Angiogenin Protein, Human (His)

Human angiopoietin protein is a ribonuclease that cleaves tRNA to generate stress-induced fragments, inhibits protein synthesis and triggers stress granule assembly. It binds to endothelial cell actin, undergoes endocytosis and nuclear translocation, and stimulates ribosomal RNA synthesis. Angiogenin Protein, Human (His) is the recombinant human-derived Angiogenin protein,Human, expressed by E. coli , with N-6*His labeled tag.

Angiogenin protein, a ribonuclease, demonstrates the ability to cleave tRNA within anticodon loops, producing tRNA-derived stress-induced fragments (tiRNAs). These tiRNAs play a crucial role in inhibiting protein synthesis and triggering the assembly of stress granules (SGs). Additionally, Angiogenin binds to actin on the surface of endothelial cells, and upon binding, it is endocytosed and translocated to the nucleus. In the nucleus, Angiogenin stimulates ribosomal RNA synthesis, including the initiation site sequences of 45S rRNA. Furthermore, Angiogenin exhibits angiogenic activity, promoting vascularization in both normal and malignant tissues. This angiogenic function is intricately regulated by its interaction with RNH1 in vivo. Structurally, Angiogenin forms homodimers and interacts with RNH1 to create tight 1:1 complexes, with the possibility of dimerization involving two such complexes.

Human

E. coli

N-6*His

P03950 (D26-P147)

283  [NCBI]

DNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP

18.0 kDa

Greater than 90 % as determined by SDS-PAGE.

<1 EU/ug, determined by LAL method.