Magic™ Anti-hCG monoclonal antibody, clone N/A

As a quantitatively inherited trait related to high yield potential, grain weight (GW) development in wheat is constrained by abiotic stresses such as limited water supply and high temperature. Data from a doubled haploid population, derived from a cross of (Hanxuan 10 x Lumai 14), grown in four environments were used to explore the genetic basis of GW developmental behavior in unconditional and conditional quantitative trait locus (QTL) analyses using a mixed linear model. Thirty additive QTLs and 41 pairs of epistatic QTLs were detected, and were more frequently observed on chromosomes 1B, 2A, 2D, 4A, 4B and 7B. No single QTL was continually active during all stages or periods of grain growth. The QTLs with additive effects (A-QTLs) expressed in the period S1|S0 (the period from the flowering to the seventh day after) formed a foundation for GW development. GW development at these stages can be used as an index for screening superior genotypes under diverse abiotic stresses in a wheat breeding program. One QTL, i.e. Qgw.cgb-6A.2, showed high adaptability for water-limited and heat-stress environments. Many A-QTLs interacted with more than one other QTL in the two genetic models, such as Qgw.cgb-4B.2 interacted with five QTLs, showing that the genetic architecture underlying GW development involves a collective expression of genes with additive and epistatic effects.

Although the role of secretory granules as the inositol 1,4,5-trisphosphate (IP3)-sensitive intracellular Ca2+ store and the presence of the IP3 receptor (IP3R)/Ca2+ channel on the secretory granule membrane have been established, the identity of the IP3R types present in the secretory granules is not known. We have therefore investigated the presence of different types of IP3R in the secretory granules of bovine adrenal medullary chromaffin cells using immunogold electron microscopy and found the existence of all three types of IP3R in the secretory granules. To determine whether these IP(3)Rs interact with CGA and CGB, each IP3R isoform was cotransfected with CGA or CGB into NIH3T3 or COS-7 cells, and the expressed IP3R isoform. and CGA or CGB were co-immunoprecipitated. From these studies it was shown that all three types of IP3R form complexes with CGA and CGB in the cells. To further confirm whether the IP3R isoforms and CGA and CGB form a complex in the secretory granules the potential interaction between all three isoforms of IP3R and CGA and CGB was tested by co-immunoprecipitation experiements of the mixture of secretory granule lysates and the granule membrane proteins. The three isoforms of IP3R were shown to form complexes with CGA and CGB, indicating the complex formation between the three isoforms of IP3R and CGA and CGB in the secretory granules. Moreover, the pH-dependent Ca2+ binding property of CGB was also studied using purified recombinant CGB, and it was shown that CGB bound 93 mol of Ca2+/mol with a dissociation constant (K-d) of 1.5 mm at pH 5.5 but virtually no Ca2+ at pH 7.5. The high capacity, low affinity Ca2+-binding property of CGB at pH 5.5 is comparable with that of CGA and is in line with its role as a Ca2+ storage protein in the secretory granules.