Bacterial collagenase

Manufactured by Merck Group

Sourced in United States

Bacterial collagenase is a proteolytic enzyme derived from certain bacteria. It functions to cleave the peptide bonds in collagen, a structural protein found in various connective tissues.

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Lab products found in correlation

Caspase 9 total and cleaved, by Cell Signaling Technology (2 mentions) Caspase 7 total and cleaved, by Cell Signaling Technology (2 mentions) Horseradish peroxidase conjugated anti rabbit igg and anti mouse igg antibodies, by Merck Group (2 mentions) Cox 2, by Cell Signaling Technology (2 mentions) P ampkα, by Cell Signaling Technology (2 mentions) Caspase 8, by Cell Signaling Technology (2 mentions) β actin, by Cell Signaling Technology (2 mentions) Pycr1, by Abnova (2 mentions) Pycrl, by Abnova (2 mentions) Hoechst 33342, by BD (2 mentions) Diclofenac, by Merck Group (2 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (2 mentions) Puromycin, by Thermo Fisher Scientific (1 mentions) Mcf 7 cells atcc htb 22, by American Type Culture Collection (1 mentions) Mem eagle s medium, by Thermo Fisher Scientific (1 mentions) Pen strep mix, by Thermo Fisher Scientific (1 mentions) Beclin 1, by Cell Signaling Technology (1 mentions) Prodh pox, by Santa Cruz Biotechnology (1 mentions) Phosphate buffered saline (pbs), by Thermo Fisher Scientific (1 mentions) Nc slide a2, by ChemoMetec (1 mentions)

Close spelling variants of this product

Collagenase (2150 citations) Bacterial type IV collagenase (11 citations) Bacterial collagenase type VII (10 citations) Bacterial collagenase I (7 citations) Bacterial collagenase type I (5 citations) Bacterial collagenase VII-S (5 citations) Bacterial collagenase (Type IV-S, (4 citations) Bacterial collagenase type VII-S (3 citations) Bacterial collagenase VII (3 citations) Type IA Crude Bacterial Collagenase (3 citations)

13 protocols using bacterial collagenase

Molecular Mechanisms of MCF-7 Cell Apoptosis

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MCF-7 cells (ATCC^® HTB-22™) were obtained from ATCC (Manassas, VA, USA). MEM Eagle’s medium, fetal bovine serum, puromycin, Pen/Strep mix, and PBS were products of Gibco (Waltham, MA, USA). Propidium iodide (PI), annexin V-CF488A conjugate, and annexin V binding buffer were provided by the Biotium Company (Fremont, CA, USA). NC-Slide A2™ was purchased from Chemometec (Allerod, Denmark). Horseradish peroxidase conjugated anti-rabbit IgG and anti-mouse IgG antibodies, bacterial collagenase, 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenyltetrazolium bromide (MTT), 2′,7′-dichlorofluorescin diacetate (DCFDA), indomethacin, and diclofenac were purchased from Sigma Aldrich (Saint Louis, MO, USA). Primary antibodies against COX2, p-AMPKα, mTor, caspase 8, caspase 9 total and cleaved, caspase 7 total and cleaved, BID, PARP, Beclin 1, AGT5, ATG 7, and B-actin were products of Cell Signaling Technology (Danvers, MA, USA). Primary antibodies for PRODH/POX, PPARγ, GLUD 1/2, and prolidase were products of Santa Cruz Biotechnology (Dallas, TX, USA). PYCR1, PYCRL, and PPARδ primary antibodies were obtained from Abnova (Taipei, Taiwan). Hoechst 33342 was obtained from Becton Dickinson (Franklin Lakes, NJ, USA). CRISPR All-In-One Non-Viral Vector and lipofectamine were products of Applied Biological Materials Inc. (Richmond, BC, Canada).

Kazberuk A., Chalecka M., Palka J., Bielawska K, & Surazynski A. (2022). NSAIDs Induce Proline Dehydrogenase/Proline Oxidase-Dependent and Independent Apoptosis in MCF7 Breast Cancer Cells. International Journal of Molecular Sciences, 23(7), 3813.

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Isolation and Culture of Murine Chondrocytes and BMSCs

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All primary cells were harvested from femurs of male transgenic mice at 3–4 weeks of age. Chondrocytes were isolated from cartilage of the proximal epiphysis, which lacks a secondary ossification center (26 (link)). Briefly, the epiphysis was removed with a pair of tweezers and incubated in Ca²⁺- and Mg²⁺-free HBSS with 0.2% bacterial collagenase (Sigma, St. Louis) for 3–4 hours at 37°C to release chondrocytes from their extracellular matrix. BMSCs were isolated from femurs by cutting off both ends and flushing out the contents of the remaining diaphyseal shaft via brief high-speed centrifugation. Chondrocytes or BMSCs from multiple animals were pooled and plated at a density of 1 × 10⁵ cells/cm² in 24-well tissue-culture-treated plates with complete media consisting of DMEM and the following components: 10% FBS, 4.5mg/ml D-glucose, 100 units/ml penicillin, 100μg/ml streptomycin, 0.25μg/ml Fungizone (Life Technologies, Carlsbad), 2 mM L-alanyl-L-glutamine, and 2mM sodium pyruvate. Cultures were incubated at 37°C in a humidified chamber with 5% CO₂ and media was replaced every 2–3 days. Beginning at confluence, the complete media was supplemented with 100μg/ml ascorbate-2-phosphate and 2mM sodium phosphate (pH 7.4) to support mineralization.

