Recombinant Human DYNLL2 Protein, N-His-SUMO from ProteoGenix; catalogue ARO-P11252; research use only.
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Recombinant Human DYNLL2 Protein, also known as Dynein Light Chain LC8-Type 2 or DLC8, is a protein that plays a crucial role in a variety of cellular processes. It is a member of the dynein light chain family and is highly conserved across species, with a 97% sequence identity between human and mouse. The protein is encoded by the DYNLL2 gene and is expressed in almost all tissues, with the highest levels found in the brain, heart, and skeletal muscle.
Recombinant Human DYNLL2 Protein is a small protein consisting of 89 amino acids with a molecular weight of approximately 10 kDa. It has a globular structure with a beta-sheet core surrounded by alpha-helices. The protein contains a highly conserved LC8 domain, which is essential for its function. DYNLL2 also has a flexible C-terminal tail that is involved in protein-protein interactions.
The recombinant form of DYNLL2 is produced by cloning the DYNLL2 gene into a suitable expression vector and expressing it in a host organism, usually E. coli or yeast. This allows for large-scale production of the protein for research purposes.
Recombinant Human DYNLL2 Protein is a multifunctional protein that is involved in a wide range of cellular processes. It was initially identified as a subunit of the dynein motor complex, which is responsible for intracellular transport along microtubules. DYNLL2 binds to the light chain of the dynein motor and facilitates its movement, thus playing a crucial role in cellular transport processes.
Aside from its role in intracellular transport, DYNLL2 has also been found to interact with a variety of other proteins, including transcription factors, cytoskeletal proteins, and enzymes. These interactions suggest that DYNLL2 may have a regulatory role in various cellular processes, such as cell division, apoptosis, and metabolism.
Recent studies have also shown that DYNLL2 is involved in the regulation of mitosis and cytokinesis. It has been found to interact with the spindle checkpoint protein Bub3 and play a crucial role in ensuring proper chromosome segregation during cell division. DYNLL2 has also been implicated in the regulation of cytokinesis by interacting with the contractile ring protein Anillin.
Recombinant Human DYNLL2 Protein has a wide range of applications in scientific research, particularly in the fields of cell biology and molecular biology. Its involvement in various cellular processes makes it a valuable tool for studying the function and regulation of these processes.
One of the main applications of DYNLL2 is in the study of intracellular transport. Its interaction with the dynein motor complex makes it a useful tool for investigating the mechanisms of intracellular transport and its role in various diseases, such as neurodegenerative disorders and cancer.
Additionally, DYNLL2 has been found to have potential as a therapeutic target. Its involvement in cell division and cytokinesis makes it a promising target for the development of new cancer treatments. Furthermore, its interaction with various signaling proteins suggests that it may have a role in regulating cellular processes that are dysregulated in diseases such as diabetes and cardiovascular diseases.
Recombinant Human DYNLL2 Protein is a highly conserved and multifunctional protein that plays a crucial role in various cellular processes. Its structure and activity make it a valuable tool for studying intracellular transport and its potential as a therapeutic target. As research on DYNLL2 continues, it is likely that its applications in scientific research and medicine will continue to expand.
ProteoGenix catalogue number ARO-P11252. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 22.56 kDa; Fragment: Ser2-Gly89; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
This product is manufactured by ProteoGenix and sold through ABMIUM without relabelling.
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