Journal: Frontiers in Pediatrics

Article Title: Prevalence of osteopathologies in a single center cohort of survivors of childhood primary brain tumor

doi: 10.3389/fped.2022.913343

Figure Lengend Snippet: Descriptive statistics of the cohort and parameters of bone health.

Article Snippet: Plasma levels of osteoprotegerin (pmol/l), receptor activator of nuclear factor kappa-B ligand (RANKL, pmol/l), and tartrate-resistant acid phosphatase 5b (TRAP5b, U/l) were measured using commercially available ELISA assays, according to the manufacturer’s instructions (Osteoprotegerin: OPG, Quidel ® ; RANKL: sRANKL, BIOMEDICA and TRAP 5b: TRAP5b, Quidel ® ; all TECOmedical, Germany).

Techniques:

Journal: Biomaterials

Article Title: Local pulsatile PTH delivery regenerates bone defect via enhanced bone remodeling in a cell-free scaffold

doi: 10.1016/j.biomaterials.2016.10.049

Figure Lengend Snippet: Analysis of the systemic effects of PTH release from the local delivery devices. (A) Representative μCT reconstructions of the tibiae from different treatment groups; (B) Trabecular bone volume; (C) Serum P1NP level and (D) TRAP5b level measured using ELISA kits. n=6~9 per group, *P<0.05, **P<0.005, #P<0.05, ##P<0.005, ###P<0.001.

Article Snippet: Serum procollagen I N-terminal propeptide (P1NP) (MyBioSource, Inc) and TRAP5b (Novatein Biosciences, MA) ELISA immunoassays were performed following the manufacturer’s protocols.

Techniques: Enzyme-linked Immunosorbent Assay

Journal: International Journal of Molecular Sciences

Article Title: Identification and Functional Analysis of Tartrate-Resistant Acid Phosphatase Type 5b (TRAP5b) in Oreochromis niloticus

doi: 10.3390/ijms24087179

Figure Lengend Snippet: Structure and sequence analysis of TRAP5b from Nile tilapia. ( A ) The nucleotide and deduced amino acid sequences of OnTRAP5b. The signal peptide is marked in a gray shadow. The metallophosphatase domain is marked with a single underline. The translation start (ATG) and stop (TGA) codons are boxed. ( B , C ) Alignment of the predicted amino acid sequences of OnTRAP5b homologs and predicted conserved domains of OnTRAP5b. Symbol (●) represents metal binding sites, and active sites are in red boxed. Symbol (▲) represents the N-glycosylation site. The numbers indicate the sequence identities between OnTRAP5b and the compared sequences. The conserved and identical residues are represented by black shading, and the residues that are ≥75% identical among the aligned are in gray. ( D ) Phylogenetic tree analysis of OnTRAP5b among other vertebrates. A neighbor-joining phylogenetic tree of TRAP5 proteins based on protein sequence analyzed with mega 6.0. The degree of confidence in each branch point was determined by bootstrap analysis (1000 times). ( E ) The predicted three-dimensional structure of protein TRAP5b from Oreochromis niloticus ( left ), Homo sapiens ( middle ), and overlapped three-dimensional structure of TRAP5 from them ( right ).

Article Snippet: Phylogenetic analysis revealed that TRAP5 has two major branches, TRAP5a and TRAP5b, and OnTRAP5b belongs to the member of the fish TRAP5b group and is closely related to TRAP5 of Haplochromis burtoni , Pundamilia nyererei , Simochromis diagramma and M. zebra ( D).

Techniques: Sequencing, Binding Assay, Glycoproteomics