You searched for: Protein Extraction Reagents

Supplier: G-Biosciences

Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues and typically there is little or no cleavage at arginyl-proline and lysyl-proline bonds. The distribution of these residues in proteins allows trypsin digestion to produce peptides that are readily identified by mass spectrometry.

Supplier: Thermo Fisher Scientific

Immobilised Pepsin agarose consists of an acidic endopeptidase that has been immobilised onto beaded agarose resin to enable generation and purification of Fab and F(ab')2 fragments from antibodies.

Supplier: Thermo Fisher Scientific

Pierce™ Trypsin Protease, MS Grade, is highly purified porcine trypsin that has been chemically modified for maximum activity and stability in proteomic applications.

Supplier: Thermo Fisher Scientific

The Digestion Indicator for Mass Spectrometry is a non-mammalian recombinant protein (26kDa) with five signature peptides for use in determining the digestion efficiency and reproducibility across multiple samples.

Supplier: Thermo Fisher Scientific

This Micrococcal Nuclease (MNase) is suitable for removing nucleic acids from cell lysates, releasing chromatin-bound proteins and shearing chromatin for use in chromatin immunoprecipitation (ChIP) experiments.

Supplier: G-Biosciences

A proteolytic enzyme immobilised on 4% agarose that is routinely used for the generation of F(ab’)₂ fragments from Immunoglobulin G (IgG). The pepsin has the ability to cleave the heavy chains near the hinge region. The immobilised Pepsin offers the distinct advantage of eliminating enzyme contamination of the F(ab)₂ fragments.

Supplier: Thermo Fisher Scientific

SDS-Out™ SDS Precipitation Kit provides convenient removal of SDS from small-volume (0,1 to 10 ml) protein samples.

Supplier: G-Biosciences

A cysteine protease enzyme (EC 3.4.22.2) immobilised on 4% agarose, cleaves Immunoglobulin G (IgG) antibody molecules in the hinge region, generating three ~50 kDa fragments; two Fab domains and a Fc domain. The papain-digested antibody is unable to promote agglutination, precipitation, opsonisation, and lysis.

Supplier: Merck Millipore (Novagen)

The CytoBuster™ protein extraction reagent is a proprietary formulation of detergents optimised for efficient extraction of soluble proteins from mammalian and insect cells. The gentle, non-ionic composition of the reagent enables isolation of functionally active endogenous or expressed proteins without a need for secondary treatment such as sonication or freeze/thaw.

Supplier: Merck Millipore (Novagen)

BugBuster® master mix combines BugBuster® protein extraction reagent with Benzonase® Nuclease and rLysozyme™ solution in one convenient reagent. It allows for maximum recovery of active soluble protein from both Gram-negative and Gram-positive bacteria. The master mix provides sufficient reagents for protein extraction from 20 g and 100 g cell paste.

Supplier: Merck Millipore (Novagen)

PopCulture® Reagent is a detergent-based concentrate that can be added directly to cultures of E. coli to effectively extract proteins without the need for cell harvest. Recombinant proteins can be directly screened in the crude extract, or purified by adding an affinity matrix, washing the matrix-target protein complex to remove spent culture medium and cellular contaminants, and eluting the purified protein from the matrix. The PopCulture protein purification procedure is ideally suited to high-throughput robotic processing of samples for proteomics research or any application that would benefit from the increased speed and convenience.

Supplier: Merck Millipore (Calbiochem‎)

Native endoproteinase Glu-C from Staphylococcus aureus. Serine protease that specifically hydrolyses peptide bonds at the carboxylic side of glutamic acid and aspartic acid residues. Inhibited by DFP and α2-macroglobulin. Suggested working concentration: 1:20 to 1:100 (protease:protein by weight) for sequence analysis.

Supplier: Merck Millipore (Calbiochem‎)

Native endoproteinase Asp-N from Pseudomonas fragi. Designed for protein sequencing or sequence verification, analysis of protein structural domains, and cleavage of fusion proteins. Metalloprotease that specifically hydrolyses proteins at the N-terminal side of aspartic acid and cysteic acid residues. Inhibited by aprotinin, DFP, leupeptin, and TLCK. Suggested working concentration: 1:20 to 1:100 (protease:protein by weight) for sequence analysis.

Supplier: G-Biosciences

Protein-OUT™ is a washing solution that cleans plastic and glassware used in the proteolytic digestion and peptide isolation for mass spectrometry analysis. The rinsing of plastic and glassware with Protein-OUT™ will remove interfering chemicals and peptides that can leach from the tube walls and interfere or suppress the mass spectrometry signal. In addition, rinsing with Protein-OUT™ removes inadvertent contamination with dust and keratin.

Supplier: VARIAN

Uniform latex particles are used in a wide range of applications that exploit their physico-chemical properties in sophisticated immunoassay formats, both in medicine and veterinary science research.