collagenase ii Search Results


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  • 93
    Santa Cruz Biotechnology collagenase cls type ii
    Collagenase Cls Type Ii, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/collagenase cls type ii/product/Santa Cruz Biotechnology
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    96
    Proteintech mmp2
    Mmp2, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mmp2/product/Proteintech
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    96
    Proteintech rabbit anti mmp2
    Triptolide (TPL) inhibition of the polarization induction of M2-type macrophages may be accomplished by inhibiting the PI3K/AKT/NF-κB pathway. (A) Images of tumors in the M, DDP, TPL, and DDP + TPL groups on day 15. (B) Weights (n = 3) of tumors in different treatment groups. (C) Kaplan–Meier survival curves of model mice bearing ovarian cancer after the intraperitoneal administration of TPL or DDP (n = 5). (D) Representative immunohistochemical expression of CD206 and CD31 in tumor tissues of different treatment groups. (E, F) Relative expression of MMP9, <t>MMP2,</t> VEGF, p-PI3K, PI3K, p-AKT, p-p65, AKT, and p65 in tumor tissues. *P < 0.05, **P < 0.01.
    Rabbit Anti Mmp2, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Proteintech mmp9
    Effects of PHLPP1 on myocardial apoptosis and fibrosis. A, Immunostaining of PHLPP1 (first row, n = 6) and cell apoptosis as determined by TUNEL assay (second‐fourth row, n = 5): apoptosis cell stained red; nuclei stained blue with DAPI. B, Cell apoptosis rate determined by TUNEL assay. C, The levels of cleaved caspase‐3 following PHLPP1 inhibition were measured by Western blot (n = 6). D, The levels of Bax and Bcl‐2 following PHLPP1 inhibition were measured by Western blot (n = 6). E, Representative Masson's trichrome staining (first row) and Sirius red staining (second and third rows) of the myocardium (n = 6). Immunostaining of collagen I (fourth row) and collagen III (fifth row) (n = 6). F, Quantification of Masson's trichrome staining (n = 6). G, Quantification of Sirius red staining (n = 6). H‐K, Western blot analysis of the protein expression of collagen I (F), collagen III (G), MMP2 (H) and <t>MMP9</t> (I) (n = 6). Control: normal rats. DM: diabetes mellitus. shN.C: negative control shRNA. shPHLPP1: PHLPP1 shRNA. All experiments were performed at least 3 times. Data are expressed as the means ± SD. Statistical analysis was performed using one‐way ANOVA followed by Bonferroni's post hoc test. * P < .05 compared with control, and # P < .05 compared with DM or shN.C in DM
    Mmp9, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Proteintech mmp2 proteintech 10373 2 ap
    Primary antibodies used in this study
    Mmp2 Proteintech 10373 2 Ap, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Triptolide (TPL) inhibition of the polarization induction of M2-type macrophages may be accomplished by inhibiting the PI3K/AKT/NF-κB pathway. (A) Images of tumors in the M, DDP, TPL, and DDP + TPL groups on day 15. (B) Weights (n = 3) of tumors in different treatment groups. (C) Kaplan–Meier survival curves of model mice bearing ovarian cancer after the intraperitoneal administration of TPL or DDP (n = 5). (D) Representative immunohistochemical expression of CD206 and CD31 in tumor tissues of different treatment groups. (E, F) Relative expression of MMP9, MMP2, VEGF, p-PI3K, PI3K, p-AKT, p-p65, AKT, and p65 in tumor tissues. *P < 0.05, **P < 0.01.

