DYNLL2 Recombinant Protein

DYNLL2 Recombinant Protein

Catalog Number:
P001415759ABE
Mfr. No.:
Abe32-3696
Price:
  • Size:
    20 µg
    Quantity:
    Add to Cart:
      • Overview
        • DYNLL2 Human Recombinant produced in E. Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89a.a) and having a molecular mass of 12.5kDa. DYNLL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Dyneins are multi-subunit, high molecular weight ATPases which cooperate with microtubules to create energy by altering the chemical energy of ATP into the mechanical energy of movement. DYNLL2 is a large protein complex made up of six different subunits and is in charge of a large number of intracellular movements to the minus ends of microtubules. DYNLL2 is an extremely conserved eukaryotic hub protein with dozens of binding partners and numerous roles other than being a subunit of dynein and myosin Va motor proteins.

          Please contact us at for specific academic pricing.

      • Properties
        • Protein Name
          Dynein light chain LC8-type 2, DNCL1B, Dlc2, MGC17810, RSPH22, 8kDa dynein light chain b, DLC8b, dynein light chain 2 cytoplasmic, radial spoke 22 homolog.
          Source
          E. coli
          Type
          Recombinant Proteins
          Purification
          Greater than 90.0% as determined by SDS-PAGE.
          Formulation
          DYNLL2 protein solution (1 mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl and 1mM DTT.
          Storage
          DYNLL2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

          * For Research Use Only. Not for use in diagnostic/therapeutics procedures.

    Note: If you don't receive our verification email, do the following:

    • Confirm that you entered your email address correctly.
    • Check if the email is in your spam or junk folder.
    • Or you may contact us at .
    Copyright © Amerigo Scientific. All rights reserved.