Journal: Genes & Development

Article Title: Transcriptional derepression of negative regulators of MAP kinase supports maintenance of diapause ES cells in the pluripotent state

doi: 10.1101/gad.353143.125

Figure Lengend Snippet: The differentiation block in I-BET-resistant (I-BETR) diapause-like ES cells. ( A ) Alkaline phosphatase (AP) levels in control and I-BETR ES cells. Scale bar, 100 µm. ( B ) Expression levels of the pluripotency ( left panel) or differentiation-inducing ( right panel) genes in control, 2i-treated, or I-BETR ES cells. RNA expression levels were quantified by qPCR. Values represent normalized mean ± SD. n = 3. ( C ) Colony morphology and/or alkaline phosphatase (AP) levels in control and I-BETR ES cells following vehicle or FGF4 triggering. Scale bar, 100 µm. The bar graph represents quantification of relative percentage of pluripotent colonies in different groups. Values represent ± SD. n = 9. (n.s.) No significance, (****) P < 0.0001, one-way ANOVA with Dunnett's multiple comparisons test. ( D ) Expression levels of selected pluripotency ( left ) or differentiation-inducing ( right ) genes in control and I-BETR ES cells treated or not treated with FGF4. Error bars indicate SD. n = 3. (n.s.) No significance, (****) P < 0.0001, one-way ANOVA with Dunnett's multiple comparisons test. ( E ) Withdrawal of I-BET (I-BETW) restores the control ES cell-like pluripotency gene expression pattern in I-BETR ES cells. Values represent gene expression levels normalized to the mean of control samples based on TPM values observed by bulk mRNA RNA-seq analysis . ( F ) Generation of chimeras by I-BETR ES cells. The I-BETR ES cells were incubated in I-BET-free medium for 12–14 h and injected into the C57BL/6J blastocysts. White coat color indicates the chimerism.

Article Snippet: For FGF4-driven ES cell differentiation, 10 ng/μL recombinant FGF4 (R&D Systems 235-F4) was added on day 0 together with 1 μg/μL heparin (Sigma-Aldrich H3149).

Techniques: Blocking Assay, Control, Expressing, RNA Expression, Gene Expression, RNA Sequencing, Incubation, Injection

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 recombinant COL11A1 Fusion Protein from Proteintech was also assayed in an ELISA and Western blot with finally purified preparations of the anti-colXIα1 clone 9 and PLY-7 mAbs. shows their ELISA immunoreactivity characteristics.

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 recombinant COL11A1 Fusion Protein from Proteintech was also assayed in an ELISA and Western blot with finally purified preparations of the anti-colXIα1 clone 9 and PLY-7 mAbs. shows their ELISA immunoreactivity characteristics.

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 recombinant COL11A1 Fusion Protein from Proteintech was also assayed in an ELISA and Western blot with finally purified preparations of the anti-colXIα1 clone 9 and PLY-7 mAbs. shows their ELISA immunoreactivity characteristics.

Techniques: Derivative Assay, Sequencing, Recombinant