    Journal: Frontiers in Oncology

    Article Title: TPL Inhibits the Invasion and Migration of Drug-Resistant Ovarian Cancer by Targeting the PI3K/AKT/NF-κB-Signaling Pathway to Inhibit the Polarization of M2 TAMs

    doi: 10.3389/fonc.2021.704001

    Figure Lengend Snippet: Triptolide (TPL) inhibition of the polarization induction of M2-type macrophages may be accomplished by inhibiting the PI3K/AKT/NF-κB pathway. (A) Images of tumors in the M, DDP, TPL, and DDP + TPL groups on day 15. (B) Weights (n = 3) of tumors in different treatment groups. (C) Kaplan–Meier survival curves of model mice bearing ovarian cancer after the intraperitoneal administration of TPL or DDP (n = 5). (D) Representative immunohistochemical expression of CD206 and CD31 in tumor tissues of different treatment groups. (E, F) Relative expression of MMP9, MMP2, VEGF, p-PI3K, PI3K, p-AKT, p-p65, AKT, and p65 in tumor tissues. *P < 0.05, **P < 0.01.

    Article Snippet: The PVDF membranes were incubated with rabbit anti-MMP2 (1:1000; Proteintech, Cat. no.: 10373-2-AP), rabbit anti-Arg-1 (1:1000; CST, Cat. no.: 93668T), rabbit anti-MMP9 (1:1000; Proteintech, Cat. no.: 10375-2-AP), rabbit anti-VEGF (1:1000; Proteintech, Cat. no.: 19003-1-AP), rabbit anti-p65 (1:1000; Proteintech, Cat. no.: 10745-1-AP), rabbit anti-p-p65 (1:1000; CST, Cat. no.: 3033S), anti-AKT (1:1000; Proteintech, Cat. no.: 10176-2-AP), mouse anti-p-AKT (1:1000; Proteintech, Cat. no.: 66444-1-Ig), and mouse anti-β-actin (1:5000; Proteintech, Cat. no.: 60008-1-Ig) primary antibodies overnight at 4°C after blocking with 5% skim milk.

    Techniques: Inhibition, Immunohistochemical staining, Expressing

    Effects of PHLPP1 on myocardial apoptosis and fibrosis. A, Immunostaining of PHLPP1 (first row, n = 6) and cell apoptosis as determined by TUNEL assay (second‐fourth row, n = 5): apoptosis cell stained red; nuclei stained blue with DAPI. B, Cell apoptosis rate determined by TUNEL assay. C, The levels of cleaved caspase‐3 following PHLPP1 inhibition were measured by Western blot (n = 6). D, The levels of Bax and Bcl‐2 following PHLPP1 inhibition were measured by Western blot (n = 6). E, Representative Masson's trichrome staining (first row) and Sirius red staining (second and third rows) of the myocardium (n = 6). Immunostaining of collagen I (fourth row) and collagen III (fifth row) (n = 6). F, Quantification of Masson's trichrome staining (n = 6). G, Quantification of Sirius red staining (n = 6). H‐K, Western blot analysis of the protein expression of collagen I (F), collagen III (G), MMP2 (H) and MMP9 (I) (n = 6). Control: normal rats. DM: diabetes mellitus. shN.C: negative control shRNA. shPHLPP1: PHLPP1 shRNA. All experiments were performed at least 3 times. Data are expressed as the means ± SD. Statistical analysis was performed using one‐way ANOVA followed by Bonferroni's post hoc test. * P < .05 compared with control, and # P < .05 compared with DM or shN.C in DM

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Inhibition of PHLPP1 ameliorates cardiac dysfunction via activation of the PI3K/Akt/mTOR signalling pathway in diabetic cardiomyopathy

