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

Journal: Regenerative Therapy

Article Title: Extracellular vesicles derived from adipose-derived mesenchymal stem/stromal cells prevent synovial inflammation and attenuate cartilage degeneration in rodent osteoarthritis

doi: 10.1016/j.reth.2025.101056

Figure Lengend Snippet: Differential gene expression besed on Single-cell RNA sequencing of joint cell clusters following extracellular vesicle (EVs) treatment . ( a-d ) Comparison of gene expression in EVs, PBS, and WT groups (a) in Cluster 6 (chondrocyte progenitors) (COL2A1, COL1A2, PRG4, MMP3, CCL2, and FGF18). ( b ) in Cluster 1 (NK cells) (CD14, MRC1, CD163, CD86, CD80, and NOS2). ( c ) in Cluster 8 (Mesenchymal cells) (COL2A1, COL1A2, PRG4, CCL2, and FGF18) ( d ) in Cluster 4 (Neutrophils) (APOE, AGPAT4, HAPLN1, CDKN1C, MET, and CEMIP2). (e) Flow cytometry analysis confirmed that the proportion of CD11b + CD163 + M2 macrophages was approximately 2.5-fold higher in the EVs-treated group compared to the PBS-treated group.

Article Snippet: After 24 h of stimulation, the supernatant was collected and the amount of Fibroblast Growth Factor 18 (FGF18) protein in the supernatant was measured using Human FGF18 ELISA set (Elabscience Biotechnology Inc.).

Techniques: Gene Expression, RNA Sequencing, Comparison, Flow Cytometry