Journal: Archives of dermatological research

Article Title: Interactions of human tenascin-X domains with dermal extracellular matrix molecules.

doi: 10.1007/s00403-006-0706-9

Figure Lengend Snippet: Fig. 1 Binding of recombinant C-terminal 100 kDa TNX to hu- man collagen type I, III and V. a TNX binds dose dependently to human collagens type I, III and V. Binding to BSA, which served as a negative control, was absent. b Comparisons of binding of re- combinant C-terminal 100 kDa TNX and BSA to collagens type I, III, and V at the highest concentration used (10 M)

Article Snippet: Human Collagen type I from Chemicon International (Chemicon International, Temecula, CA, USA), human collagen type III and V from Rockland Inc (Tebu-bio, Heerhugowaard, NL).

Techniques: Binding Assay, Recombinant, Negative Control, Concentration Assay

Journal: Archives of dermatological research

Article Title: Interactions of human tenascin-X domains with dermal extracellular matrix molecules.

doi: 10.1007/s00403-006-0706-9

Figure Lengend Snippet: Fig. 2 Binding of recombinant C-terminal 100 kDa TNX to bo- vine collagen type I and bTE. a TNX binds dose dependently to bTE and bovine collagen type I. No binding to denatured bovine collagen type I (gelatin) was observed (the gelatin signal coin- cides with the BSA baseline signal). b Comparison of binding of recombinant C-terminal 100 kDa TNX and BSA to collagens type I, III and V at the highest concentration used (10 M)

Article Snippet: Human Collagen type I from Chemicon International (Chemicon International, Temecula, CA, USA), human collagen type III and V from Rockland Inc (Tebu-bio, Heerhugowaard, NL).

Techniques: Binding Assay, Recombinant, Comparison, Concentration Assay

Journal: Archives of dermatological research

Article Title: Interactions of human tenascin-X domains with dermal extracellular matrix molecules.

doi: 10.1007/s00403-006-0706-9

Figure Lengend Snippet: Fig. 4 Binding of TNX FNIII repeats to collagen type I, III an V. a Binding curves of recombinant TNX proteins containing FNIII29 show dose dependent binding to Wbrillar collagens as shown here for human collagen type V. b Comparison of binding of MBP–FNIII29, MBP-FNIII27–28 and MBP to collagens type I, III and V at the highest concentration used (16 M) Fig. 5 Binding of TNX FNIII repeats and FbgX domain to TE. a Recombinant TNX fragments containing FNIII29 and the FbgX domain bind dose dependently to recombinant TE. The other investigated FNIII repeats of TNX do not show signiWcant bind- ing to bTE (not shown here). MBP alone shows non-speciWc bind- ing which is signiWcantly lower than the TNX containing fusion proteins. b Comparison of binding of MBP-FNIII29, MBP– FNIII27–28, MBP–FbgX and MBP to recombinant TE at the highest concentration used (16 M)

Article Snippet: Human Collagen type I from Chemicon International (Chemicon International, Temecula, CA, USA), human collagen type III and V from Rockland Inc (Tebu-bio, Heerhugowaard, NL).

Techniques: Binding Assay, Recombinant, Comparison, Concentration Assay

Journal: Archives of dermatological research

Article Title: Interactions of human tenascin-X domains with dermal extracellular matrix molecules.

doi: 10.1007/s00403-006-0706-9

Figure Lengend Snippet: Fig. 6 Binding of FNIII29–30 to ECM proteins. Recombinant FNIII29–30 (without fusion tag) binds to collagen types I, III and V and to TE essentially in the same manner as the MBP fusion proteins containing FNIII29. BSA is used as a control for back- ground staining (7.5 g/ml)

Article Snippet: Human Collagen type I from Chemicon International (Chemicon International, Temecula, CA, USA), human collagen type III and V from Rockland Inc (Tebu-bio, Heerhugowaard, NL).

Techniques: Binding Assay, Recombinant, Control, Staining

Journal: bioRxiv

Article Title: Apical expansion of calvarial osteoblasts and suture patency is dependent on graded fibronectin cues

doi: 10.1101/2023.01.16.524278

Figure Lengend Snippet: (A) Immunofluorescence of unfolded collagen chains in E12.5 coronal sections. Immunofluorescence of collagen III (B), Laminin (C), RGB Trichrome staining for collagen (D) in E12.5 coronal sections. (E, F, G) Immunofluorescence of FN1 in coronal sections showing graded FN1 protein expression in cranial mesenchyme at E11.5-13.5. N≥3 controls; 3 mutants. (H) Schematic depicting the graded FN1 substrate towards the apex of the cranial mesenchyme. Nuclei were labeled with DAPI in blue. CHP, collagen hybridizing peptide; FN1, Fibronectin 1; fbp, frontal bone primordia. mn, meninges. Scale Bar= 100 μM.

Article Snippet: Following primary antibodies were used: Collagen hybridizing peptide (CHP) (Hwang et al., 2017; Jussila et al., 2021) (1: 250; 3Helix BIO60), rabbit anti-Fibronectin antibody (1: 250; Abcam ab2413; RRID:AB_2262874), rabbit anti-Fibulin 1 (1: 250; Abcam ab230994), rabbit anti-Collagen I (1: 250; Abcam ab270993; RRID:AB_2927551), Collagen III (Rockland Labs 1:100), rabbit anti-Laminin (1: 250; Millipore L9393), rabbit anti-Osx (1:2000 or 1:4000; Abcam ab209484; RRID:AB_2892207), rabbit anti-Caspase 3 (1: 250; Abcam ab13847; RRID:AB_443014), Goat anti-Runx 2 (1:100; R&D Systems AF2006-SP; RRID:AB_2184528) and mouse anti-GM130 (1:100; Thermo Fisher Scientific BDB610822; RRID:AB_398141).

Techniques: Immunofluorescence, Staining, Expressing, Labeling