    doi: 10.1111/jcmm.15123

    Figure Lengend Snippet: Effects of PHLPP1 on myocardial apoptosis and fibrosis. A, Immunostaining of PHLPP1 (first row, n = 6) and cell apoptosis as determined by TUNEL assay (second‐fourth row, n = 5): apoptosis cell stained red; nuclei stained blue with DAPI. B, Cell apoptosis rate determined by TUNEL assay. C, The levels of cleaved caspase‐3 following PHLPP1 inhibition were measured by Western blot (n = 6). D, The levels of Bax and Bcl‐2 following PHLPP1 inhibition were measured by Western blot (n = 6). E, Representative Masson's trichrome staining (first row) and Sirius red staining (second and third rows) of the myocardium (n = 6). Immunostaining of collagen I (fourth row) and collagen III (fifth row) (n = 6). F, Quantification of Masson's trichrome staining (n = 6). G, Quantification of Sirius red staining (n = 6). H‐K, Western blot analysis of the protein expression of collagen I (F), collagen III (G), MMP2 (H) and MMP9 (I) (n = 6). Control: normal rats. DM: diabetes mellitus. shN.C: negative control shRNA. shPHLPP1: PHLPP1 shRNA. All experiments were performed at least 3 times. Data are expressed as the means ± SD. Statistical analysis was performed using one‐way ANOVA followed by Bonferroni's post hoc test. * P < .05 compared with control, and # P < .05 compared with DM or shN.C in DM

    Article Snippet: The membranes were blocked in 5% non‐fat milk for 90 minutes at room temperature and then incubated at 4°C with specific primary antibodies against GAPDH (Abways, P04406), PHLPP1 (Proteintech, 22789‐1‐AP), collagenI (novusbio, NBP1‐30054), collagenIII (novusbio, NB600‐594SS), MMP2 (Proteintech, 10373‐2‐AP), MMP9 (Proteintech, 10387‐2‐AP), cleaved caspase‐3, Bcl2‐associated X protein (Bax) (CST, 2772), B‐cell lymphoma/leukaemia‐2 (Bcl‐2) (Affinity, AF6139), p‐PI3K (CST, 4228), p‐Akt (abcam, ab38449), p‐mTOR (abcam, ab109268), PI3K (CST, 4292), Akt (abcam, ab179463) and mTOR (abcam, ab134903) for detection.

    Techniques: Immunostaining, TUNEL Assay, Staining, Inhibition, Western Blot, Expressing, Negative Control, shRNA

    Primary antibodies used in this study

    Journal: Annals of Translational Medicine

    Article Title: Kiaa0101 serves as a prognostic marker and promotes invasion by regulating p38/snail1 pathway in glioma

    doi: 10.21037/atm-20-3219

    Figure Lengend Snippet: Primary antibodies used in this study

    Article Snippet: The contents were then incubated with secondary antibody (Lincoln, NE, USA; 1:10,000) in darkness for 1 h. The experiment was performed in triplicate. table ft1 table-wrap mode="anchored" t5 caption a7 Primary antibody Supplier Catalog number Dilution GAPDH Proteintech 60004-1-Ig 1:5,000 Kiaa0101 Sigma WH0009768M1 1:1,000 MMP2 Proteintech 10373-2-AP 1:1,000 Snail1 Proteintech 13099-1-AP 1:1,000 Vimentin Proteintech 10366-1-AP 1:1,000 E-cadherin Abcam ab15148 1:500 P38 Cell signaling technology 9212S 1:1,000 p-p38 (Thr180/Tyr182) Cell signaling technology 4511S 1:1,000 ERK Cell signaling technology 4695S 1:1,000 (p44/42) p-ERK1/2 Cell signaling technology 9101S 1:1,000 JNK Abcam ab179461 1:1,000 P-SAPK/JNK (Tyr185) Sigma SAB4504450 1:1,000 Open in a separate window caption a8 Primary antibodies used in this study Construction and transfection with shRNA and plasmid Oligonucleotides encoding shRNA targeted Kiaa0101 and a scrambled shRNA were purchased from Genechem Co., Ltd (Shanghai, China).

