Rink amide resin

Manufactured by AnaSpec

Sourced in United States

Rink amide resin is a solid-phase synthesis resin used for the preparation of peptides. It is a polystyrene-based resin functionalized with a Rink linker, which enables the synthesis of C-terminal amide-protected peptides.

Automatically generated - may contain errors

Lab products found in correlation

Fmoc protected amino acids, by AnaSpec (1 mentions) Cbm 20a, by Shimadzu (1 mentions) Sciex 5800 maldi tof tof mass spectrometer, by AB Sciex (1 mentions) Jupiter 250, by Phenomenex (1 mentions) Orbitrap velos, by Thermo Fisher Scientific (1 mentions) Restriction endonuclease, by New England Biolabs (1 mentions) Du 640 spectrophotometer, by Beckman Coulter (1 mentions) Recombinant human histones, by New England Biolabs (1 mentions) 4800 maldi tof tof mass spectrometer, by Thermo Fisher Scientific (1 mentions) Oligonucleotide primers, by Integrated DNA Technologies (1 mentions) 5800 maldi tof tof mass spectrometer, by AB Sciex (1 mentions) Fmoc amino acids, by AnaSpec (1 mentions)

6 protocols using rink amide resin

Synthesis of Fmoc-Protected Peptide F6C11

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

All Fmoc-protected
amino acids,
Rink Amide resin, and 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium
hexafluorophosphate were purchased from Anaspec, Inc. The peptide
F6C11 was prepared according to our previous paper.^{45 (link)} All the other reagents were used as received.

Lin Y., Penna M., Thomas M.R., Wojciechowski J.P., Leonardo V., Wang Y., Pashuck E.T., Yarovsky I, & Stevens M.M. (2019). Residue-Specific Solvation-Directed Thermodynamic and Kinetic Control over Peptide Self-Assembly with 1D/2D Structure Selection. ACS Nano, 13(2), 1900-1909.

+ Open protocol

+ Expand

Synthesis and Characterization of C16GSH Peptide Amphiphiles

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

The GSH peptide was purchased fully protected on rink amide resin (China Tech Peptides Co., Suzhou, China) or synthesized on rink amide resin (Anaspec, Fremont, CA) using an automated PS3 Benchtop Peptide Synthesizer (Protein Technologies, Tucson, AZ). Fatty acid tails were conjugated to the lysine residue of the peptide as described previously³⁵ to create C₁₆GSH PAs (Fig. 1). The synthesis products were precipitated in diethyl ether and purified to above 90% purity on a Shimadzu CBM-20A high-performance liquid chromatography (HPLC) system in reverse phase, employing a Waters Symmetry 300 semipreparative C8 column. Product identity was confirmed by mass spectrometry, employing an Applied Biosystems 4700 Proteomics Analyzer, and purity was determined using analytical HPLC with a Waters Symmetry 300 analytical column. Exact concentrations were determined by UV spectroscopy,^{38 (link)} and it was determined that the peptides accounted for 60% of the measured mass of peptide salts. This correction was taken into account when considering molarity.

Black K.A., Lin B.F., Wonder E.A., Desai S.S., Chung E.J., Ulery B.D., Katari R.S, & Tirrell M.V. (2015). Biocompatibility and Characterization of a Peptide Amphiphile Hydrogel for Applications in Peripheral Nerve Regeneration. Tissue Engineering. Part A, 21(7-8), 1333-1342.

+ Open protocol

+ Expand

Synthesis and Purification of Chlorotoxin Peptide

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

Chlorotoxin (CTX) was purchased from Iris Biotech GmbH (Marktredwitz, Germany). CTX fragments were chemically synthesized using standard stepwise Fmoc solid-phase peptide synthesis methods on the rink amide resin (Anaspec, Fremont, CA, USA) using an automated PS3 bench top peptide synthesizer (Protein Technologies, Tuscon, AZ, USA). Peptides were deprotected and cleaved from the resin using the following cleavage cocktail: 95% TFA: 2.5% TIPS: 2.5% H₂O (v/v/v). The peptide was then precipitated and washed several times with cold diethyl ether, dissolved in 50% acetonitrile:50% H₂O, lyophilized, and stored as lyophilized powder. Crude peptide mixtures were purified by reversed-phase HPLC (RP-HPLC) on a C₁₈ preparative column (Phenomenex Jupiter 250 × 21.2 mm, 10 μm, 300 Å). The peptides were eluted with a 1% gradient from 1 to 60% of solvent Β in solvent A over 60 min at the flow rate of 5 ml/min (Solvent A: 0.05% TFA/water, Solvent B: 0.05% TFA in 90% acetonitrile/water). The purified fractions were characterized by a SCIEX 5800 MALDI TOF/TOF mass spectrometer (SCIEX, Foster city, CA, USA).

