of those protein containing samples were used. Anti human B2M antibody EP2978Y (1:5,000, Abcam, Cambridge, United Kingdom) was used and was detected with donkey anti-rabbit IgG HRP conjugate secondary antibody (1:5,000, Thermo Fisher Scientific) in a peroxidase assay using SuperSignal West Pico Chemiluminescent substrate (Thermo Fisher Scientific).

Bassani-Sternberg M., Bräunlein E., Klar R., Engleitner T., Sinitcyn P., Audehm S., Straub M., Weber J., Slotta-Huspenina J., Specht K., Martignoni M.E., Werner A., Hein R., H. Busch D., Peschel C., Rad R., Cox J., Mann M, & Krackhardt A.M. (2016). Direct identification of clinically relevant neoepitopes presented on native human melanoma tissue by mass spectrometry. Nature Communications, 7, 13404.

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Publication 2016

Acetic Acid acetonitrile Acids anti-IgG Antibodies Antibodies, Anti-Idiotypic Biological Assay Buffers Cells Centrifugation Deoxycholic Acid, Monosodium Salt dimethyl pimelimidate Edetic Acid Equus asinus Freezing Homo sapiens Immunoglobulins Iodoacetamide Melanoma Neoplasms Peptides Peroxidase Protease Inhibitors Proteins Protein Subunits Rabbits Silicon Dioxide sodium borate Sodium Chloride Staphylococcal protein A-sepharose Tissues Tromethamine Vacuum Western Blotting

Immunoprecipitation and Ubiquitination Assays for Cap-H2 and Plk4

Cited 7 times

Polyclonal anti-Slimb antibody was bound to equilibrated Protein A–coupled Sepharose (Sigma-Aldrich) by gently rocking overnight at 4°C in 0.2 M sodium borate. For GFP immunoprecipitations, GFP-binding protein (GBP; Rothbauer et al., 2008 (link)) was fused to the Fc domain of human IgG (pIg-Tail; R&D Systems), tagged with His₆ in pET28a (EMD Millipore), expressed in E. coli, and purified on Talon resin (Takara Bio Inc.) according to manufacturer’s instructions. GBP was bound to Protein A–coupled Sepharose, cross-linked to the resin using dimethyl pimelimidate, and rocked for 1 h at 22°C; the coupling reaction was then quenched in 0.2 M ethanolamine, pH 8.0, and rocked for 2 h at 22°C. Antibody or GBP-coated beads were washed three times with 1.5 ml of cell lysis buffer (CLB; 100 mM Tris, pH 7.2, 125 mM NaCl, 1 mM DTT, 0.1% Triton X-100, and 0.1 mM PMSF). Transfected S2 cells were induced to express recombinant Cap-H2 with 1–2 mM CuSO₄. After 24 h, transfected cells were lysed in CLB, clarified by centrifugation, and then diluted to 2–5 mg/ml in CLB. Antibody-coated beads were mixed with lysate for 40 min at 4°C, washed three times with CLB, and then boiled in Laemmli sample buffer. Lambda phosphatase (New England Biolabs, Inc.) treatments were performed for 1 h at 37°C. In vivo ubiquitination assays were performed by coexpressing Plk4-GFP (Rogers et al., 2009 (link)) or Cap-H2-GFP constructs with 3×FLAG–tagged Drosophila ubiquitin (CG32744), driven under the inducible metallothionein promoter pMT vector, immunoprecipitated using anti-GFP JL8 antibody, and analyzed by anti-FLAG immunoblotting.

Buster D.W., Daniel S.G., Nguyen H.Q., Windler S.L., Skwarek L.C., Peterson M., Roberts M., Meserve J.H., Hartl T., Klebba J.E., Bilder D., Bosco G, & Rogers G.C. (2013). SCFSlimb ubiquitin ligase suppresses condensin II–mediated nuclear reorganization by degrading Cap-H2. The Journal of Cell Biology, 201(1), 49-63.

