Proteomics
Our Protein Research section covers the spectrum of research products for proteomics.
There are products for Protein Purification, including Protein Extraction, Fractionation, Sample Preparation and Protein Concentration.
Our Protein Analysis products cover Protein Electrophoresis, Western Blot, and Mass Spectrometry. A wide selection of Protein Labeling and Protein Modification tools are available for protein binding and protein structure studies.
A large selection of Protein Assays are available, including unique Protein Estimation Assays.
Keyhole limpet hemocyanin is a widely used carrier protein due to its large molecular mass (4.5x105-1.3x107Da aggregates) and large number of primary amines that can react with cross-linkers for the coupling of peptides. The KLH is supplied as a clear to slightly hazy, bluish solution in phosphate b..
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The blot is prepared using total protein extracted from a variety of species, where whole species is not available the whole liver lysate is used. These blots can be used to identify similar proteins in other species, including human, chicken, frog, worm, drosophila, yeast, aspergillus, E. col..
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A proteomic grade iodoacetamide in two different quantities. Iodoacetamide is supplied in 5gm bulk quantities or in the OneQuant™ format.
OneQuant™ Iodoacetamide
OneQuant™ iodoacetamide are single aliquots of iodoacetamide that eliminate the need for weighing, preventing ..
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A Solid Phase Iodination Reagent
Radioactive iodine (125I) is routinely used by researchers to label proteins. The iodination of proteins can be performed enzymatically or chemically. The Iodination reagent is designed to aid in the labeling of proteins with radioactive iodine.
The iodinat..
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-500x500h.jpg "Insect PE LB™")
Insect Cell-PE LB™ has been developed for extraction of cytoplasmic soluble protein from insect cultured cells. The Insect Cell-PE LB™ is based on organic buffering agents, which utilizes a mild non-ionic detergent, and a proprietary combination of various salts and agents to enhance ext..
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A reliable method for the proteolytic digestion and subsequent extration of silver stained proteins in gel for subsequent analysis by mass spectrometry.
The protein spots are first excised from the gel and transferred to a proteomic grade tube. Silver stained gel pieces are washed with Sil..
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The InGel™ Blue kit provides a complete set of reagents for the in gel tryptic digestion and extraction of peptides for mass spectrometry (MALDI and LC MS/MS). The kit is specifically designed for use with Coomassie or fluorescent stained protein spots/bands.
The kit has all th..
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A 96-well format kit suitable for processing larger numbers of protein spots concurrently and compatible with spot-picking instruments. Fewer than 96 samples a batch may also be processed without any waste.
Excise protein spots and transfer to the supplied proteomic grade titer plate, des..
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Gene/Protein:
Immobilized Trypsin is TPCK Treated Trypsin immobilized on 4% agarose that eliminates the contamination of protein digests by the trypsin. The immobilized trypsin is readily removed by separating the agarose from the digestion solution.
Trypsin is a serine endopeptidase that spe..
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-500x500h.jpg "Immobilized Streptavidin Resin")
Biotin, a 244Da vitamin (Vitamin H) molecule, exhibits an extraordinary binding affinity for avidin (Ka=10¹âµM-¹) and streptavidin (Ka=10¹âµM-¹). Biotin and (strept)avidin interaction is rapid. Once the bond is established, it can survive up to 3M guanid..
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-500x500h.jpg "Immobilized Protein G")
Gene/Protein:
Immobilized protein G is for binding the constant domains of immunoglobulin (Ig) molecules (see Figure 1). It is ideal for the easy one-step purification of classes, subclasses and fragments of immunoglobulins for biological fluids and cell culture media. Protein G is a modified form of Streptococca..
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-500x500h.jpg "Immobilized Protein A")
Gene/Protein:
Immobilized Protein A is for binding the constant domains of immunoglobulin (Ig) molecules (see Figure 1). Protein A is coupled to agarose beads by reductive amination method that provides high coupling efficiency for immunoglobulins and minimal protein A leaching (<5ng protein A/ml). Our im..
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-500x500h.jpg "IBS™ Buffer")
Gene/Protein:
The expression of recombinant proteins is a popular and routinely used technique in protein studies. The expression of recombinant proteins often has one drawback and that is the recombinant proteins aggregate and form inclusion bodies, especially when expressed at high levels. The aggre..
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The expression of recombinant proteins is a popular and routinely used technique in protein studies. The expression of recombinant proteins often has one drawback and that is the recombinant proteins aggregate and form inclusion bodies, especially when expressed at high levels. The aggre..
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HyperCarrier™ is normal BSA that has been treated with ethylene diamine, which substitutes anionic carboxyl groups with cationic aminoethyl-amide groups.
Researchers were able to demonstrate that a cationized form of BSA, produced by replacing anionic side chain carboxylic groups with..
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Gene/Protein:
HOOK™ Sulfo-NHS-SS-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up t..
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HOOK™ Sulfo-NHS-LC-LC-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which u..
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Gene/Protein:
HOOK™-Sulfo-NHS-LC-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up t..
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HOOK™ Sulfo-NHS-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 3..
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The use of biotin for non-radioactive labeling of proteins and nucleic acids has now become an increasingly popular technique in life science research. Several factors must be considered when coupling a biotin reagent to a protein to ensure a successful reaction. The primary consideration is the sel..
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HOOK™ PFP-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 35 are ..
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HOOK™ PEG2-Iodoacetyl-Biotin reacts with protein free sulhydryl groups.
Sulfhydryl reactive reagents are more specific and react only with free sulfhydryl residues (-SH or thiol groups). The side chain of the amino acid cysteine is the most common source of free sulfhydryl groups.
If..
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HOOK™ NHS-SS-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 35 a..
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HOOK™ NHS-LC-LC-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 3..
$0.00
HOOK™-NHS-LC-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 35 a..
$0.00