goat anti shh (R&D Systems)
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goat anti shh
Goat Anti Shh, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+shh/Human%2FMouse+Sonic+Hedgehog%2FShh+N-Terminus+Antibody/pmc12660939-386-90-93
Average 93 stars, based on 49 article reviews
Goat Anti Shh, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/goat+anti+shh/Human%2FMouse+Sonic+Hedgehog%2FShh+N-Terminus+Antibody/pmc12660939-386-90-93
Average 93 stars, based on 49 article reviews
goat anti shh - by Bioz Stars,
2026-10
93/100 stars
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Labeling:Article Title: Convergent flow-mediated mesenchymal force drives embryonic foregut constriction and splitting Article Snippet: After three washes with the Washing Buffer, the samples were mounted in ProLong Diamond Antifade Mountant (Invitrogen, P36970) with #1 coverglass (VWR, 48393-106). .. Primary antibodies used were: rat anti-SOX2 (1:300, Invitrogen, 14-9811-82), rabbit anti-NKX2-1 (1:300, Abcam, 76013), rabbit anti-cleaved Caspase 3 (1:300, Cell Signaling Technology, 9661), rabbit anti-phospho-Histone H3 (1:300, Cell Signaling Technology, 3377), rabbit anti phospho-MLC2 (1:100, Cell Signaling Technology, 3674), rabbit anti-mCherry (1:500, Abcam, 167453, for labeling tdTomato), biotinylated Hyaluronic Acid Binding Protein (1:200, Sigma-Aldrich, 385911), goat anti-NKX6-1 (10 μg/mL, R&D Systems, AF5857), rabbit anti-TBX1 (1:50, Invitrogen, 34-9800), Article Title: Convergent flow-mediated mesenchymal force drives embryonic foregut constriction and splitting Article Snippet: After three washes with the Washing Buffer, the samples were mounted in ProLong Diamond Antifade Mountant (Invitrogen, P36970 ) with #1 coverglass (VWR, 48393-106). .. Primary antibodies used were: rat anti-SOX2 (1:300, Invitrogen, 14-9811-82), rabbit anti-NKX2-1 (1:300, Abcam, 76013), rabbit anti-cleaved Caspase 3 (1:300, Cell Signaling Technology, 9661), rabbit anti-phospho-Histone H3 (1:300, Cell Signaling Technology, 3377), rabbit anti phospho-MLC2 (1:100, Cell Signaling Technology, 3674), rabbit anti-mCherry (1:500, Abcam, 167453, for labeling tdTomato), biotinylated Hyaluronic Acid Binding Protein (1:200, Sigma-Aldrich, 385911), mouse anti-GM130 (1:150, BD Biosciences, 610822), rabbit anti-phospho-FAK (1:200, Invitrogen, 700255), goat anti-NKX6-1 (10 μg/mL, R&D Systems, AF5857), rabbit anti-TBX1 (1:50, Invitrogen, 34-9800), mouse anti-ISL1 (1:30, DSHB, 40.2D6), mouse anti-ALDH1A2 (1:50, Santa Cruz Biotechnology, sc-393204), Binding Assay:Article Title: Convergent flow-mediated mesenchymal force drives embryonic foregut constriction and splitting Article Snippet: After three washes with the Washing Buffer, the samples were mounted in ProLong Diamond Antifade Mountant (Invitrogen, P36970) with #1 coverglass (VWR, 48393-106). .. Primary antibodies used were: rat anti-SOX2 (1:300, Invitrogen, 14-9811-82), rabbit anti-NKX2-1 (1:300, Abcam, 76013), rabbit anti-cleaved Caspase 3 (1:300, Cell Signaling Technology, 9661), rabbit anti-phospho-Histone H3 (1:300, Cell Signaling Technology, 3377), rabbit anti phospho-MLC2 (1:100, Cell Signaling Technology, 3674), rabbit anti-mCherry (1:500, Abcam, 167453, for labeling tdTomato), biotinylated Hyaluronic Acid Binding Protein (1:200, Sigma-Aldrich, 385911), goat anti-NKX6-1 (10 μg/mL, R&D Systems, AF5857), rabbit anti-TBX1 (1:50, Invitrogen, 34-9800), Article Title: Convergent flow-mediated mesenchymal force drives embryonic foregut constriction and splitting Article Snippet: After three washes with the Washing