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Human fibronectin

Aota S, Nomizu M, Yamada KM (1994) The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J Biol Chem 269 24756-24761... [Pg.197]

Schwarz-Linek, U., Pilka, E. S., Pickford, A. R., Kim, J. H., Hook, M., Campbell, 1. D., and Potts, J. R. (2004). High affinity streptococcal binding to human fibronectin requires specific recognition of sequential FI modules. /. Biol. Chem. 279, 39017-39025. [Pg.157]

Leahy, D. J., Aukhil, L, and Erickson, H. P. (1996). 2.0 angstrom crystal structure of a four-domain segment of human fibronectin encompassing the RGD Loop and synergy region. Cell 84, 155-164. [Pg.59]

The mouse-mouse hybridoma CRL-1606 cell line producing IgGl monoclonal antibody (MAb) against human fibronectin was obtained from ATCC. Batch cultures... [Pg.109]

Matsuura H, Greene T, Hakomori SI. An alpha-N-acetylgalactosaminylation at the threonine residue of a defined peptide sequence creates the oncofetal peptide epitope in human fibronectin. J Biol Chem 1989 264 10472-6. [Pg.2201]

Sekiguchi, K., Siri, A., Zardi, L., and Hako-mori, S. (1985) Differences in domain structure between human fibronectins isolated from plasma and from culture supernatants of normal and transformed fibroblasts. Studies with domain-specific antibodies, J Biol Ghem 260, 5105-5114. [Pg.1294]

Human fibrinogen containing fibronectin and von Willebrand factor, purified human fibrinogen, von Willebrand factor a2-macroglobulin, and fibronectin used for preadsorption to the surfaces in this study were chosen primarily because of their increased accessibility over the canine analogs. Fibronectin is very similar in structure in all mammalian species tested so far, and all types of fibronectin have similar effects on cultured cells and cross-react with antibodies elicited in rabbits to one species of fibronectin. Thus, the use of human fibronectin is probably justified. Recent unpublished data of W. J. Dodds and G. S. Johnson suggest that washed canine platelets will not respond to human factor VIII concentrates in the ristocetin-induced platelet aggregation test. From these results, the conclusions for the von Willebrand... [Pg.344]

Kornblihtt, A.R., Umezawa, K., Vibe-Pedesen, K. and Baralle, R.E. (1985) Primary stmcture of human fibronectin differential splicing may generate at least ten polypeptides from a single gene. EMBOJ. 4 1755-1759. [Pg.62]

Lavigueur, A., La Branche, H., Komblihtt, A.R. Chabot, B. (1993), Genes Dev. 7, 2405-2417. A splicing enchancer in the human fibronectin alternate DEI exon interacts with SR proteins and stimulates U2 snRNP binding. [Pg.102]

The main charmel of the device is coated with human fibronectin at a 100 pg/ml concentration for 1 h at room temperature and rinse with HBSS bufier to remove excess fibronectin in the channels before loading cells. [Pg.30]

Figure 1. Single residue Tt-based hydrophobicity plots for bovine elastin (A) and human fibronectin (B) (see text for discussion). Part A reproduced with permission from Urry et aL (1995), Part B reproduced with permission from Urry and Luan (1995a). Figure 1. Single residue Tt-based hydrophobicity plots for bovine elastin (A) and human fibronectin (B) (see text for discussion). Part A reproduced with permission from Urry et aL (1995), Part B reproduced with permission from Urry and Luan (1995a).
C. Outgrowth from explant onto static cross-linked (GVGVP)25i coated with GRGDSP-containing human fibronectin. [Pg.387]

In some cases, after the serum exposure, the waveguide was tested against solutions of 0.1 mg/mL rahhit anti-HS A and 0.28 mg/mL rahhit anti-human fibronectin for 30 min at a temperature of 25 °C and subsequently washed for 30 min in HEPES Zl. Adsorption of human fibrinogen was tested separately by exposure teal mg/mL solution of fibrinogen for 1 h at 25 °C followed by exposure to a 0.1 mg/mL solution of rabbit antihuman fibrinogen for 30 min. [Pg.238]


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Fibronectin

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