High-purity recombinant osteopontin N-terminal domain
نویسندگان
چکیده
منابع مشابه
N-Terminal Domain
Annexin I is a member of a multigene family of Ca2+ /phospholipid-binding proteins and a major substrate for the epidermal growth factor (EGF) receptor kinase, which has been implicated in membrane-related events along the endocytotic pathway, in particular in the sorting of internalized EGF receptors occurring in the multivesicular body. We analyzed in detail the intracellular distribution of ...
متن کاملN-Terminal Domain of Fragile Histidine Triad Exerts Potent Cytotoxic Effect in HT1080 Cells
Fragile histidine triad (FHIT) serves a critical function as a tumor suppressor that inhibits p53 degradation by mouse double minute 2 (MDM2). The functional domains of FHIT involved in tumor inhibition was interpreted. In-silico screening data were employed to construct truncated forms of FHIT to assess their cytotoxic effects on the HT1080 cell line. Full FHIT expression was confirmed by west...
متن کاملN-Terminal Domain of Fragile Histidine Triad Exerts Potent Cytotoxic Effect in HT1080 Cells
Fragile histidine triad (FHIT) serves a critical function as a tumor suppressor that inhibits p53 degradation by mouse double minute 2 (MDM2). The functional domains of FHIT involved in tumor inhibition was interpreted. In-silico screening data were employed to construct truncated forms of FHIT to assess their cytotoxic effects on the HT1080 cell line. Full FHIT expression was confirmed by west...
متن کاملRecombinant clotting factor VIII concentrates: Heterogeneity and high-purity evaluation.
Factor VIII is an important glycoprotein involved in hemostasis. Insertion of expression vectors containing either the full-length cDNA sequence of human factor VIII (FLrFVIII) or B-domain deleted (BDDrFVIII) into mammalian cell lines results in the production of recombinant factor VIII (rFVIII) for therapeutic usage. Three commercially available rFVIII concentrates (Advate, Helixate NexGen and...
متن کاملRimJ-mediated context-dependent N-terminal acetylation of the recombinant Z-domain protein in Escherichia coli.
N-terminal acetylation of the recombinant Z-domain protein depends on E. coli strains, expression vectors and amino acid residues near the N-terminus, and is enhanced by a high cellular level of RimJ.
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Biochimica et Biophysica Sinica
سال: 2015
ISSN: 1672-9145,1745-7270
DOI: 10.1093/abbs/gmv068