Buffer, the samples were mounted in ProLong Diamond Antifade Mountant (Invitrogen, P36970 ) with #1 coverglass (VWR, 48393-106). .. Primary antibodies used were: rat anti-SOX2 (1:300, Invitrogen, 14-9811-82), rabbit anti-NKX2-1 (1:300, Abcam, 76013), rabbit anti-cleaved Caspase 3 (1:300, Cell Signaling Technology, 9661), rabbit anti-phospho-Histone H3 (1:300, Cell Signaling Technology, 3377), rabbit anti phospho-MLC2 (1:100, Cell Signaling Technology, 3674), rabbit anti-mCherry (1:500, Abcam, 167453, for labeling tdTomato), biotinylated Hyaluronic Acid Binding Protein (1:200, Sigma-Aldrich, 385911), mouse anti-GM130 (1:150, BD Biosciences, 610822), rabbit anti-phospho-FAK (1:200, Invitrogen, 700255), goat anti-NKX6-1 (10 μg/mL, R&D Systems, AF5857), rabbit anti-TBX1 (1:50, Invitrogen, 34-9800), mouse anti-ISL1 (1:30, DSHB, 40.2D6), mouse anti-ALDH1A2 (1:50, Santa Cruz Biotechnology, sc-393204), Incubation:Article Title: Airway epithelial cell differentiation relies on deficient Hedgehog signalling in COPD. Article Snippet: .. Tissue sections were then incubated with the following primary antibodies for one night at 4 °C in 3% BSA in PBS: rabbit anti-Arl13b (17711 1-ap, ProteinTech, 1:200); mouse anti-Muc5ac (NBP2-15196, Novus Biologicals, 1:100); rabbit antiMuc5B (E-AB-15988, Elabscience, 1:100); mouse anti-Acetylateda-tubulin (T6793, Sigma Aldrich, 1:1000); goat anti-P63 (AF1916, R&D systems, 1:100); rabbit anti-Gli1 (HPA065172, Sigma Aldrich, 1 mg/mL); rabbit anti-Gli2 (HPA074275, Sigma Aldrich, 0,4 mg/mL); rabbit anti-Gli3 (HPA005534, Sigma, 0,6 mg/mL); Article Title: Airway epithelial cell differentiation relies on deficient Hedgehog signalling in COPD Article Snippet: .. Tissue sections were then incubated with the following primary antibodies for one night at 4 °C in 3% BSA in PBS: rabbit anti-Arl13b (17711–1-ap, ProteinTech, 1:200); mouse anti-Muc5ac (NBP2-15196, Novus Biologicals, 1:100); rabbit anti-Muc5B (E-AB-15988, Elabscience, 1:100); mouse anti-Acetylated-α-tubulin (T6793, Sigma Aldrich, 1:1000); goat anti-P63 (AF1916, R&D systems, 1:100); rabbit anti-Gli1 (HPA065172, Sigma Aldrich, 1 μg/mL); rabbit anti-Gli2 (HPA074275, Sigma Aldrich, 0,4 μg/mL); rabbit anti-Gli3 (HPA005534, Sigma, 0,6 μg/mL); Article Title: Sonic hedgehog signalling as a potential endobronchial biomarker in COPD Article Snippet: .. Samples were rehydrated with PBS and blocked with 10% PBS-BSA for 30 min at room temperature before incubation with the following primary antibodies overnight at 4 °C in 3% PBS-BSA: rabbit anti-Arl13b (17711–1-ap, ProteinTech, 1:200); mouse anti-Muc5ac (NBP2–15196, Novus Biologicals, 1:100); mouse anti-Acetylated-α-tubulin (T6793, Sigma Aldrich, 1:1000); goat anti-p63 (AF1916, R&D systems, 1:100); rabbit anti-pancytokeratin (E-AB-33599; Clinisciences, 1:100); mouse anti-vimentin (M0725; Dako, 1:100); rabbit anti-Gli1 (HPA065172, Sigma Aldrich, 1 μg/mL); rabbit anti-Gli2 (HPA074275, Sigma Aldrich, 0,4 μg/mL); |
![Figure 2. Reverse-phase HPLC reveals the decreased hydrophobicity of ShhC released in the presence of serum or of pharmacological cholesterol <t>acceptors.