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Gold Biotechnology Inc
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Proteintech
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Proteintech
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Beijing Solarbio Science
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Creative BioMart
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Gold Biotechnology Inc
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Gold Biotechnology Inc
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Boster Bio
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Cusabio
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Proteintech
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Image Search Results
Journal: Antibodies
Article Title: Two Highly Specific Mouse Monoclonal Antibodies to the Putative C-Telopeptide of Human Collagen XIα1, a Cancer Biomarker
doi: 10.3390/antib15020021
Figure Lengend Snippet: The amino acid sequence of the COL11A1 Fusion Protein (residues 1545 to 1806 of the P12107-1 A isoform), recombinantly expressed in Escherichia coli , after the removal of an N-terminal GST tag (provided by Proteintech). The first 19 N-terminal (1545) PLPILSSKKTRRHTEGMQA (1563) amino acid residues are part of the putative C-telopeptide. The next 243 amino acid residues (1564 to 1806) constitute the C-propeptide.
Article Snippet: The
Techniques: Sequencing
Journal: Antibodies
Article Title: Two Highly Specific Mouse Monoclonal Antibodies to the Putative C-Telopeptide of Human Collagen XIα1, a Cancer Biomarker
doi: 10.3390/antib15020021
Figure Lengend Snippet: SDS-PAGE gel staining and Western blot of recombinant antigens with finally purified preparations of anti-colXIα1 clone 9 and PLY-7 mAbs. Lane 1: PageRuler™ Plus Prestained Protein Ladder. Lane 2: COL11A1 Fusion Protein (Proteintech). Lane 3: Collagen XIα1 (GenScript). Lane 4: C-propeptide (GenScript). Western blot color development was monitored following the manufacturer’s instructions. Full-length blots/gels are presented in .
Article Snippet: The
Techniques: SDS Page, Staining, Western Blot, Recombinant, Purification
Journal: Antibodies
Article Title: Two Highly Specific Mouse Monoclonal Antibodies to the Putative C-Telopeptide of Human Collagen XIα1, a Cancer Biomarker
doi: 10.3390/antib15020021
Figure Lengend Snippet: The PEP-FOLD4-derived structural predictions of peptides related to the putative C-telopeptide. ( A ): The 50 N-terminal amino acid sequence of the COL11A1 Fusion Protein from Proteintech, with the first 19 N-terminal PLPILSSKKTRRHTEGMQA amino acid residues of the putative C-telopeptide. ( B ): A free RRHTEGMQA peptide. ( C ): The 50 C-terminal amino acid sequence of GenScript’s recombinant collagen XIα1 form, whose last 21 C-terminal IQPLPILSSKKTRRHTEGMQA amino acid residues correspond to the putative C-telopeptide. The peptide’s N-terminus is on the left in ( A , B ) and on the right in ( C ).
Article Snippet: The
Techniques: Derivative Assay, Sequencing, Recombinant
Journal: Cells
Article Title: Regulation of Transplanted Cell Homing by FGF1 and PDGFB after Doxorubicin Myocardial Injury
doi: 10.3390/cells10112998
Figure Lengend Snippet: Doxorubicin increases FGF-1 and PDGF-B protein levels in adult heart ventricular cells. Mice were given intraperitoneal injections of saline (S) or doxorubicin (D) and their hearts were harvested after 24 h (Day 1) or 72 h (Day 3). Using Western blotting, lysates containing equal amounts of total protein from the ventricular tissue of the differently treated animals were tested for FGF-1 and PDGF-B protein levels. When standardized against GAPDH, the level of both proteins (FGF-1 and PDGF-B) was found to be significantly higher in the Dox-treated ventricles than in the saline treated ventricles by Day 3. * p < 0.05 vs. saline (S), One-way ANOVA with Tukey’s multiple comparisons test, N = 3 independent experiments for each group.
Article Snippet: For the analysis of growth factor effects, the wells contained 1% FBS (Low Serum) DMEM and 40 ng/mL of
Techniques: Western Blot
Journal: Cells
Article Title: Regulation of Transplanted Cell Homing by FGF1 and PDGFB after Doxorubicin Myocardial Injury
doi: 10.3390/cells10112998
Figure Lengend Snippet: FGF-1 and PDGF-B increase embryonic ventricular cell migration, whereas their neutralizing antibodies decrease migration. 300 μL of 0.5 × 10 6 cells/mL serum-free cell suspensions were incubated for 22 h at 37 °C in polycarbonate membrane inserts with 8 μm pores, with surrounding wells containing 1% FBS DMEM and FGF-1, its antibody, or both ( A ) or PDGF-B, its antibody, or both ( B ). The inserts were then removed, migratory cells that had passed through the pores were washed and stained, and the cell stain was solubilized for measurement of absorbance. * p < 0.05 vs. all other groups; # p < 0.05 vs. all other groups, One-way ANOVA with Tukey’s multiple comparisons test, N = 3 independent experiments for each group.
Article Snippet: For the analysis of growth factor effects, the wells contained 1% FBS (Low Serum) DMEM and 40 ng/mL of
Techniques: Migration, Incubation, Staining
Journal: Scientific Reports
Article Title: Myeloid Cell-Specific Lipin-1 Deficiency Stimulates Endocrine Adiponectin-FGF15 Axis and Ameliorates Ethanol-Induced Liver Injury in Mice
doi: 10.1038/srep34117
Figure Lengend Snippet: Wild-type (WT) or mLipin-1KO (KO) mice were pair-fed either a control diet or an ethanol-containing diet for 10 days followed by single gavage of ethanol. ( A ) Representative Western analysis of liver Ac-NF-κB, NF-κB, p-IκBα and IκBα. ( B ) Relative liver protein levels of liver Ac-NF-κB, NF-κB, p-IκBα and IκBα. ( C ) Male C57/6J mice were treated by intraperitoneal injection 1 mg/kg mouse body weight of recombinant FGF19 for six hours. Relative adipose mRNA levels of adiponectin. Relative liver mRNA of Cyp7a1. ( D ) Male intestinal FGF15 knock out (FGF15KO) mice and LOX littermates (WT) mice were fed chow diets. Relative adipose mRNA levels of adiponectin. Relative liver mRNA levels of Cyp7a1. ( E ) Male C57/6J mice were treated by intraperitoneal injection with 0.5 μg/g mouse body weight of recombinant human globular adiponectin (gAcrp) for three days. Relative ileum FGF15. Relative liver mRNA of Cyp7a1. Results are expressed as means ± SEM (n = 4–6 mice). Means without a common letter differ, P < 0.05.
Article Snippet: 12 week old male C57BL/6J mice were treated by intraperitoneal injection with 1 mg/kg mouse body weight of
Techniques: Western Blot, Injection, Recombinant, Knock-Out