CaMKII beta/CAMK2B Protein, Human (sf9, His-GST)

CaMKII beta/CAMK2B, a calcium/calmodulin-dependent protein kinase, autonomously functions after Ca(2+)/calmodulin-binding and autophosphorylation. It plays vital roles in dendritic spine and synapse formation, neuronal plasticity, and the regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, it contributes to actin cytoskeleton reorganization, dendritic arborization, and migration of developing neurons. Additionally, it modulates skeletal muscle function in response to exercise and participates in the JAK-STAT signaling pathway by phosphorylating STAT1. Moreover, it phosphorylates RETREG1, enhancing its reticulophagy activity under endoplasmic reticulum stress conditions. CaMKII beta/CAMK2B Protein, Human (sf9, His-GST) is the recombinant human-derived CaMKII beta/CAMK2B protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of CaMKII beta/CAMK2B Protein, Human (sf9, His-GST) is 503 a.a., with molecular weight of ~85 kDa.

CaMKII beta/CAMK2B, a calcium/calmodulin-dependent protein kinase, functions autonomously upon Ca(2+)/calmodulin-binding and autophosphorylation, playing pivotal roles in dendritic spine and synapse formation, neuronal plasticity, and the regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, this kinase exhibits an essential structural function, orchestrating the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural role is critical for the precise targeting of CaMK2A, a downstream effector of NMDAR, facilitating dendritic spine and synapse formation and sustaining synaptic plasticity for long-term potentiation (LTP) and hippocampus-dependent learning. Furthermore, in developing hippocampal neurons, CaMKII beta promotes dendritic tree arborization, and in mature neurons, it contributes to dendritic remodeling. Additionally, it plays a role in the modulation of skeletal muscle function in response to exercise, impacting sarcoplasmic reticulum (SR) Ca(2+) transport regulation. In slow-twitch muscles, it is involved in regulating SR Ca(2+) transport, while in fast-twitch muscles, it controls Ca(2+) release from the SR through phosphorylation of triadin and phospholamban. Responding to interferon-gamma (IFN-gamma) stimulation, CaMKII beta catalyzes the phosphorylation of STAT1, thereby stimulating the JAK-STAT signaling pathway. Moreover, under endoplasmic reticulum stress conditions, it phosphorylates the reticulophagy regulator RETREG1 at 'Ser-151', enhancing RETREG1 oligomerization and its membrane scission and reticulophagy activity.

Human

Sf9 insect cells

N-His;N-GST

Q13554-3 (M1-Q503)

816  [NCBI]

Approximately 85 kDa

Greater than 80% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.