Publication 2013

Antibodies, Anti-Idiotypic Binding Proteins Biological Assay Buffers Cells Centrifugation Claw Cloning Vectors dimethyl pimelimidate Drosophila Escherichia coli Ethanolamine Homo sapiens Immunoglobulins Immunoprecipitation Laemmli buffer Metallothionein Phosphoric Monoester Hydrolases Resins, Plant sodium borate Sodium Chloride Staphylococcal protein A-sepharose Tail TRAF3 protein, human Triton X-100 Tromethamine Ubiquitin Ubiquitination

Western Blot Analysis of Retinal RIBEYE

Cited 5 times

For Western blots of retina homogenate, retinae were homogenized, total protein was precipitated with TCA, dissolved in sample buffer, separated on 3.5–8% Tris acetate gels (25 μg/lane), and transferred to PVDF membranes by tank blotting (Altrock et al., 2003 (link)). For immunodetection, membranes were blocked and primary antibodies were applied overnight at 4°C. For characterization of the RIBEYE antiserum, 5 μl RIBEYE serum was preincubated for 1 h with an excess of purified MBP-RIB (aa 179–448) fraction or with buffer alone and then diluted for overnight incubation of the Western blots. The HRP-coupled secondary antibodies were visualized by chemiluminescent detection (Amersham Biosciences).
Blots were reprobed several times with different antibodies. Evaluation of relative amounts of RIBEYE immunoreactivity was performed by determining gray values in nonsaturated expositions of X-ray films in a given area using Adobe Photoshop for four individual +/+ and −/− animal pairs. The mean value of the +/+ animals was defined as 100%.
For immunoprecipitation experiments, retinae were homogenized in 1 ml extraction buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1% Triton X-100, and 0.5% sodium deoxycholate) per animal. Insoluble material was pelleted. For antibody immobilization, protein G–Agarose beads (25 μl bed volume; Roche) were incubated overhead (for 1 h at 4°C) with 10 μg monoclonal Bassoon antibody and as control 10 μg mouse IgG (Sigma-Aldrich), or with 5 μl rabbit anti-BSN1.6 antiserum and 5 μl of a preimmune serum as control followed by washes. The extract corresponding to one retina was applied overnight to the antibody-coupled beads. Bound proteins were recovered after extensive washes in homogenization buffer by boiling in sample buffer. Extracted material (input) and unbound proteins in the supernatant were concentrated by TCA precipitation. SDS-PAGE and immunodetection were performed as described above.
For immunoprecipitation experiments from brain material, synaptosomal fractions were prepared as described previously (Phillips et al., 2001 (link)) and were extracted with detergent buffer (0.5% sodium deoxycholate, 0.1% Triton X-100, 70 mM NaCl, 25 mM Tris-HCL, pH 8.0, and total protein 0.125 μg/μl). Mouse anti-Bassoon mAb and unspecific mouse IgG (Santa Cruz Biotechnology. Inc.) were chemically coupled to GammaBind Plus Sepharose (Amersham Biosciences) to abolish background derived from antibody proteins in the immunoprecipitation fraction. In detail, 20 μg IgG was incubated for 1 h with 100 μl of beads in PBS-T buffer (8.1 mM Na₂HPO₄, 1.5 mM KH₂PO₄, 2.7 mM KCl, 137 mM NaCl, and 0.1% Tween 20, pH 7.4). Beads were washed with PBS-T and with TEA buffer (0.2 M triethanolamine, pH 8.2) before incubation for 45 min at RT in coupling buffer (20 mM dimethyl pimelimidate dihydrochlorid in TEA). Beads were washed with TEA and incubated for 10 min at RT in 20 mM ethanolamine (pH 8.2). After washing with PBS-T, beads were stored in 5% BSA in PBS-T with 0.025% NaN₃ at 4°C.
For immunoprecipitation, 10 μl of antibody-coated beads washed in extraction buffer were incubated for 1 h at 4°C with 500 μl synaptosomal extract. After washing, bound proteins were eluted with sample buffer without reducing agent for 5 min at 60°C. The eluate was incubated for 5 min at 90°C in the presence of 50 mM dithiothreitol as a reducing agent. SDS-PAGE and immunodetection were performed as described above.

tom Dieck S., Altrock W.D., Kessels M.M., Qualmann B., Regus H., Brauner D., Fejtová A., Bracko O., Gundelfinger E.D, & Brandstätter J.H. (2005). Molecular dissection of the photoreceptor ribbon synapse: physical interaction of Bassoon and RIBEYE is essential for the assembly of the ribbon complex. The Journal of Cell Biology, 168(5), 825-836.

