Anti-ICK (aa 448-497) polyclonal antibody

We investigate theoretically the quantum phase transition (QPT) between the one-channel Kondo (ICK) and two-channel Kondo (2CK) fixed points in a quantum dot coupled to helical edge states of interacting 2D topological insulators (2DTI) with Luttinger parameter 0 < K < 1. The model was studied by Law et al (2010 Phys. Rev. B 81 041305(R)), and was mapped onto an anisotropic two-channel Kondo model via bosonization. For K < 1, the strong coupling 2CK fixed point was argued to be stable for infinitesimally weak tunnelings between the dot and the 2DTI based on a simple scaling dimensional analysis (Law et al 2010 Phys. Rev. B 81 041305(R). We re-examine this model beyond the bare scaling dimension analysis via a one-loop renormalization group (RG) approach combined with bosonization and re-fermionization techniques near weak-coupling and strong-coupling (2CK) fixed points. We find for a fixed value of K < 1 that the 2CK fixed point can be unstable towards the 1CK fixed point and the system is expected to undergo a quantum phase transition between 1CK and 2CK fixed points with changing Kondo couplings. Our RG approach is controlled near K = 1. In general, this QPT can also occur upon tuning the Luttinger parameter K to a critical value K-c smaller than unity (0 < K-c < 1) for fixed Konodo couplings. The QPT in our model comes as a result of the combined Kondo and the helical Luttinger physics in 2DTI, and it serves as the first example of the 1CK-2CK QPT that is accessible by the controlled RG approach. We extract quantum critical and crossover behaviors from various thermodynamical quantities near the transition. Our results are robust against particle-hole asymmetry for 1/2 < K < 1.

Inhibitor cysteine knot (ICK) peptides exhibit ion channel blocking, insecticidal, and antimicrobial activities, but currently, no functional roles for bee-derived ICK peptides have been identified. In this study, a bee (Apis cerana) ICK peptide (AcICK) that acts as an antifungal peptide and as an insecticidal venom toxin was identified. AcICK contains an ICK fold that is expressed in the epidermis, fat body, or venom gland and is present as a 6.6-kDa peptide in bee venom. Recombinant AcICK peptide (expressed in baculovirus-infected insect cells) bound directly to Beauveria bassiana and Fusarium graminearum, but not to Escherichia coli or Bacillus thuringiensis. Consistent with these findings, AcICK showed antifungal activity, indicating that AcICK acts as an antifungal peptide. Furthermore, AcICK expression is induced in the fat body and epidermis after injection with B. bassiana. These results provide insight into the role of AcICK during the innate immune response following fungal infection. Additionally, we show that AcICK has insecticidal activity. Our results demonstrate a functional role for AcICK in bees: AcICK acts as an antifungal peptide in innate immune reactions in the body and as an insecticidal toxin in venom. The finding that the AcICK peptide functions with different mechanisms of action in the body and in venom highlights the two-pronged strategy that is possible with the bee ICK peptide. (C) 2014 Elsevier Ltd. All rights reserved.