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

CaMKII beta/CAMK2B is a calcium/calmodulin-dependent protein kinase that functions autonomously upon Ca(2+)/calmodulin binding and autophosphorylation. It plays an important role in dendritic spine and synapse formation, neuronal plasticity, and the regulation of skeletal muscle sarcoplasmic reticulum Ca(2+) transport. 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.