Publication 2005

Immunoprecipitation of TgAMA1 from Toxoplasma Lysates

Cited 4 times

The mAbs specific for TgAMA1 were CL22 [18 (link)] and B3.90 [19 (link)]. For immunoprecipitation of TgAMA1, these monoclonal antibodies were bound and coupled using dimethyl pimelimidate to fastflow Protein G sepharose (Amersham Biosciences, Little Chalfont, United Kingdom) [59 ].
Tachyzoite lysates were generated by extracting 5 × 10⁹ extracellular parasites in 10 ml of TEN buffer (50 mM Tris [pH 8.0], 5 mM EDTA, 150 mM NaCl) containing RIPA detergents [1% NP40, 0.5% Deoxycholate, 0.01% SDS, and Complete protease inhibitor, (Roche Diagnostics, Mannheim, Germany)] on ice for 30 min and removing insoluble material by centrifugation at 3,000 × g for 20 min.
These extracts were incubated with the indicated antibodies coupled to protein G sepharose for 4 hr at 4 °C, followed by three washes (15-min each) in RIPA buffer and three washes in Tris-buffered saline (TBS; 50 mM Tris [pH 8.0], 150 mM NaCl). Bound polypeptides were eluted with 0.1 M triethylamine [pH 11.5] (using five successive elutions), and lyophilized to concentrate the eluate and remove the triethylamine. The 10⁶ parasite equivalents were fractionated by SDS-PAGE for immunoblot analysis, or, similarly, 10⁸ parasites for Coomassie brilliant blue staining.

Alexander D.L., Mital J., Ward G.E., Bradley P, & Boothroyd J.C. (2005). Identification of the Moving Junction Complex of Toxoplasma gondii: A Collaboration between Distinct Secretory Organelles. PLoS Pathogens, 1(2), e17.

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Publication 2005

Antibodies brilliant blue G Buffers Centrifugation Deoxycholate Detergents Diagnosis dimethyl pimelimidate Edetic Acid G-substrate Immunoblotting Immunoprecipitation Monoclonal Antibodies Parasites Polypeptides Protease Inhibitors Radioimmunoprecipitation Assay Saline Solution SDS-PAGE Sepharose Sodium Chloride triethylamine Tromethamine

Antibody-mediated Identification of L5 Interactors

Cited 4 times

500 µg of wild type procyclic nuclear extract was used for each IC sample. An affinity-purified antibody against the L5 peptide ²⁹⁶VAAVIERIRDRAK³⁰⁸ (Bethyl Laboratories) was used. Dynabeads (Invitrogen) were cross-linked to anti-L5 antibody using dimethyl pimelimidate (DMP, Thermo Scientific) following the manufacturer’s instructions. As a negative control, no antibody was added to one reaction to assess the degree of non-specific interactions with the Dynabeads. Nuclear extracts were added to the Dynabeads coated with antibody and incubated overnight at 4°C. Supernatants (S) were collected and the beads were washed five times with phosphate-buffered saline (PBS). The Dynabeads were then resuspended in SDS-PAGE sample buffer and boiled for five minutes to dissociate interacting proteins. Finally, samples were subjected to denaturing gel electrophoresis. To detect the presence of P34 and P37 in association with L5, the proteins were transferred to a nitrocellulose membrane. The membrane was blocked with 10% non-fat milk and incubated with an anti-P34/P37 affinity purified, polyclonal antibody previously described [10] (link). A secondary goat anti-rabbit antibody conjugated to horseradish peroxidase (HRP) was used for detection in conjunction with the SuperSignal West Pico Chemiluminiscent Substrate (Thermo Scientific). These experiments were repeated three times and representative results are shown.
For the IC with recombinant proteins, 100 ng of recombinant L5 were incubated with 100 ng of recombinant P34 or P37 in the absence or presence of stoichiometric amounts of in vitro-transcribed 5S rRNA and immunoprecipitated with Dynabeads cross-linked to the L5 peptide antibody as indicated above. The experiments were repeated a minimum of three times with different preparations of recombinant proteins and synthetic 5S rRNAs.

