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Anti-Dynein Antibody, IC, cytosolic, clone 74.1, Alexa Fluor(R) 555 conjugate clone 74.1, from mouse, ALEXA FLUOR(R) 555

ITEM#: 3042-MAB1618AF555

MFR#: MAB1618-AF555

Cytoplasmic dynein 1 intermediate chain 1 (UniProt Q29RQ3; also known as Cytoplasmic dynein intermediate chain 1, Dynein intermediate chain 1, cytosolic, DH IC-1) and Cytoplasmic dynein 1 intermediate chain 2 (UniProt Q0III3; also known as Cytoplasmi

Cytoplasmic dynein 1 intermediate chain 1 (UniProt Q29RQ3; also known as Cytoplasmic dynein intermediate chain 1, Dynein intermediate chain 1, cytosolic, DH IC-1) and Cytoplasmic dynein 1 intermediate chain 2 (UniProt Q0III3; also known as Cytoplasmic dynein intermediate chain 2, Dynein intermediate chain 2, cytosolic, DH IC-2) are encoded by the DYNC1I1 gene (Gene ID 613724) and DYNC1I2 gene (Gene ID 526329) in bovine, respectively. Cytoplasmic dynein complexes are microtubules-associated retrograde transport motors. Cytoplasmic dynein 1 is the more abundant motor in cells, while cytoplasmic dynein 2 takes part in intraflagellar transport. Cytoplasmic dynein 1 is a multisubunit complex of >=1.5 MDa composed of a homodimer of heavy chains (encoded by DYNC1H1), two intermediate chains (encoded by DYNC1I1 and DYNC1I2), light-intermediate chains (encoded by DYNC1LI1, DYNC1LI2) and light chains (encoded by DYNLT1, DYNLT3, DYNLRB1, DYNLRB2, DYNLL1, DYNLLl2). The heavy chain homodimer acts as the dynein complex core and binds microtubules to enable ATP-dependent cytoplasmic dynein movement. The other dynein subunits associate as homodimers and play regulatory roles in maintaining the complex stability, modulating its activity, and mediating its interaction with accessory and cargo proteins. The intermediate chain proteins (IC1 & IC2) are involved in cargo binding and specificity, either alone or via interaction with the dynactin complex. IC1 and IC2 share 69% protein identity. They interact with the dynein light chains and the p150 subunit of dynactin at the N-terminus and with the heavy chains through WD40 repeats at the intermediate chain C-terminus.