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Matrix Metalloproteinase 13

Matrix metalloproteinase-13 (MMP-13) is a member of the matrix metalloproteinase family, invloved in the breakdown of extracellular matrix.
It plays a role in tissue remodeling and degradation, and has been implicated in various pathological conditions such as osteoarthritis, cancer, and cardiovascular disease.
Optimizing MMP-13 research can be facilitated by PubCompare.ai, which utilizes AI-driven comparisons to identify the best protocols from literature, preprints, and patents, enhancing reproducibility and accuracy.
This streamlines the research process and helps discover the optimal tools and techniques for studying MMP-13.

Most cited protocols related to «Matrix Metalloproteinase 13»

1
Collagenase-Induced Germinal Matrix Hemorrhage

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Publication 2012
Anesthesia Animals Asepsis Betadine Clostridium Collagenase collagenase 1 Cranium Dura Mater Gender Institutional Animal Care and Use Committees Isoflurane Loma Matrix Metalloproteinase 13 Needles Operative Surgical Procedures Oxygen Rats, Sprague-Dawley Reading Frames Scalp Sutures Syringes Trephining
2
Expansion of Undifferentiated Human Pluripotent Stem Cells
Low passage hESCs (H9, WiCell) were used. Similar results were obtained using HUES13 (Harvard) and hIPSCs derived in our laboratory. Undifferentiated hESCs were cultured as described [33] with slight modification. Briefly, cells were cultured in Knockout Dulbecco's modified Eagle's medium (KODMEM, Invitrogen, 10829-018) supplemented with 1 mM L-glutamine with 20% Knockout Serum Replacement medium (KOSR, Invitrogen), 1 mM sodium pyruvate, 0.1 mM nonessential amino acids (NEAA, Invitrogen), 50 U/ml penicillin, 50 µg/ml streptomycin (Invitrogen), 0.1 mM beta-mercaptoethanol (Invitrogen) and 8 ng/ml basic fibroblast growth factor (bFGF, Sigma catalogue F0291-25UG). hESCs were grown on Matrigel (growth factor-reduced, BD Bioscience)-coated 6-well plates (Corning, Inc. catalogue 3506) on a feeder layer of primary MEFs from E13.5 CD-1 mice isolated as described [33] . Passage 3 to 4 MEFs were gamma-irradiated with 3,000 rads (30 Grays) and plated at 104 cells per cm2. All hESC lines were passaged following enzymatic digestion with either collagenase IV (Invitrogen, 17104-019) approximately every 7 days or Accutase (Chemicon) approximately every 10 days [34] (link), depending on cell condition and confluency. For collagenase treatment, cells were exposed to 1 mg/ml in KODMEM, sterile filtered, at room temperature. Once the edge of colonies were about to lift from the plate, the cells were rinsed twice with DPBS (Ca2+- and Mg2+-free), culture medium was added and cells were mechanically dispersed into 100–500-cell clusters by trituration using a 5 ml pipette and re-plated. For Accutase treatment, cells were washed twice with DPBS and then subsequently washed with a small amount of Accutase (1× concentration, Innovative Cell Technologies) and then exposed to Accutase at room temperature. After a few minutes, when MEFs and hESC-derived fibroblasts began to lift from the plate, accutase was removed and hESCs were washed twice with DPBS (Ca2+- and Mg2+-free) to remove MEFs and hESC-derived fibroblasts. A third of the volume of culture medium normally used was added and the stem cells were mechanically dispersed into 10–50-cell clusters by trituration as above. Each passage was a 1∶3 split ratio for collagenase IV-treated cells and 1∶4 to 1∶6 ratio for accutase-treated cells. Cells were routinely tested for mycoplasma (MycoAlert; Cambrex, Walkersville, MD).