Ciganda M., Prohaska K., Hellman K, & Williams N. (2012). A Novel Association between Two Trypanosome-Specific Factors and the Conserved L5-5S rRNA Complex. PLoS ONE, 7(7), e41398.

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Publication 2012

Antibodies, Anti-Idiotypic Antibody Affinity Buffers dimethyl pimelimidate Electrophoresis Goat Horseradish Peroxidase Immunoglobulins Milk, Cow's Nitrocellulose Peptides Phosphates Proteins Rabbits Recombinant Proteins RNA, Ribosomal, 5S Saline Solution SDS-PAGE Tissue, Membrane

Most recents protocols related to «Dimethyl pimelimidate»

Navitoclax-Induced Protein Interactome

Cells were treated with 2500nM navitoclax or solvent control (DMSO) for 6h. Immunoprecipitation (IP) was performed with Dynabeads Protein G Immunoprecipitation Kit (Invitrogen, 10007D) according to manufacturer’s instructions, antibodies were crosslinked to the beads with dimethyl pimelimidate solution (20mM) in triethanolamine buffer (0.2M). For antibodies see Suppl. Table 3.

Zeuner S., Vollmer J., Sigaud R., Oppermann S., Peterziel H., ElHarouni D., Oehme I., Witt O., Milde T, & Ecker J. (2024). Combination drug screen identifies synergistic drug interaction of BCL-XL and class I histone deacetylase inhibitors in MYC-amplified medulloblastoma cells. Journal of Neuro-Oncology, 166(1), 99-112.

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Publication 2024

In Vitro Protein Cross-Linking with DMP

In vitro cross-linking
using the bifunctional cross-linking reagent dimethyl pimelimidate
(DMP) was performed, as previously described.^{6 (link)} Briefly, 30 μL of proteins reconstituted into SUVs were incubated
with 1.8 μL of decanoic acid (332 mM) and 18 μL of freshly
prepared DMP in phosphate buffer saline (pH = 7.4, 150 mM) for 2 h
at room temperature to ensure partitioning of C10 to the bilayer.
The cross-linking reaction was terminated with 15 μL of stop
solution (50 mM Tris-HCl, 1 M glycine, 150 mM NaCl, pH = 8.3).

Gentile R., Modric M., Thiele B., Jaeger K.E., Kovacic F., Schott-Verdugo S, & Gohlke H. (2024). Molecular Mechanisms Underlying Medium-Chain Free Fatty Acid-Regulated Activity of the Phospholipase PlaF from Pseudomonas aeruginosa. JACS Au, 4(3), 958-973.

Publication 2024

Isotopic Labeling and Immunoprecipitation Mass Spectrometry

All reagents and solvents were liquid chromatography (LC)/mass spectrometry (MS)-grade quality unless otherwise noted. [¹³C₆]-leucine was obtained from Cambridge Isotope Laboratories (Andover, MA). Anti-FXN recombinant rabbit monoclonal antibody (mAb) EPR21840 (cat. # ab219414) was from Abcam (Cambridge, UK). Ethylenediaminetetraacetic acid (EDTA)-free protease inhibitor cocktail, DL-dithiothreitol (DTT), EDTA-free Easypack protease inhibitor cocktail tablets, and dimethyl pimelimidate dihydrochloride (DMP) were purchased from MilliporeSigma (Billerica, MA). LC-grade water and acetonitrile were obtained from Burdick and Jackson (Muskegon, MI). Protein G Dynabeads for immunoprecipitation (IP) and radioimmunoprecipitation assay (RIPA) lysis buffer with EDTA were from ThermoFisher Scientific (Waltham, MA). LC/MS grade water and Optima LC/MS grade solvents were from Fisher Scientific (Pittsburgh, PA).

Rojsajjakul T., Selvan N., De B., Rosenberg J.B., Kaminsky S.M., Sondhi D., Janki P., Crystal R.G., Mesaros C., Khanna R, & Blair I.A. (2024). Expression and processing of mature human frataxin after gene therapy in mice. Scientific Reports, 14, 8391.

