Measured by its binding ability in a functional ELISA. When Recombinant Human Cerebellin-2 is coated at 5 μg/mL, biotinylated recombinant rat NRXN-1 beta binds with an apparent KD <1.5 nM. Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Recombinant Human Cerebellin-2, immobilized at 3-30 μg/mL, is able to significantly enhance neurite outgrowth.
Function Acts as a synaptic organizer in specific subsets of neurons in the brain (By similarity). Essential for long-term maintenance but not establishment of excitatory synapses (By similarity).
Measured by its binding ability in a functional ELISA. When Recombinant Human Cerebellin-2 is coated at 5 μg/mL, biotinylated recombinant rat NRXN-1 beta binds with an apparent KD <1.5 nM. Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Recombinant Human Cerebellin-2, immobilized at 3-30 μg/mL, is able to significantly enhance neurite outgrowth.
Lyophilized from 10mM PBS, 5% Trehalose, 5% Mannitol, pH 7.4
复溶
Reconstitute in sterile water to a concentration of 0.1-0.5 mg/ml.
储存条件
-20°C储存,避免反复冻融
运输条件
超低温运输
稳定性与储存
在 -20~-80℃ 下可保存 1 年以上。复溶后建议分装。避免冷冻/解冻循环。
图片
Recombinant Human Cerebellin-2 Protein (rp166920) - SDS-PAGE 2 μg/lane of Recombinant Human Cerebellin-2 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 28 kDa under reducing conditions and >120 kDa under non-reducing conditions. Cerebellin-2 protein forms a stable homohexamer through dual-layer disulfide bonding: 1.Trimer formation: Three identical subunits associate via non-covalent interactions of their globular C1q domains and are stabilized by inter-subunit disulfide bonds, constituting a homotrimer. 2.Hexamer assembly: Two trimers connect through disulfide bonds formed by N-terminal cysteine residues, ultimately yielding a covalently linked hexamer. This hierarchical architecture relies on disulfide bonds and C1q domains to ensure protein stability and function (inferred from homologous proteins).