</t> <t>Goat-α-Shh</t> antibodies (R&D Systems, <t>AF464)</t> were used for all blots to detect full-length unprocessed Shh (decreased electrophoretic mobility band, top) and N-truncated proteins that were solubilized from the cellular precursor (increased electrophoretic mobility band, bottom). Lower fraction numbers (fr#) indicate more hydrophilic (delipidated) proteins and higher fraction numbers indicate more lipophilic (lipidated) proteins. (A–D) RP-HPLC calibration. Consistent with its dual lipidation, R&D 8908-SH positive control proteins elute predominantly in the late fraction #37 (black arrowhead). Artificial monolipidated cellular ShhN elutes in fractions #27–29 (red arrowhead) and monolipidated cellular C25SShh (this artificial variant has the cysteine palmitate acceptor replaced with a non-accepting serine) elutes predominantly in fraction #32 (white arrowhead). Overexpressed soluble C25SShhN, another engi- neered control protein lacking both lipids, elutes in fractions #26–28 from the C4 column (green arrowhead). N-terminal Shh peptides in the schematics are labeled in orange. (E) Overexpressed cellular Shh elutes predominantly in fraction #37 (black arrowhead); a small fraction that probably did not undergo Hhat-dependent N-terminal palmitoylation elutes in fraction #33 (white arrowhead). (F) ShhC, solubilized by Disp and Scube2 from its dually lipidated cellular precursor (E), also eluted in fractions #32–34, showing that it retained the C-cholesterol moiety but not the N-palmitate after its release (white arrowhead). (G) Consistent with this, the artificially produced soluble control C25SShhC, blocked in its ability to undergo N-palmitoylation during biosynthesis, also eluted in fractions #32–34 (white arrowhead). The increased electrophoretic mobility of the protein indicated that its N-terminus was also processed. (H,I) Similar hydrophobicity of ShhC and C25SShhC was expressed in the presence of 600 µg/mL of the pharmacological cholesterol acceptor CD. Note that the electrophoretic mobility of the most soluble ShhC is again increased (lower band), consistent with proteolytic processing of the palmitoylated N-terminal peptide during Disp- and Scube2-mediated ShhC release [32,36].](https://pub-med-unpaywalled-images-cdn.bioz.com/pub_med_ids_ending_with_1456/pm38651456/pm38651456__page7_image1.jpg)
![Figure 4. A minimal N-terminal amino acid sequence contributes to Shh signaling in vitro. (A) The N-terminal Shh peptide, including the Cardin–Weintraub (CW) motif (green) is shown. A G-to-R exchange (shown in blue) just upstream of the CW site renders G32RShh susceptible to furin cleavage (inset, right lane, red arrowhead). PCSK7 cleaves the wild-type Shh peptide at the same site (inset, and red arrowhead). (B) qPCR confirmed that ShhC and C25AShhC increased the transcription of Ptch1, Gli1, and Alp1 in C3H10T1/2 cells to a similar extent. Target gene transcription was much less induced by furin- or PCSK7-cleaved proteins, indicating that processing rendered them inactive. (C) Cryo-EM derived structures (pdb: 6e1h) reveal interactions between the palmitoylated Shh N-peptide (white backbone, nitrogens stained blue, oxygens stained red, palmitate stained green) and Ptch residues (stained yellow) [22]. (D) Shh and mutant proteins lacking the N-terminal C25 to prevent palmitoylation, and their consecutively N-truncated counterparts were expressed, pulled down with heparin, and immunoblotted. All proteins were expressed at similar levels, as indicated by polyclonal α-Shh reactivity. Bottom: C3H10T1/2 osteoblast progenitor cells were incubated with similar amounts of ShhC, C25SShhC, and their truncated variants, and relative increases in Alp1 activity were determined as biological readouts. Media obtained from mock-transfected Bosc23 cells was used as a negative control, and ShhC-conditioned media as a positive control. Inhibition of ShhC](https://pub-med-unpaywalled-images-cdn.bioz.com/pub_med_ids_ending_with_1456/pm38651456/pm38651456__page11_image1.jpg)