Page 1. WT. GSK+/-. 0. 20. 40. 60 percent in < 10 cm area from wall. WT. GSK+/-. 0. 5. 10. 15. 20 mean speed (cm/sec). A. B.
WT. DKO. E10.5. E11. E11.5 E12.5 E13.5 E10.5. E11. E11.5 E12.5 E13.5. FEMALE DIMORPHIC GENES. MALE DIMORPHIC GENES. UP in. DKO. (42 ps -.
HIF-1: upstream and downstream of cancer metabolism Gregg L. Semenza, Curr Opin Genet Dev. 2010 February; 20(1):. 2. The impact of O2 availability on ...
Page 1. WT. GSK+/-. 0. 20. 40. 60 percent in < 10 cm area from wall. WT. GSK+/-. 0. 5. 10. 15. 20 mean speed (cm/sec). A. B.
Page 1. A. B. WT. WT. WT. SlARF2B-RNAi. (B1). SlARF2AB-RNAi. (AB1). SlARF2B-RNAi. (B1)
Figure S1. DNA sequence chromatograms of wt or mutant viruses. To verify the mutations introduced in to the genomes as well as to detect possible revertants ...
n.s.. 1418182_at NM_008975. Ptp4a3 protein tyrosine phosphatase 4a3. 2.0. n.s.. n.s.. 1417622_at NM_009194. Slc12a2 solute carrier family 12, member 2.
â12 â8. 0. 12. 0. 1. PIF4. A. Relative Expression Level. â12 â8. 0. 12. 0. 1. PIF4. D. Relative Expression Level. Time (ZT Hrs). â12 â8. 0. 12. 0. 1. IAA29. B. â12 â8.
University of Cincinnati, Cincinnati, OH 45221. Michael K. Lee, Pat A. Moore and Gary T. Bums. Dow Corning Corporation, Midland, MI 48686. ABSTRACT.
â12 â8. 0. 12. 0. 1. PIF4. A. Relative Expression Level. â12 â8. 0. 12. 0. 1. PIF4. D. Relative Expression Level. Time (ZT Hrs). â12 â8. 0. 12. 0. 1. IAA29. B. â12 â8.
NAME: PROFESSION: AGE: ______. HT: ______ WT: _____ kg EYES: ______ HAIR: ______ OTHR DESC: SAVE. (4d6). SKILL. BASE. ST
WT/WT. WT/HAQ TMEM173/STING. Human PBMC. 0. 20. 40. 60. 80. RQ [. hIL1B. /G. APD. H. ] p
WT. HZ. KO. 3174. 302. 4102. 256. 5290. Plpp1. ND. A. WT. HZ. KO. 5022. 253. 6174. 167. 7131. Plpp2. ND. B. WT. HZ. KO. 4155. 256. 4328. 168. 5192. 6.
Page 1. A. B. WT versus AUK2+/-. WT versus AUK2-/- CL 2. PHL. HU. MMS. UV. PHL. HU. MMS. UV. Fig.S9.
Figure S2. Representative images of H&E stained gonadal fat pads from mutant mice and control littermates on standard chow or high fat diet (HFD). Mstn-/- and ...
1 Institute of Molecular Life Sciences, University of Zurich, Zurich, Switzerland. 2 Present address: Neural Control of Movement Laboratory, Department of Health.
K. J. Beumer et al. 6 SI. WT sequence. TTGGATATCACCCGGAAACGAATCCCAATGCTCGCACCTATAGCTACTACACGAATGGC.
WT sequence TTGGATATCACCCGGAAACGAATCCCAATGCTCGCACCTATAGCTACTACACGAATGGC GTGGGAGTCACTGTGGTAGAGATCGATTGCCTGACTGGCGACCATCAGGTGCT Oligo A TTGGATATCACCCGGAAACGAATCCCAATGCTCGCACCTATTGATAATCTAGAAGTCAC TGTGGTAGAGATCGATTGCCTGACTGGCGACCATCAGGTGCT Oligo B TTGGATATCACCCGGAAACGAATCCCAATGCCCGCACCTATAGCTACTACAC_AATGGC GTGGGAGTCACTGTGGTAGAGATCGATTGCCTGACTGGCGACCATCAGGTGCT Oligo F EcoRI TTGGATATCACCCGGAAACGAATTCCAATGCCCGCACCTATAGCTACTACAC_AATGGC GTGGGAGTCACTGTGGTAGCGATCGATTGCCTGACTGGCGACCATCAGGTGCT PvuI Oligo R AGCACCTGATGGTCGCCAGTCAGGCAATCGATCGCTACCACAGTGACTCCCACGCCATT _GTGTAGTAGCTATAGGTGCGGGCATTGGAATTCGTTTCCGGGTGATATCCAA
Figure S4 Sequences of oligonucleotides used as donors. Each sequence starts at the 5’ end. The ZFN target is highlighted in bold blue type; the sequence that replaces it in Oligo A is in bold green type. The underlined space in Oligos B, F, and R shows the site of a single nucleotide deletion. The substitutions in Oligos F and R are shown in red, and the restriction enzyme recognition sites created by two of them (identified for Oligo F) are in bold type. One additional polymorphism in B, F and R is shown in red and underlined. Oligo R is the complement of Oligo F.