Novel HIF2A mutations disrupt oxygen sensing, leading to polycythemia, paragangliomas, and somatostatinomas Blood, Mar 2013; 121: 2563 - 2566.
[anti-HA]
Regulation of the PI3-K/Akt Survival Pathway in the Rat Endometrium Biol Reprod, Mar 2013; 88: 79.
[Akt3]
RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP Nucleic Acids Res., Mar 2013; 10.1093/nar/gkt159.
[LA]
Ruxolitinib as potential targeted therapy for patients with JAK2 rearrangements Haematologica, Mar 2013; 98: 404 - 408.
[JAK2]
A synthetic peptide corresponding to residues in human C1q (subunit B) was used as an immunogen.
Buffer
Store at -20 C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
The complement component C1 is a protein complex that consists of six subunits of C1q. Each C1q subunit of the complex is known to bind to immune complexes, which often are deposited in the basement membrane. C1q is a versatile recognition protein that triggers activation of the classical pathway of complement, where the first step involves the binding of the globular domain of Clq to the Fc regions of aggregated IgG or IgM. The C1q globular domain is a heterotrimer of the C-terminal halves of one A, one B, and one C chain, held together mainly by non-polar interactions, with a Ca2+ ion bound at the top. A modular organization has been suggested of the globular domain, consistent with the view that A, B, and C chains are functionally autonomous modules and have distinct and differential ligand-binding properties (1-3).
Related Pathway
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