Kita-Matsuo H., Barcova M., Prigozhina N., Salomonis N., Wei K., Jacot J.G., Nelson B., Spiering S., Haverslag R., Kim C., Talantova M., Bajpai R., Calzolari D., Terskikh A., McCulloch A.D., Price J.H., Conklin B.R., Chen H.S, & Mercola M. (2009). Lentiviral Vectors and Protocols for Creation of Stable hESC Lines for Fluorescent Tracking and Drug Resistance Selection of Cardiomyocytes. PLoS ONE, 4(4), e5046.
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Publication 2009
2-Mercaptoethanol accutase Amino Acids Cells Collagenase collagenase 1 Culture Media Digestion Enzymes Feeder Cell Layers Fibroblast Growth Factor 2 Fibroblasts Gamma Rays Glutamine Growth Factor Human Embryonic Stem Cells Human Induced Pluripotent Stem Cells matrigel Matrix Metalloproteinase 13 Mus Mycoplasma Penicillins Pyruvate RRAD protein, human Serum Sodium Stem Cells Strains Streptomycin
3
Collagenase-Induced Achilles Tendon Injury
Forty 12-weeks-old male Sprague Dawley rats (Rattus norvegicus) (Envigo, Huntingdon, UK) (mean body weight 347 ± 9 g) were used in this study. In the absence of suitable data to perform the power analysis, the sample size was calculated according to the Mead’s resource equation (E = N-T, 10<E<20). Thus, considering two treated limbs per animal for a total of 16 treated tendons per time-point, the sample size was calculated as follows: E = (16–1)-(4–1) = 12. The rats were randomly divided into two treated groups that were injected within the Achilles tendon with collagenase type I (collagenase from Clostridium histolyticum, Worthington Lakewood, NJ, USA, 185 IU/mg): 1) collagenase 1 mg/mL defined as low dose (LD); 2) collagenase 3 mg/mL defined as high dose (HD). In each group, the contralateral tendon was treated either with phosphate buffered saline (PBS) and served as control (CTRL), or left untreated and served the sham control (S-CTRL). For each time point, 4 tendons were injected with LD, 4 tendons with HD, 4 tendons received PBS and 4 tendons were left untreated (n = 4). Tendon explants were analyzed at 3, 7, 15, 30 and 45 days.
Perucca Orfei C., Lovati A.B., Viganò M., Stanco D., Bottagisio M., Di Giancamillo A., Setti S, & de Girolamo L. (2016). Dose-Related and Time-Dependent Development of Collagenase-Induced Tendinopathy in Rats. PLoS ONE, 11(8), e0161590.
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Publication 2016
Animals Body Weight Collagenase, Clostridium histolyticum collagenase 1 Males Matrix Metalloproteinase 13 Phosphates Rats, Sprague-Dawley Rattus norvegicus Saline Solution Tendon, Achilles Tendons
4
Quantitative Analysis of Chondrogenic and Osteogenic Markers
Total cellular RNA was extracted from the cultures by using the RNeasy Protect Mini Kit with an on-column RNase-free DNase treatment (Qiagen, Hilden, Germany) [16 (link),37 (link),46 (link)]. RNA was eluted in 30 μl RNase-free water. Reverse transcription was carried out with 8 μl of eluate by using the 1st Strand cDNA Synthesis kit for RT-PCR (AMV) (Roche Applied Science). An aliquot of the cDNA product (2 μl) was amplified with real-time PCR by using the Brilliant SYBR Green QPCR Master Mix (Stratagene, Agilent Technologies, Waldbronn, Germany) [16 (link)] on an Mx3000P QPCR operator system (Stratagene) as follows: (95°C, 10 minutes), amplification by 40 cycles (denaturation at 95°C, 30 seconds; annealing at 55°C, 1 minute; extension at 72°C, 