Reagents, B

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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…

  • HOOK™ Iodoacetyl-LC-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 free…

  • HOOK™ NHS-dPEG™4-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…

  • Blue-OUT™

    G-Biosciences

    Blue-OUT™ is a unique product that washes the interfering Coomassie and fluorescent protein stains from gel pieces prior to their treatment for protein sequencing or mass spectrometry. Also supplied in the InGel™ Blue kit for the tryptic digestion and peptide extraction of…

  • G-Biosciences Bolton-Hunter Reagent conjugatestyrosine-like groups to end-terminal α-amino groups or ε-amino groups of lysineto increase the number of tyrosyl groups that can be iodinated by iodine-125 labeling procedures. Radioactive iodine ( 125 I) is routinely used by…

  • ( Bis (2-[Succinimidooxycarbonyloxy]ethyl) sulfone Features Molecular Weight: 436.35 Spacer Arm (Å): 13 Reactive Toward: Primary Amines Membrane Permeable: YES Water Soluble: NO Cleavable/ Reversible: Base

  • HOOK™-Biotin-Hydrazide

    G-Biosciences

    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…

  • The use of biotin for non-radioactive labeling of proteins and nucleic acids has become an increasingly popular technique in life science research. Several factors must be considered when coupling a biotin reagent to a protein in order to ensure a successful reaction. The primary consideration is…

  • HOOK™-Biotin-PDA

    G-Biosciences

    HOOK™ Biotin-PDA 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 free sulfhydryl…

  • HOOK™-NHS-LC-LC-Biotin

    G-Biosciences

    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 35 are…

  • HOOK™-NHS-LC-Biotin

    G-Biosciences

    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 are…

  • 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…

  • HOOK™-Biotin-BMMCC

    G-Biosciences

    HOOK™ Biotin-BMMCC 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 free sulfhydryl…

  • HOOK™-NHS-Biotin

    G-Biosciences

    HOOK™ 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 35 are…

  • Features Molecular Weight: 244.32

  • ß-Mercaptoethanol

    G-Biosciences

    High quality proteomic grade β-mercaptoethanol. β-mercaptoethanol, a popular reducing agent, is offered in 5ml and 100ml bottles. Features Synonym: β-Mercaptoethanol CAS#: 60-24-2 Molecular Formula: C2H6OS Molecular Weight: 78.13 …

  • HOOK™-NHS-SS-Biotin

    G-Biosciences

    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 are…

  • Bis (β-[4-azidosalicylamido]-ethyl) disulfide Iodinatable Features Molecular Weight: 474.52 Spacer Arm (Å): 21.3 Reactive Toward: Non Selective Membrane Permeable: YES Water Soluble: NO Cleavable/ Reversible: Reducing Agents (Thiols)

  • HOOK™-PFP-Biotin

    G-Biosciences

    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…

  • The use of biotin for non-radioactive labeling of proteins and nucleic acids has become an increasingly popular technique in life science research. Several factors must be considered when coupling a biotin reagent to a protein in order to ensure a successful reaction. The primary consideration is…

  • 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…

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