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Publication 2024

Co-immunoprecipitation and Protein Detection

We performed co-immunoprecipitation using Pierce Anti-HA Magnetic Beads (Life Technologies) or using Dynabeads-protein G (Thermo) magnetic beads with primary antibodies (anti-GFP Genetex No#GTX113717; anti-Sec5 Proteintech No#12751-1-AP) cross-linked using dimethyl pimelimidate (Life Technologies).
For the production of whole-cell lysates, cells were lysed at 4 °C in lysis buffer (50 mM Tris at pH 7.4, 1% NP-40 [v/v], 150 mM NaCl, 0.25% sodium deoxycholate [v/v], protease inhibitor cocktail [1× EDTA-free protease inhibitors, Sigma], 10 mM NaF). 1/10 part of the clarified lysate was saved as an input fraction, and the rest was subjected to immunoprecipitation.
After adding beads, binding of the protein of interest was performed overnight with gentle rotation at 4 °C. The next day, beads were washed 4 × 10 min at 4 °C in the same lysis buffer to remove unbound proteins, and complexes were eluted off the beads using 2x SDS sample buffer at 37C for 30min. We analyzed the composition of eluent using the SDS-PAGE and Western Blot method.

Niedziółka S.M., Datta S., Uśpieński T., Baran B., Skarżyńska W., Humke E.W., Rohatgi R, & Niewiadomski P. (2024). The exocyst complex and intracellular vesicles mediate soluble protein trafficking to the primary cilium. Communications Biology, 7, 213.

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Publication 2024

Mitochondrial Protein Interactions by Cross-link IP

Not available on PMC !

For cross-link immunoprecipitation, mitochondria enriched heavy membrane fractions (200 μg) from control fibroblasts were chemically cross-linked with 1 mM dithiobis-sulfosuccinimidyl propionate (DSP) (Sigma) in HIM buffer, for 2 h on ice. The reaction was stopped by adding glycine pH 8.0 at 70 mM final concentration for 10 min on ice. Mitochondria were pelleted, rinsed once, and extracted in 200 μl of lysis buffer (10 mM Tris-HCl pH 7.5, 150 mM NaCl, 1% n-dodecyl-D-maltoside (DDM) (Sigma), and complete protease inhibitors (Roche)) on ice for 30 min. The extract was centrifuged at 20,000g at 4°C for 20 min, and the supernatant was precleared overnight with non-coated Dynabeads Protein A (Invitrogen) to reduce non-specific protein binding to the beads. Binding of indicated antibodies to Dynabeads Protein A (Invitrogen) was performed overnight. Antibodies were then cross-linked to the beads using 20 mM dimethyl pimelimidate (DMP) (Sigma). The immunoprecipitation reaction was performed overnight at 4°C. Beads were washed with lysis buffer and samples were eluted using 0.1 M glycine pH 2.5/0.5% DDM, precipitated with trichloroacetic acid and analyzed by mass spectrometry at the IRCM (Institut de Recherches cliniques de Montreal).

Schuettpelz J., Watt K., Antonická H., Janer A., Larsson O., & Shoubridge E.A. (2024). SLC25A46 is in contact with lysosomes and plays a role in mitochondrial cholesterol homeostasis.

Publication 2024

Top products related to «Dimethyl pimelimidate»

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Dimethyl pimelimidate is a chemical compound used as a lab equipment product. It functions as a cross-linking agent for proteins and other biomolecules.

Dynabeads protein g by Thermo Fisher Scientific

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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.

Dimethyl pimelimidate by Thermo Fisher Scientific

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Dimethyl pimelimidate is a chemical reagent used for cross-linking proteins in biochemical and molecular biology applications. It is a bifunctional imidoester that forms covalent bonds between primary amine groups, facilitating the study of protein-protein interactions and structural analysis.

Protein g dynabead by Thermo Fisher Scientific

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Protein G Dynabeads are magnetic beads coated with recombinant Protein G. Protein G is a bacterial cell wall protein that binds to the Fc region of immunoglobulins. These beads can be used for the rapid and efficient purification of antibodies from various samples.

Dimethyl pimelimidate dihydrochloride by Merck Group

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Dimethyl pimelimidate dihydrochloride is a chemical compound used in biochemistry and molecular biology applications. It is a cross-linking agent that can be used to covalently link proteins or other biomolecules. The compound's core function is to facilitate the formation of stable chemical bonds between target molecules.