30 seconds), denaturation (95°C, 1 minute), and final incubation (55°C, 30 seconds). The primers (Invitrogen GmbH) used were SOX9 (chondrogenic marker) (forward 5'-ACACACAGCTCACTCGACCTTG-3'; reverse 5'-GGGAATTCTGGTTGGTCCTCT-3'), type II collagen (COL2A1) (chondrogenic marker) (forward 5'-GGACTTTTCTCCCCTCTCT-3'; reverse 5'-GACCCGAAGGTCTTACAGGA-3'), type I collagen (COL1A1) (osteogenic marker) (forward 5'-ACGTCCTGGTGAAGTTGGTC-3'; reverse 5'-ACCAGGGAAGCCTCTCTCTC-3'), type X collagen (COL10A1) (marker of hypertrophy) (forward 5'-CCCTCTTGTTAGTGCCAACC-3'; reverse 5'-AGATTCCAGTCCTTGGGTCA-3'), alkaline phosphatase (ALP) (osteogenic marker) (forward 5'-TGGAGCTTCAGAAGCTCAACACCA-3'; reverse 5'-ATCTCGTTGTCTGAGTACCAGTCC-3'), matrix metalloproteinase 13 (MMP13) (marker of terminal differentiation) (forward 5'-AATTTTCACTTTTGGCAATGA-3'; reverse 5'-CAAATAATTTATGAAAAAGGGATGC-3'), osteopontin (OP) (osteogenic marker) (forward 5'-ACGCCGACCAAGGAAAACTC-3'; reverse 5'-GTCCATAAACCACACTATCACCTCG-3'), runt-related transcription factor 2 (RUNX2) (osteogenic marker) (forward 5'-GCAGTTCCCAAGCATTTCAT-3'; reverse 5'-CACTCTGGCTTTGGGAAGAG-3'), β-catenin (mediator of the Wnt signaling pathway for osteoblast lineage differentiation) (forward 5'-CAAGTGGGTGGTATAGAGG-3'; reverse 5'-GCGGGACAAAGGGCAAGA-3'), parathyroid hormone-related protein (PTHrP) (hypertrophy-associated gene) (forward 5'-CGACGACACACGCACTTGAAAC-3'; reverse 5'-CGACGCTCCACTGCTGAACC-3'), lipoprotein lipase (LPL) (adipogenic marker) (forward 5'-GAGATTTCTCTGTATGGCACC-3'; reverse 5'-CTGCAAATGAGACACTTTCTC-3'), peroxisome proliferator-activated receptor gamma 2 (PPARG2) (adipogenic marker) (forward 5'-GCTGTTATGGGTGAAACTCTG-3'; reverse 5'-ATAAGGTGGAGATGCAGGCTC-3'), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (housekeeping gene and internal control) (forward 5'-GAAGGTGAAGGTCGGAGTC-3'; reverse 5'-GAAGATGGTGATGGGATTTC-3') (all 150 nM final concentration) [13 (link),15 (link),16 (link),46 (link)-49 (link)]. Control conditions included reactions using water and non-reverse-transcribed mRNA. Specificity of the products was confirmed by melting curve analysis and agarose gel electrophoresis. The threshold cycle (Ct) value for each gene of interest was measured for each amplified sample by using the MxPro QPCR software (Stratagene), and values were normalized to GAPDH expression by using the 2-ΔΔCt method, as previously described [16 (link)].
Venkatesan J.K., Ekici M., Madry H., Schmitt G., Kohn D, & Cucchiarini M. (2012). SOX9 gene transfer via safe, stable, replication-defective recombinant adeno-associated virus vectors as a novel, powerful tool to enhance the chondrogenic potential of human mesenchymal stem cells. Stem Cell Research & Therapy, 3(3), 22.
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Publication 2012
Adipogenesis Alkaline Phosphatase Anabolism beta-Catenin brilliant green Cells Chondrogenesis Collagen Type I Collagen Type II Collagen Type X Deoxyribonuclease I Differentiation Antigens DNA, Complementary Electrophoresis, Agar Gel Endoribonucleases Genes Genes, Housekeeping Glyceraldehyde-3-Phosphate Dehydrogenases Hypertrophy Lipoprotein Lipase Matrix Metalloproteinase 13 Neoplasm Metastasis Oligonucleotide Primers Osteoblasts Osteogenesis Osteopontin PPAR gamma PTHLH protein, human Real-Time Polymerase Chain Reaction Reverse Transcriptase Polymerase Chain Reaction Reverse Transcription RNA, Messenger RUNX2 protein, human SOX9 protein, human Training Programs Wnt Signaling Pathway
5
Isolation of Primary Tumor Cells