Pregizer S.K, & Mortlock D.P. (2015). Dynamics and Cellular Localization of Bmp2, Bmp4, and Noggin Transcription in the Postnatal Mouse Skeleton. Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 30(1), 64-70.

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Collagenase-Induced Intracerebral Hemorrhage Model

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ICH was induced by intrastriatal injection of Bacterial collagenase into the right basal ganglia as previously described [14 (link)]. Briefly, mice were anesthetized with ketamine (100 mg/kg) and xylazine (10 mg/kg) (2:1 vol/vol, intraperitoneal injection) and positioned prone in a stereotaxic head frame. Bacterial collagenase (0.075 units, type VII-S; Sigma-Aldrich, St. Louis, MO) was dissolved in 0.5 μL PBS and infused into the right basal ganglia at a rate of 0.1667 μL/min, using an infusion pump (Stoelting, IL). The needle was left for an additional 5 min to prevent possible leakage of the collagenase solution, and withdrawn slowly at a rate of 1 mm/min. After removal of the needle, the cranial burr hole was sealed with bone wax, the incision was sutured, and 0.4 mL of normal saline was injected subcutaneously, and the mice were allowed to recover. The sham operation was performed with PBS only. All ICH animals with hematoma and neurological deficits were included. Animals that died before experimental endpoints reached were replaced with new animals. Animals with no hematoma were excluded.

Zhao L., Chen S., Sherchan P., Ding Y., Zhao W., Guo Z., Yu J., Tang J, & Zhang J.H. (2018). Recombinant CTRP9 administration attenuates neuroinflammation via activating adiponectin receptor 1 after intracerebral hemorrhage in mice. Journal of Neuroinflammation, 15, 215.

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Chondrocyte Culture and Cytokine Treatment

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Small slices of cartilage were sequentially digested with 0.06% bacterial collagenase (Sigma) then seeded at a density of 1.5 × 10⁴ cells/cm² in culture medium consisting of DMEM (Gibco-Invitrogen) supplemented with 10% fetal bovine serum (FBS), 100 U/ml penicillin, and 100 μg/ml streptomycin (Gibco-Invitrogen). Cells were treated with 5 ng/ml for IL-1β (R&D systems, Minneapolis, MN), 3 ng/ml for TGF-βs (R&D systems, Minneapolis, MN), and 300 nM for TSA (Sigma, St Louis, MO, USA) in this study.

Song J., Jin E.H., Kim D., Kim K.Y., Chun C.H, & Jin E.J. (2014). MicroRNA-222 regulates MMP-13 via targeting HDAC-4 during osteoarthritis pathogenesis. BBA Clinical, 3, 79-89.

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3D Collagen Matrix Cell Apoptosis Assay

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Cells growing on plastic culture plates were detached enzymatically with trypsin-EDTA solution (Invitrogen) and cell embedded in 3D COL1 were recovered after dissolving gels in 2 mg/ml bacterial collagenase (Sigma-Aldrich). Apoptosis was quantified as described previously [38 (link)].

Assent D., Bourgot I., Hennuy B., Geurts P., Noël A., Foidart J.M, & Maquoi E. (2015). A Membrane-Type-1 Matrix Metalloproteinase (MT1-MMP) – Discoidin Domain Receptor 1 Axis Regulates Collagen-Induced Apoptosis in Breast Cancer Cells. PLoS ONE, 10(3), e0116006.

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Quantifying Collagen Internalization and Deposition

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To analyze the amount of collagen internalized in the intracellular space or deposited in the extracellular space quantitatively, hMSCs were incubated with culture medium containing fluorescently labeled collagen monomers for various period of time. Quantitative analysis of internalized Alexa 488-labeled collagen was determined by measuring the total fluorescence, using a microplate reader (Safire II; Tecan, San Jose, CA, USA), in the cell lysate fraction collected up to 50 h after discarding the extracellular fraction containing deposited collagen fibrils by digestion with excess bacterial collagenase (Sigma-Aldrich). In separate experiments, after discarding the culture medium, the collagen fibrils deposited in the extracellular space were digested by collagenase, and the amount of collagen was determined by measuring the total fluorescence in this fraction.

Han S., Li Y.Y, & Chan B.P. (2015). Protease inhibitors enhance extracellular collagen fibril deposition in human mesenchymal stem cells. Stem Cell Research & Therapy, 6, 197.