Dimethyl pimelimidate dihydrochloride dmp by Merck Group

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Dimethyl pimelimidate dihydrochloride (DMP) is a chemical crosslinking agent used in various laboratory applications. It is a water-soluble, amine-reactive compound that can form stable covalent bonds between primary amines. DMP is commonly used for the immobilization, stabilization, or conjugation of proteins, peptides, or other biomolecules in biochemical and analytical procedures.

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Protein G agarose beads are a type of affinity chromatography resin used for the purification of immunoglobulins (antibodies) from biological samples. The beads consist of Protein G, a bacterial protein with a high affinity for the Fc region of various immunoglobulin classes, immobilized on an agarose matrix. The core function of Protein G agarose beads is to selectively bind and capture immunoglobulins, allowing for their separation and purification from complex mixtures such as cell culture supernatants or serum.

Protein a sepharose beads by GE Healthcare

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Protein A-Sepharose beads are a widely used chromatographic resin primarily used for the purification and isolation of immunoglobulins and other proteins that bind to Protein A. The beads consist of Sepharose, a cross-linked agarose-based matrix, with Protein A covalently immobilized on the surface.

What is Dimethyl pimelimidate and how is it used in research?

Dimethyl pimelimidate is a chemical compound that has various applications in research. It is commonly used as a cross-linking agent, helping to create stable bonds between different molecules or proteins. This makes it valuable for techniques like Western blotting, protein purification, and cell surface labeling. Researchers often use Dimethyl pimelimidate to study protein-protein interactions and protein complex formation.

What are some common challenges in working with Dimethyl pimelimidate?

One of the main challenges with Dimethyl pimelimidate is ensuring optimal reaction conditions. The cross-linking process is sensitive to factors like pH, temperature, and incubation time. Improper conditions can lead to inconsistent results or even damage the target proteins. Additionaly, Dimethyl pimemlimidate has a relatively short shelf-life and requires careful storage to maintain its effectiveness.

Are there different variations or types of Dimethyl pimelimidate?

Yes, there are a few different variants of Dimethyl pimelimidate that researchers may encounter. The most common form is the dihydrochloride salt, but water-soluble versions like the di-N-hydroxysuccinimide ester also exist. These alternatives can have slightly different reactivity profiles and may be preferable for certain applications. It's important to carefully select the right Dimethyl pimelimidate variant to match your experimental needs.

How can PubCompare.ai help optimize the use of Dimethyl pimelimidate?

PubCompare.ai is an invaluable tool for researchers working with Dimethyl pimelimidate. The platform allows you to efficiently screen the protocol literrature to identify the most effective uses of this cross-linking agent. Its AI-driven analysis can highlight key differences between protocols, such as optimal reaction conditions, sample preparation steps, and downstream analytical techniques. This helps you choose the protocol that will provide the most reproducible and accurate results for your specific research goals involving Dimethyl pimelimidate.

More about "Dimethyl pimelimidate"

Dimethyl pimelimidate (DMP) is a versatile chemical compound used in various research applications.
It is commonly employed as a crosslinking agent, facilitating the covalent attachment of proteins or other biomolecules to solid supports such as Dynabeads Protein G, Protein G Dynabeads, or Protein G agarose beads.
This process is often used for the purification and immobilization of proteins, including antibodies.
DMP can also be used in conjunction with other reagents like ethanolamine and Benzonase to help remove unwanted proteins, nucleic acids, and other contaminants from samples.
The dimethyl pimelimidate dihydrochloride (DMP) form of the compound is particularly useful in these applications.
The PubCompare.ai platform is an AI-driven tool that allows researchers to efficiently locate and compare protocols from the literature, preprints, and patents related to the use of dimethyl pimelimidate and related techniques.
By utilizing intelligent comparison algorithms, PubCompare.ai can help identify the most effective protocols and products, streamlining the research process and leading to better results.
Whether you're working with dimethyl pimelimidate, Dynabeads Protein G, Protein G Dynabeads, or other related reagents and techniques, PubCompare.ai can be a valuable resource in optimizing your research and achieving your desired outcomes.