Dastpeyman M., Giacomin P., Wilson D., Nolan M.J., Bansal P.S, & Daly N.L. (2019). A C-Terminal Fragment of Chlorotoxin Retains Bioactivity and Inhibits Cell Migration. Frontiers in Pharmacology, 10, 250.

+ Open protocol

+ Expand

Epigenetic Modification Analysis Toolkit

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

Unless specified otherwise, laboratory chemicals
and reagents were purchased from Sigma-Aldrich and used without additional
purification. Peptide synthesis reagents, including Fmoc amino acids
and Rink-amide resin, were purchased from Anaspec. Selectively methylated
Fmoc-arginine amino acids and H-Ala-sulfamylbutyryl NovaSyn TG resin
are products of Novabiochem (EMD Millipore). Plasmids containing human
PCAF and histone H3.3 were purchased from ATCC, and remaining molecular
biology materials were purchased from Invitrogen. Oligonucleotide
primers were from Integrated DNA Technologies. Restriction endonucleases,
recombinant human histones, and control DNA were purchased from New
England Biolabs. Histone H3R8me2a protein was purchased from ActiveMotif.
Spectrophotometric data were collected on a DU-640 spectrophotometer
(Beckman Coulter) unless indicated otherwise. Matrix-assisted laser
desorption/ionization (MALDI)-time of flight (TOF) and self-assembled
monolayers with matrix-assisted laser desorption-ionization (SAMDI)-TOF
mass spectrometry were performed on a 4800 MALDI TOF/TOF mass spectrometer
(Applied Biosystems) by manual and automated protocols. High-resolution
proteomic data were obtained on an Orbitrap Velos mass spectrometer
equipped with a nanoflow HPLC (Thermo Scientific). Gel filtration
was performed on an ÄKTA FPLC. All experiments were performed
in triplicate.

Kornacki J.R., Stuparu A.D, & Mrksich M. (2014). Acetyltransferase p300/CBP Associated Factor (PCAF) Regulates Crosstalk-Dependent Acetylation of Histone H3 by Distal Site Recognition. ACS Chemical Biology, 10(1), 157-164.

+ Open protocol

+ Expand

Phosphatase Activity Assay Protocol

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

Laboratory chemicals and reagents were purchased from MilliporeSigma and used without additional purification unless specified. Peptide synthesis reagents, including Fmoc amino acids and Rink-amide resin, were purchased from Anaspec. Phosphatases were purchased from MilliporeSigma. Self-assembled monolayers with matrix-assisted laser desorption-ionization (SAMDI) mass spectrometry were performed on a 5800 MALDI TOF/TOF mass spectrometer (AbSciex) using either manual or automated protocols. A detailed protocol of monolayer plate preparation, peptide synthesis and phosphatase assay can be found in a previously published method paper.^{44 (link)}

Huang C.F, & Mrksich M. (2019). Profiling Protein Tyrosine Phosphatase Specificity with SAMDI Mass Spectrometry and Peptide Arrays. ACS combinatorial science, 21(11), 760-769.

+ Open protocol

+ Expand

Peptide Synthesis Using Fmoc Chemistry

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

Peptides were manually synthesized using standard fmoc chemistry with blocked amino acids obtained from Anaspec, Inc. Each peptide was synthesized on a 0.1 mmol scale. Rink amide resin from Anaspec, Inc. was used as the solid support to provide C-terminal amidation. 31, 32 HPLC purification was done with a Vydac 218TP510 C-18 reversed-phase column on a Waters 600 system using an acetonitrile (ACN) solvent gradient from 20%

Tobias F, & Keiderling T.A. (2016). Role of Side Chains in β-Sheet Self-Assembly into Peptide Fibrils. IR and VCD Spectroscopic Studies of Glutamic Acid-Containing Peptides. Langmuir : the ACS journal of surfaces and colloids, 32(18).

+ 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!