    Techniques:

    Kiaa0101 induced invasion and upregulated expression of Snail1. (A) Spearman correlation was used to analysis the relationship between Kiaa0101 and Snail1, Vimentin and MMP2. Western blot was performed to investigate the expression of snail1 after inhibiting (B,C) and forcing (B,D) the expression of Kiaa0101 in U251 and U87 cells. GAPDH as loading control. (E) Representative fluorescent images of Kiaa0101 (green) and snail1 (red) staining in U87 cells. Nuclei were stained with DAPI. Scan bar 10 µm. (F) Representative images of IHC staining of Kiaa0101 and Snail1 in glioma and (G) Chi-square test was used for statistical analysis. *, P<0.05.

    Journal: Annals of Translational Medicine

    Article Title: Kiaa0101 serves as a prognostic marker and promotes invasion by regulating p38/snail1 pathway in glioma

    doi: 10.21037/atm-20-3219

    Figure Lengend Snippet: Kiaa0101 induced invasion and upregulated expression of Snail1. (A) Spearman correlation was used to analysis the relationship between Kiaa0101 and Snail1, Vimentin and MMP2. Western blot was performed to investigate the expression of snail1 after inhibiting (B,C) and forcing (B,D) the expression of Kiaa0101 in U251 and U87 cells. GAPDH as loading control. (E) Representative fluorescent images of Kiaa0101 (green) and snail1 (red) staining in U87 cells. Nuclei were stained with DAPI. Scan bar 10 µm. (F) Representative images of IHC staining of Kiaa0101 and Snail1 in glioma and (G) Chi-square test was used for statistical analysis. *, P<0.05.

    Article Snippet: The contents were then incubated with secondary antibody (Lincoln, NE, USA; 1:10,000) in darkness for 1 h. The experiment was performed in triplicate. table ft1 table-wrap mode="anchored" t5 caption a7 Primary antibody Supplier Catalog number Dilution GAPDH Proteintech 60004-1-Ig 1:5,000 Kiaa0101 Sigma WH0009768M1 1:1,000 MMP2 Proteintech 10373-2-AP 1:1,000 Snail1 Proteintech 13099-1-AP 1:1,000 Vimentin Proteintech 10366-1-AP 1:1,000 E-cadherin Abcam ab15148 1:500 P38 Cell signaling technology 9212S 1:1,000 p-p38 (Thr180/Tyr182) Cell signaling technology 4511S 1:1,000 ERK Cell signaling technology 4695S 1:1,000 (p44/42) p-ERK1/2 Cell signaling technology 9101S 1:1,000 JNK Abcam ab179461 1:1,000 P-SAPK/JNK (Tyr185) Sigma SAB4504450 1:1,000 Open in a separate window caption a8 Primary antibodies used in this study Construction and transfection with shRNA and plasmid Oligonucleotides encoding shRNA targeted Kiaa0101 and a scrambled shRNA were purchased from Genechem Co., Ltd (Shanghai, China).

    Techniques: Expressing, Western Blot, Staining, Immunohistochemistry

    Kiaa0101 enhanced invasion through Snail1. (A) Cells co-transfected with Kiaa0101 plasmid and si-Snail1, then wound healing and transwell were employed to investigate snail1-mediated invasion of U251 (A,B) and U87 (C,D) cells, respectively. A&C, Original magnification ×200. (E,F) Western blot was performed to investigate the expression of snail1, mmp2 and Vimentin. (G) Representative fluorescent images of snail1 in U251 cells. Scan bar 10 µm. *, P<0.05.

    Journal: Annals of Translational Medicine

    Article Title: Kiaa0101 serves as a prognostic marker and promotes invasion by regulating p38/snail1 pathway in glioma

    doi: 10.21037/atm-20-3219

    Figure Lengend Snippet: Kiaa0101 enhanced invasion through Snail1. (A) Cells co-transfected with Kiaa0101 plasmid and si-Snail1, then wound healing and transwell were employed to investigate snail1-mediated invasion of U251 (A,B) and U87 (C,D) cells, respectively. A&C, Original magnification ×200. (E,F) Western blot was performed to investigate the expression of snail1, mmp2 and Vimentin. (G) Representative fluorescent images of snail1 in U251 cells. Scan bar 10 µm. *, P<0.05.

