Anti-MMP13 antibody

• WB

Unknown

Western blot - Anti-MMP13 antibody (AB39012)

The loading amount is 15 ul/lane, and the condrosarcoma media was concentrated 40x.

All lanes:

Western blot - Anti-MMP13 antibody (ab39012) at 1/3000 dilution

Lane 1:

cell media from human chondrosarcoma (untreated).

Lane 2:

cell media from human chondrosarcoma (IL1 beta treated).

Predicted band size: 54 kDa

Observed band size: 60 kDa

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• sELISA

Unknown

Sandwich ELISA - Anti-MMP13 antibody (AB39012)

Standard curve for MMP13; dilution range 1pg/ml to 1μg/ml using Capture Antibody Mouse monoclonal [181-15A12] to MMP13 (ab77949) at 1μg/ml and Detector Antibody Rabbit polyclonal to MMP13 - Hinge region (ab39012) at 0.5μg/ml.

• IHC-Fr

CiteAb

Immunohistochemistry (Frozen sections) - Anti-MMP13 antibody (AB39012)

MMP13 immunohistochemistry-immunofluorescence using Anti-MMP13 antibody ab39012. Publication image and figure legend from Patil, P., Dong, Q., et al., 2019, Aging Cell, Pubmed 30900385.

Effects of GCV treatment on aggrecan and MMP13 mRNA and protein levels in intervertebral discs of p16-3MR mice. Aggrecan mRNA levels were quantified by qRT-PCR (a), and protein was quantified by immunofluorescence signals (b) in nucleus pulposus and annulus fibrosus section of disc tissue. MMP13 expression of whole disc mRNA by qRT-PCR (c) and protein by immunofluorescence (d) in inner nucleus pulposus and outer annulus fibrosus section of disc tissue. Graphs on the right are quantification of the immunofluorescence results. Data shown are mean ± SEM of four independent experiments (4 mice), *p < < 0.05, ***p < < 0.001. Scale bar = 10 μm

• IHC-Fr

CiteAb

Immunohistochemistry (Frozen sections) - Anti-MMP13 antibody (AB39012)

MMP13 immunohistochemistry-immunofluorescence using Anti-MMP13 antibody ab39012. Publication image and figure legend from Jafari, L., Savard, M., et al., 2019, Biomed Eng Online, Pubmed 31068196.

immunohistochemistry analysis of MMP-13. a Representative epifluorescence micrographs of freshly isolated and SD tendons stained for MMP-13 protein using the rabbit polyclonal anti-MMP-13 antibody ab39012. Scale bar = 200 μm. b Bar graph illustrating semiquantitative MMP-13 immunofluorescent intensity in freshly isolated tendons and SD tendons. Inset : consolidation of increased MMP-13 in one tendon sample by PCR analysis. *p < < 0.050 versus control fresh tendons

• WB

CiteAb

Western blot - Anti-MMP13 antibody (AB39012)

Western Blotting using Anti-MMP13 antibody, ab39012. Publication image from Wang, H. et al., 2016, Nat Commun, 27039827. Legend direct from paper.

Inhibition of mTORC1 prevents chondrocyte proliferation while promoting differentiation.(a) CCK8 proliferation assay of chondrocytes cultured in normal growth medium or with 1, 10 or 50 nM rapamycin treatment. OD450values were converted to cell numbers. One-way analysis of variance (ANOVA) and Dunnett's multiple comparison test; NS, not significant, *P<0.05, n=5; Error bars indicate s.d. (b) qPCR and western blot analysis of primary chondrocytes cultured in growth medium or ITS medium. Cells were treated with or without rapamycin from day 6 and were harvested on day 14 after confluence. One-way ANOVA and Dunnett's multiple comparison test, *P<0.05, n≥3; Error bars indicate s.d. (c) HE staining, pS6 immunofluorescence and MMP-13 in situ mRNA analysis of Tibia sections of mice at P0 whose maternal mice receiving a daily intraperitoneal injection of rapamycin (1.5 mg kg−1 per day) or 0.9% saline for 3 days before sacrifice. Scale bar, 100 µm. PZ, proliferative chondrocyte zone; HZ, hypertrophic chondrocyte zone. (d) Quantification of Tibia PZ and HZ length in P0 mice receiving rapamycin. Student's t-test, *P<0.05, n≥3; Error bars indicate s.d. (e) Western blot of pure cartilage tissues harvested from long bone mice receiving rapamycin.

