in Iron Carriers and
Iron Proteins (Loehr, T.M., et al., eds.), VCH
Publishers (Weinheim), pp. 239-351 (1989).
5. Shongwe, M.S., et al., Biochemistry, 31(18), 4451-
4458 (1992).
6. Bailey
Iron Carriers and Iron
Proteins, Loehr, T. M., et al., eds., VCH Publishers
(Weinheim: 1989), pp. 239-351
5. Shongwe, M.S. et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and Iron
Proteins, Loehr, T. M., et al., eds., VCH Publishers
(Weinheim: 1989), pp. 239-351.
5. Shongwe, M.S. et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and Iron
Proteins, Loehr, T. M., et al., eds., VCH Publishers
(Weinheim: 1989), pp. 239-351.
5. Shongwe, M.S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and Iron
Proteins, Loehr, T. M., et al., eds., VCH Publishers
(Weinheim: 1989), pp. 239-351
5. Shongwe, M.S. et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and Iron
Proteins, Loehr, T.M. et al., eds., VCH Publishers
(Weinheim: 1989), pp. 239-351.
5. Shongwe, M.S. et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and Iron
Proteins, Loehr, T. M., et al., eds., VCH Publishers
(Weinheim: 1989), pp. 239-351.
5. Shongwe, M.S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
Iron Carriers and
Iron Proteins, Loehr, T. M., et al., eds., VCH
Publishers (Weinheim: 1989), pp. 239-351.
5. Shongwe, M. S., et al., Anion binding by human
lactoferrin: results from crystallographic
purification of long chain
nucleic acids (> 20 kbp) by anion
exchange chromatography is
protected by EP 0 268 946 and
corresponding patents. Purchase
of the Mobius Kits does not
include a license under these
Herrera, B ., et al . FEBS Lett. 520, 93; Deveraux, Q .L . and Reed, J .C . 1999 . Genes
Dev. 13, 239; Deveraux, Q .L ., et al . 1997 . Nature 388, 300; Roy, N .
Reacts with most
mammalian species and Xenopus. ELISA, FS, IB, IC, PS
Cat. No. ST1110 100 ml € 239
Anti-Myelin Basic Protein Mouse mAb (SMI-94)
Liquid, undiluted ascites. Immunogen used was purified
purification of long chain
nucleic acids (> 20 kbp) by anion
exchange chromatography is
protected by EP 0 268 946 and
corresponding patents. Purchase of
the Mobius Kits does not include a
license under these
al. 2001. J. Biol. Chem. 276, 27058.
Smac/DIABLO, Human, Recombinant, E. coli
Amino acids 56 - 239 of human Smac/DIABLO with a carboxy terminal His•Tag® sequence was
expressed in and purified from E