Recombinant Human CAMK2G Protein, N-His

Description of Recombinant Human CAMK2G Protein, N-His

The structure of Recombinant Human CAMK2G Protein is a crucial aspect that determines its function and activity. CAMK2G, also known as Calcium/calmodulin-dependent protein kinase type II subunit gamma, is a member of the CAMK2 family of serine/threonine protein kinases. It is encoded by the CAMK2G gene and is primarily expressed in the brain, heart, and skeletal muscle.

The Recombinant Human CAMK2G Protein is a 53 kDa protein with a highly conserved catalytic domain and a regulatory domain. The catalytic domain contains the ATP binding site and the catalytic residues, which are essential for the enzymatic activity of the protein. The regulatory domain, on the other hand, contains the calmodulin binding site, which plays a crucial role in the activation of the protein.

The crystal structure of Recombinant Human CAMK2G Protein has been extensively studied, and it has been found to be a dodecamer, consisting of 12 subunits arranged in a hexagonal ring. Each subunit is composed of three distinct regions: the N-terminal domain, the catalytic domain, and the regulatory domain. The N-terminal domain is responsible for the assembly of the dodecamer, while the catalytic and regulatory domains are involved in the enzymatic activity of the protein.

Recombinant Human CAMK2G Protein is a multifunctional protein that plays a vital role in various cellular processes, including neuronal signaling, synaptic plasticity, and muscle contraction. The activity of the protein is regulated by the binding of calcium/calmodulin, which leads to the autophosphorylation of specific residues in the regulatory domain. This autophosphorylation results in the activation of the protein, allowing it to phosphorylate its substrates.

The primary substrate of Recombinant Human CAMK2G Protein is the α subunit of the AMP-activated protein kinase (AMPK). Phosphorylation of this subunit by CAMK2G leads to the activation of AMPK, which plays a crucial role in energy homeostasis and metabolism. Additionally, CAMK2G has been shown to phosphorylate other substrates, such as ion channels, transcription factors, and cytoskeletal proteins, which further highlights its diverse role in cellular processes.

The activity of Recombinant Human CAMK2G Protein is also regulated by other factors, such as protein-protein interactions and post-translational modifications. For example, binding of the protein to its regulatory subunit, CAMK2B, can modulate its activity and substrate specificity. Furthermore, phosphorylation of specific residues by other kinases can also affect the activity of CAMK2G.

The unique structural and functional characteristics of Recombinant Human CAMK2G Protein make it a valuable tool in various research fields. One of its primary applications is in the study of neurological disorders, as CAMK2G has been implicated in the pathogenesis of diseases such as Alzheimer’s, Parkinson’s, and schizophrenia. Recombinant Human CAMK2G Protein can be used to investigate the role of this protein in these disorders and potentially develop therapeutic interventions.

Additionally, Recombinant Human CAMK2G Protein has been used in drug discovery and development. As CAMK2G is involved in various cellular processes, it is a potential target for the development of drugs to treat diseases such as cancer, diabetes, and cardiovascular disorders. Recombinant Human CAMK2G Protein can be used to screen for potential inhibitors or activators of the protein, which can then be further studied for their therapeutic potential.

Furthermore, Recombinant Human CAMK2G Protein has been used in studies related to muscle contraction and exercise physiology. As CAMK2G is a key regulator of muscle contraction,