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Publication 2015
Cells Digestion Hemoglobin, Sickle Immunoglobulins Matrix Metalloproteinase 13 Neoplasms

Most recents protocols related to «Matrix Metalloproteinase 13»

1
Isolation and Culture of hPDLSCs
Healthy premolars donated by periodontally healthy individuals undergoing orthodontic treatment at Shenzhen Longgang District Maternity & Child Healthcare Hospital were selected. Then, periodontal ligament tissue from the tooth’s root was scraped with a sharp knife and collected. Next, the tissue was enzymatically hydrolyzed with 0.3% collagenase type I for 30 min and then centrifuged. Subsequently, the sediment was transferred to a culture flask and cultured in α minimum essential medium (a-MEM) containing 10% fetal bovine serum (FBS, Gibco) and 1% penicillin streptomycin (PS) (Solarbio, China). When reaching a confluence of 70%, the primary PDLSCs were passaged cultured, and the third-generation cells were taken for subsequent tests [20 (link)]. In addition, the above teeth were collected with informed consent from donors and the experiment was approved by the Ethics Committee of Shenzhen Longgang District Maternity & Child Healthcare Hospital (LGFYYXLLL-2022-009).hPDLSCs cells in the logarithmic growth phase were taken and seeded in a 6-well plate at the same density. And the cells were divided into four groups. CTRL group: untreated hPDLSCs; Ori group: hPDLSCs were treated with 2 μM oridonin (Ori) 24 h; LPS group: hPDLSCs were treated with 10 μg/mL LPS 24 h [20 (link)]; LPS + Ori group: hPDLSCs were treated with 10 μg/mL LPS and 2 μM oridonin for 24 h.
Jiang J., Zhang N., Song H., Yang Y., Li J, & Hu X. (2023). Oridonin alleviates the inhibitory effect of lipopolysaccharide on the proliferation and osteogenic potential of periodontal ligament stem cells by inhibiting endoplasmic reticulum stress and NF-κB/NLRP3 inflammasome signaling. BMC Oral Health, 23, 137.
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Publication 2023
Bicuspid Cells Children's Health Culture Media Donors Ethics Committees, Clinical Matrix Metalloproteinase 13 oridonin Penicillins Periodontal Ligament Streptomycin Tissues Tooth Tooth Root
2
Biomarkers of Intervertebral Disc Degeneration
We determined the levels of TNF‐α, IL‐1β, IL‐6, matrix metalloproteinase (MMP)‐3, MMP‐13, Collagen II, and aggrecan in the serum and vertebral disc tissue. We used TNF‐α (RTA00, Bio‐Techne, Minneapolis, Minnesota, USA), IL‐1β (RLB00, Bio‐Techne, Minneapolis, Minnesota, USA), IL‐6 (437107, BioLegend, San Diego, CA, USA), MMP‐3 (SEA101Ra, Cloud‐Clone Corp, Houston, TX, USA), MMP‐13 (SEA099Ra, Cloud‐Clone Corp, Houston, TX, USA), Collagen II (ER0852, Wuhan Fine Biotech, Wuhan, China), and aggrecan (SEB908Ra, Cloud‐Clone Corp, Houston, TX, USA) Enzyme‐Linked Immunosorbent Assay (ELISA) kits to measure relative factors.
Yao B., Cai Y., Wang W., Deng J., Zhao L., Han Z, & Wan L. (2023). The Effect of Gut Microbiota on the Progression of Intervertebral Disc Degeneration. Orthopaedic Surgery, 15(3), 858-867.
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Publication 2023
Aggrecans Clone Cells Collagen Enzyme-Linked Immunosorbent Assay Interleukin-1 beta Matrix Metalloproteinase 3 Matrix Metalloproteinase 13 Serum Tissues Tumor Necrosis Factor-alpha Vertebra
3
Isolation and Functional Assessment of Pancreatic Islets
Islets were isolated from 8- to 36-week-old male and female mice. Isolation of pancreatic islets was performed as previously described (62 (link)). In brief, pancreas was perfused by injection of 3 mM Collagenase-P (Roche) (0.3 mg/mL) in HBSS containing 25 mM HEPES and 0.5% (w/v) BSA into the common bile duct. Isolated islets were recovered for 48 hours in RPMI 1640 (Thermo Fisher Scientific) in humidified 5% CO2, at 37°C. After this period, islets were used for functional assessments. Before determination of insulin secretion, islets were equilibrated for 1 hour in KRB buffer (115 mM NaCl, 4.5 mM KCl, 1.2 mM KH2PO4, 2.6 mM CaCl2, 1 mM MgCl2, 10 mM HEPES, 20 mM NaHCO3, 0.2% w/v BSA, pH 7.4) with 2.8 mM glucose. Determination of insulin secretion from the islets was performed in 12-well plates containing 60 μL KRB (8 islets/well, 5 independent experiments performed in triplicate). After 1 hour preincubation in KRB with 2.8 mM glucose, islets were incubated for 1 hour in 20 mM glucose, 25 mM KCl, or 300 μM tolbutamide. Released insulin was measured in the supernatant using an insulin ELISA kit. Insulin content was determined from groups of 10 islets lysed in the protein extraction reagent M-PER (Thermo Fisher Scientific), using insulin ELISA kit.
Khajavi N., Beck A., Riçku K., Beyerle P., Jacob K., Syamsul S.F., Belkacemi A., Reinach P.S., Schreier P.C., Salah H., Popp T., Novikoff A., Breit A., Chubanov V., Müller T.D., Zierler S, & Gudermann T. (2023). TRPM7 kinase is required for insulin production and compensatory islet responses during obesity. JCI Insight, 8(3), e163397.
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Publication 2023
Bicarbonate, Sodium Buffers Choledochus Enzyme-Linked Immunosorbent Assay Females Glucose Hemoglobin, Sickle HEPES Insulin Insulin Secretion Islets of Langerhans Magnesium Chloride Males Matrix Metalloproteinase 13 Mice, House M protein, multiple myeloma Pancreas Sodium Chloride Tolbutamide
4
Isolation and Culture of Murine Cardiomyocytes

