Monoclonal Anti-DYNLT3 antibody produced in mouse

DYNLT3 has been located in both the cytoplasm and the nucleus, in cell- and tissue-specific manners. The subunit binds to SATB1 complex and the activity of this complex is independent of the dynein motor.

Monoclonal Anti-DYNLT3 (mouse IgG2a isotype) is derived from the hybridoma R1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with rat dynein 3 light chain-myosin basic protein fusion protein. DYNLT3 belongs to the Tctex-light chain family. It is also known as rp3.

rat dynein 3 light chain myosin basic protein fusion protein.

Monoclonal Anti-DYNLT3 antibody produced in mouse has been used in immunoblotting and immunoprecipitation.

Cytoplasmic dynein motor complex is responsible for minus-end, microtubule-based motile processes. It is thus involved in a wide range of eukaryotic cellular processes including trafficking of membranal vesicles, viruses and other intracellular particles. DYNLT3 is a light chain subunit of the complex that binds to Bub3, a spindle checkpoint protein and is depleted from the kinetochore during chromosome alignment. It contributes to dynein cargo binding specificity as dynein binds directly to a component of the spindle checkpoint complex through this light chain. The interaction of the Herpes simplex virus capsid protein VP26 with dynein light chains facilitates the binding of the virus capsid to cytoplasmic dynein during cellular infection.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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