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Home > Proteins & Peptides > A-Z Proteins
All natural and recombinant proteins.
    6292 A-Z Proteins Products
  • BP002491-CKI-275: Recombinant Human Creatine Kinase, Mitochondrial 1A (CKMT1A) Enzyme

    Source: E. coli-derived.
    Purity: > 95% as determined by SDS-PAGE.

  • BP002493-PKA-033: Recombinant Human Cyclin-A2 (CCNA2) Protein

    Source: E. coli-derived.
    Purity: > 90% as determined by SDS-PAGE.

  • BP002494-PKA-037: Recombinant Human Cyclin-B1 (CCNB1) Protein

    Source: E. coli-derived.
    Purity: > 80% as determined by SDS-PAGE.

  • BP002495-PKA-035: Recombinant Human Cyclin-B2 (CCNB2) Protein

    Source: E. coli-derived.
    Purity: > 90% as determined by SDS-PAGE.

  • BP002496-PKA-311: Recombinant Human Cyclin C (CCNC) Protein

    Source: E. coli-derived.
    Purity: > 98% as determined by SDS-PAGE.
    Applications: WB, ELISA.

  • BP002498-PRO-1005: Recombinant Human Cyclin G1 (CCNG1) Protein

    Source: E. coli-derived.
    Purity: > 85% as determined by SDS-PAGE.

  • BP002500-PKA-362: Recombinant Human Cyclin-Dependent Kinase 2 Associated Protein 1 (CDK2AP1) Enzyme

    Source: E. coli-derived.
    Purity: > 95.0% as determined by SDS-PAGE.

  • BP002505-ENZ-174: Recombinant Human Peptidyl-prolyl cis-trans isomerase-like 3 (PPIL3) Enzyme

    Source: E. coli-derived.
    Specific activity is > 280 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.
    Purity: > 90.0% as determined by SDS-PAGE.

  • BP002506-ENZ-147: Recombinant Human Adenosine Deaminase (ADA) Enzyme

    Source: E. coli-derived.
    Specific activity: approximately >25 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme that deaminates 1.0 umol of adenosine to inosine per minute at pH 7.5 at 25C.
    Purity: > 85.0% as determined by SDS-PAGE.

  • BP002507-ENZ-180: Recombinant Human Serine Dehydratase-Like (SDSL) Enzyme

    Source: E. coli-derived.
    Purity: > 90% as determined by SDS-PAGE.

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