Batch dependent - please inquire should you have specific requirements.
Buffer
0.01M pH7.4 PBS
Preservative
None
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Antigen Description
Vitamin K is a group of structurally similar; fat-soluble vitamins the human body requires for complete synthesis of certain proteins that are prerequisites for blood coagulation that the body needs for controlling binding of calcium in bones and other tissues. The vitamin K-related modification of the proteins allows them to bind calcium ions; which they cannot do otherwise. Without vitamin K; blood coagulation is seriously impaired; and uncontrolled bleeding occurs. Low levels of vitamin K also weaken bones and promote calcification of arteries and other soft tissues.
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References
Pulse ENDOR studies on the radical pair P(700)(+center dot)A(1)(center dot-) and the photoaccumulated quinone acceptor A(1)(center dot-) of photosystem I
The secondary acceptor A(1) of the electron transport chain(s) of photosystem (PS) I is a phylloquinone (vitamin K-1, VK1). Pulse electron paramagnetic resonance and electron nuclear double resonance (ENDOR) experiments at X-band frequencies were performed on the photoaccumulated acceptor radical A(1)(.-) and the radical pair state P(700)(.+)A(1)(.-) in PS I of Thermosynechococcus elongatus. The data obtained were compared with data from the respective radical anion of VK1 in organic solvents. The unusual g tensor magnitude of A(1)(.-) is explained by the hydrophobic binding pocket of this radical. The hyperfine couplings and the spin (and charge) density distribution is very different for A(1)(.-) in PS I and VK1.- in frozen alcoholic solution. This is attributed to a rather strong one-sided hydrogen bond to A(1)(.-). The presence of a hydrogen bond to A(1)(.-) has only a minor effect on g. The hyperfine coupling constants of A(1)(.-) determined from the radical pair spectra deviate only slightly from those derived from photoaccumulated A(1)(.-) in PS I treated with dithionite at high pH. ENDOR resonances of the proton in a H bond were detected and an estimate of the strength and geometry of this bond to A(1)(.-) was obtained. The significance of the hydrogen bond and other (hydrophobic) interactions of A(1) with the surrounding are briefly discussed.
A tetrahelical DNA fold adopted by tandem repeats of alternating GGG and GCG tracts
DNA can form diverse higher-order structures, whose details are greatly dependent on nucleotide sequence. G-rich sequences containing four or more repeats of three guanines are expected to form G-quadruplexes. Here we show that DNA sequences with GGGAGCG repeats found in the regulatory region of the PLEKHG3 gene are capable of forming tetrahelical DNA structures that are distinct from G-quadruplexes. The d(GGGAGCGAG GGAGCG) sequence, VK1, forms a dimer. Two VK1 sequences connected by an adenine residue, VK2, fold into a monomer, which shares identical structural characteristics with the VK1 fold. Their four-stranded architectures are stabilized by four G-C, four G-A and six G-G base pairs. No G-quartets or Hoogsteen-type hydrogen-bonded guanine residues are present and the overall topology is conserved in the presence of Li+, Na+, K+ and NH4+ ions. Unique structural features include two edgewise loops on each side of the structure stabilized by three G-G base pairs in N1-carbonyl symmetric geometry.
COA
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