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Collagenase and Proteinase Assay Protocol

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Bacterial collagenase and alkaline proteinase were purchased from Sigma-Aldrich (St. Louis, MO, USA). The bicinchoninic acid (BCA) protein assay kit was purchased from Beijing Solarbio Science and Technology Co., Ltd. (Beijing, China). Commercial kits used for determining hydroxyproline (Hyp), alkaline phosphatase (ALP) concentration and tartrate-resistant acid phosphatase-5b (TRAP-5b) activity were purchased from Jiancheng Inst. of Biotechnology (Nanjing, China). Rabbit monoclonal anti-transforming growth factor β1 (TGFβ) and rabbit monoclonal anti-Smad3 were purchased from Cell Signaling Technology (Danvers, MA, USA). Rabbit monoclonal anti-Smad7, rabbit monoclonal anti-α2 and rabbit monoclonal anti-β1 were purchased from Abcam (Cambridge, MA, USA). Other chemicals used in this study were of analytical grade or better and were commercially available.

Zhang L., Zhang S., Song H, & Li B. (2018). Effect of Collagen Hydrolysates from Silver Carp Skin (Hypophthalmichthys molitrix) on Osteoporosis in Chronologically Aged Mice: Increasing Bone Remodeling. Nutrients, 10(10), 1434.

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Comprehensive Antibody and ECM Protocol

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A complete and detailed list of the polyclonal and monoclonal antibodies used in this study is provided in Supplementary Table 2. Doxycycline (DOX) hyclate was purchased from Sigma (St. Louis, MO; Cat #D9891). Rat-tail COL1 (regular and high concentration) was purchased from Discovery Labware Inc., Corning™ (Bedford, MA; Cat # 354236, regular; and # 354249, high concentration). Mouse collagen IV was purchased from Corning™ (Cat # 354233). Matrigel (Cultrex^®) was purchased from Trevigen (Gaithersburg, MD; Cat # 3444-005-01). Bacterial collagenase was purchased from Sigma (Cat# C9263). Trypsin-EDTA was purchased from Gibco (Cat # 25200).

Wasinski B., Sohail A., Bonfil R.D., Kim S., Saliganan A., Polin L., Bouhamdan M., Kim H.R., Prunotto M, & Fridman R. (2020). Discoidin Domain Receptors, DDR1b and DDR2, Promote Tumour Growth within Collagen but DDR1b Suppresses Experimental Lung Metastasis in HT1080 Xenografts. Scientific Reports, 10, 2309.

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Protein and Antioxidant Analysis

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Alcalase was purchased from Novozymes (Beijing, China). Proline (food grade) and bacterial collagenase were purchased from Sigma-Aldrich (St. Louis, MO, USA). The bicinchoninic acid (BCA) protein assay kit was purchased from Beijing Solarbio Science and Technology Co., Ltd. (Beijing, China). Commercial kits used for determining hydroxyproline (Hyp), type I and type III collagen, hyaluronic acid (HA), superoxide dismutase (SOD), catalase (CAT), and malondialdehyde (MDA) were purchased from Jiancheng Inst. of Biotechnology (Nanjing, China). All other chemicals used in the study were of analytical grade or better.

Song H., Zhang S., Zhang L, & Li B. (2017). Effect of Orally Administered Collagen Peptides from Bovine Bone on Skin Aging in Chronologically Aged Mice. Nutrients, 9(11), 1209.

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Molecular Signaling in MCF7 Breast Cancer

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MCF7 (ATCC^® HTB-22™) were obtained from the ATCC. Horseradish-peroxidase-conjugated anti-rabbit IgG and anti-mouse IgG antibodies, Alexa488 conjugated anti-rabbit IgG, bacterial collagenase, 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenyltetrazolium bromide (MTT), DCFDA, tetrahydro-2-furoic acid (THFA), glycyl-L-proline, ibuprofen, indomethacin, diclofenac, and sulindac were purchased from Sigma-Aldrich. The celecoxib and troglitazone were products of Targetmol. Solution 5 (VB-48™ PI–AO) was purchased from ChemoMetec. The primary antibodies against: COX2; p53; p-AMPKα; m-TOR; caspase-8; caspase-9, total and cleaved; caspase-7, total and cleaved; PARP, total and cleaved; and B-actin were products of Cell Signaling Technology. The PRODH/POX primary antibodies and PPARγ were products of Santa Cruz Biotechnology. The PYCR1, PYCRL, and PPAR delta primary antibodies were obtained from Abnova. The Hoechst 33342 was obtained from Becton Dickinson.

Kazberuk A., Chalecka M., Palka J, & Surazynski A. (2022). Nonsteroidal Anti-Inflammatory Drugs as PPARγ Agonists Can Induce PRODH/POX-Dependent Apoptosis in Breast Cancer Cells: New Alternative Pathway in NSAID-Induced Apoptosis. International Journal of Molecular Sciences, 23(3), 1510.

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