    Article Snippet: The contents were then incubated with secondary antibody (Lincoln, NE, USA; 1:10,000) in darkness for 1 h. The experiment was performed in triplicate. table ft1 table-wrap mode="anchored" t5 caption a7 Primary antibody Supplier Catalog number Dilution GAPDH Proteintech 60004-1-Ig 1:5,000 Kiaa0101 Sigma WH0009768M1 1:1,000 MMP2 Proteintech 10373-2-AP 1:1,000 Snail1 Proteintech 13099-1-AP 1:1,000 Vimentin Proteintech 10366-1-AP 1:1,000 E-cadherin Abcam ab15148 1:500 P38 Cell signaling technology 9212S 1:1,000 p-p38 (Thr180/Tyr182) Cell signaling technology 4511S 1:1,000 ERK Cell signaling technology 4695S 1:1,000 (p44/42) p-ERK1/2 Cell signaling technology 9101S 1:1,000 JNK Abcam ab179461 1:1,000 P-SAPK/JNK (Tyr185) Sigma SAB4504450 1:1,000 Open in a separate window caption a8 Primary antibodies used in this study Construction and transfection with shRNA and plasmid Oligonucleotides encoding shRNA targeted Kiaa0101 and a scrambled shRNA were purchased from Genechem Co., Ltd (Shanghai, China).

    Techniques: Transfection, Plasmid Preparation, Western Blot, Expressing

    Kiaa0101 slicing suppressed the malignancy of glioma in vivo. (A) Images of the xenograft tumors formed in nude mice injected with sh-Kiaa0101 cells and control cells. (B,C) Tumor volume and tumor weight were calculated. (D) Representative images of IHC staining of Kiaa0101, snail1, mmp2, vimentin and p-p38. Scan bar 50 µm. *, P<0.05.

    Journal: Annals of Translational Medicine

    Article Title: Kiaa0101 serves as a prognostic marker and promotes invasion by regulating p38/snail1 pathway in glioma

    doi: 10.21037/atm-20-3219

    Figure Lengend Snippet: Kiaa0101 slicing suppressed the malignancy of glioma in vivo. (A) Images of the xenograft tumors formed in nude mice injected with sh-Kiaa0101 cells and control cells. (B,C) Tumor volume and tumor weight were calculated. (D) Representative images of IHC staining of Kiaa0101, snail1, mmp2, vimentin and p-p38. Scan bar 50 µm. *, P<0.05.

    Article Snippet: The contents were then incubated with secondary antibody (Lincoln, NE, USA; 1:10,000) in darkness for 1 h. The experiment was performed in triplicate. table ft1 table-wrap mode="anchored" t5 caption a7 Primary antibody Supplier Catalog number Dilution GAPDH Proteintech 60004-1-Ig 1:5,000 Kiaa0101 Sigma WH0009768M1 1:1,000 MMP2 Proteintech 10373-2-AP 1:1,000 Snail1 Proteintech 13099-1-AP 1:1,000 Vimentin Proteintech 10366-1-AP 1:1,000 E-cadherin Abcam ab15148 1:500 P38 Cell signaling technology 9212S 1:1,000 p-p38 (Thr180/Tyr182) Cell signaling technology 4511S 1:1,000 ERK Cell signaling technology 4695S 1:1,000 (p44/42) p-ERK1/2 Cell signaling technology 9101S 1:1,000 JNK Abcam ab179461 1:1,000 P-SAPK/JNK (Tyr185) Sigma SAB4504450 1:1,000 Open in a separate window caption a8 Primary antibodies used in this study Construction and transfection with shRNA and plasmid Oligonucleotides encoding shRNA targeted Kiaa0101 and a scrambled shRNA were purchased from Genechem Co., Ltd (Shanghai, China).

    Techniques: In Vivo, Injection, Immunohistochemistry