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• WB

CiteAb

Western blot - Anti-MMP13 antibody (AB39012)

MMP13 western blotting using Anti-MMP13 antibody ab39012. Publication image and figure legend from Chen, Z., Lin, C. X., et al., 2020, Cell Death Dis, Pubmed 32632306.

Spermidine treatment inhibits TNF-a induced arthritis (TIA).a immunohistochemistry was used to assess the expression of TNF-α in synovial tissue of the knee joint after 4, 8, and 16 weeks of spermidine treatment to TNF-a induced arthritis mice. b TNF-α score was calculated based on IHC staining. c, d Western blot analysis of the expression of iNOS, MMP-3, MMP-13, and Adamts4 in FLS. e qRT-PCR analysis of the expression of IL-6, MMP-3, and MMP-13 in FLS. Data are shown as mean ± SD, n = 10, *p < < 0.05, **p < < 0.01, ***p < < 0.001, scale bar, 200 µm.

false

• WB

CiteAb

Western blot - Anti-MMP13 antibody (AB39012)

MMP13 western blotting using Anti-MMP13 antibody ab39012. Publication image and figure legend from Sun, K., Guo, Z., et al., 2023, Cell Death Discov, Pubmed 37002200.

The protective effects of ICCB-19 on chondrocytes.After a pre-treatment of ICCB-19 for 2 h, chondrocytes were stimulated by TNF-α for 24 h. A, B the protein expression of iNOS, COX2, COL2A1, and MMP13 were examined. C The semi-quantitative analysis of protein expression. D The apoptotic chondrocytes were stained by Annexin V-FITC /PI and analyzed by flow cytometry. The average apoptotic rates were shown in (E). F The apoptotic chondrocytes were labeled by TUNEL staining, scale bar : 50 μm. G After the indicated treatment, the phosphorylation of RIPK1, RIPK3, and MLKL as well as protein expression of these three markers were detected by western blot. H The semi-quantitative analysis of protein expression. I After the induction of necroptosis, the supernatant containing TNF-α and z-VAD was replaced by refresh culture medium. 24 h later, the culture medium was transferred to untreated primary chondrocytes and culture for 24 h. The protein expression of MMP13 and phosphorylation of MLKL were examined. J The semi-quantitative analysis of protein expression. Data are expressed as means ± SD. *p < < 0.05, **p < < 0.01. NS not significant. z-VAD, Z-VAD-FMK. P-, Phosphorylated-.

false

• WB

CiteAb

Western blot - Anti-MMP13 antibody (AB39012)

MMP13 western blotting using Anti-MMP13 antibody ab39012. Publication image and figure legend from Li, Y., Sun, B., et al., 2017, J Cell Mol Med, Pubmed 28766880.

Transfection of cells with MMP-13 and treatment with MMP-13 Ln-5 cleavage fragments disrupted VM formation ( *p < < 0.05). (A) MMP-13 expression was successfully regulated by transfection plasmids. In H460 cells, MMP-13 was up-regulated by transfection with pcDNA-MMP-13 plasmids, and in H661 cells, MMP-13 was down-regulated by transfection with MMP-13-siRNA plasmids. Transfection efficiency was confirmed via WB. MMP-2 was highly expressed in both cell lines (B) Transfection of H460 cells with pcDNA-MMP-13 abrogated the capillary-like tube formation ability on Matrigel. However, knockdown of MMP-13 expression in H661 cells induced typical tube formation. (C) Exogenous addition of recombinant human MMP-13 proteins in the 3D culture medium resulted in the inability of H460 and H661 cells to form capillary-like tubes. In contrast, the exogenous addition of recombinant human MMP-2 proteins induced the cells to form more typical capillary-like tubes on the Matrigel. Exogenous addition of recombinant human Ln-5 protein induced the H460 cells to form more typical capillary-like tubes but not in H661 cells that overexpressed MMP-13. (D) Exogenous addition of Ln-5 cleaved by MMP-13 in the 3D culture medium resulted in the inability of H460 and H661 cells to form capillary-like tubes. In contrast, the exogenous addition of the MMP-2 Ln-5 cleavage products induced the cells to form more typical capillary-like tubes. The addition of all three of these proteins also suppressed tube formation (Bar = 100 μm).

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