Preparation and dilution: prepare 100 ml of double antibody (add 5 ml saline to 5 ml streptomycin, shake well, then add 5 ml saline to the penicillin vial to dissolve, transfer all 5 ml to 95 ml saline, and divide into 10 vials). Prepare 100 ml DMEM culture solution containing 15% fetal bovine serum (85 ml DMEM, 15 ml fetal bovine serum, and 1 ml double antibody), and prepare 10 ml 0.1% collagenase I (10 mg collagenase I dissolved in 10 ml PBS). The solution is usually prepared in advance and filtered through a 0.22 pore filter

Irradiation with UV light for 20-30 min (2 culture flasks, 2 15 ml centrifuge tubes, and 4 lunch boxes were placed on the UV table)

SD mice immersed in 75% alcohol (5~10 min)

Add two drops of medium (DMEM + serum + double antibodies) to one vial of medium, and leave the other vial of medium undisturbed and screwed to one side of the ultrathin table (note: this step can be performed with a 50 ml pipette)

Take another dropper with a straight tip, rinse it, insert PBS, then remove the round container set, and add the appropriate amount of PBS

Take the heart. Six milk mice can be sewn sequentially onto a plastic foam plate using a broad-headed needle, and then open the chest sequentially using scissors to reveal the heart. Take another knife and forceps, lift the heart, cut it out, place it in a round dish with prechilled PBS, rinse the heart 2 times with PBS, and cut it out (1 mm × 1 mm × 1 mm)

Remove the drop and aspirate the PBS; then take the penicillin vial and transfer the excised myocardial tissue into the penicillin vial into the penicillin vial. Add 2 drops of collagenase I (approximately 3 ml) to the penicillin vial with dropper. After 10 minutes, add collagenase I (approximately 3 ml) to the dropper vial, close tightly, and leave for 10 minutes in a water bath at 37°C. After 10 minutes, add the digestion solution to the centrifuge tube with DMEM to complete the digestion

Centrifugation (room temperature, 1000 rpm, 10 min/time)

Through a 200-mesh sieve, after centrifugation, discard the supernatant, and use the medium in a third tube to resuspend the cells. After centrifugation, discard the supernatant, resuspend the cell pellet with the medium in the third centrifuge tube, take another set of round dishes, pass the cell suspension through a 200-mesh sieve, and then collect the sieved cells

Ren C., Yi W., Jiang B., Gao E., Liang J., Zhang B., Yang Z., Zheng D, & Zhang Y. (2023). Diminished AdipoR1/APPL1 Interaction Mediates Reduced Cardioprotective Actions of Adiponectin against Myocardial Ischemia/Reperfusion Injury in Type-2 Diabetic Mice. Stem Cells International, 2023, 7441367.
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Publication 2023
Antibodies Bath Cells Centrifugation Chest Collagenase, Clostridium histolyticum Ethanol Fetal Bovine Serum Forceps Gastrointestinal Tract Heart Hyperostosis, Diffuse Idiopathic Skeletal Immunoglobulins Matrix Metalloproteinase 13 Milk, Cow's Mus Myocardium Needles Penicillins Saline Solution Serum Streptomycin Technique, Dilution Tremor
5
Immunohistochemical Analysis of Coccygeal Disc Samples
Rats were euthanized via excess carbon dioxide inhalation, and the coccygeal discs were collected 6 weeks after implantation, and an immunohistochemical analysis was performed for aggrecan and type II collagen. We performed immunofluorescence analysis for a calcitonin gene receptor protein (CGRP), Tie2, brachyury, matrix metalloproteinase-13 (MMP-13), human nuclei antibody, tumor necrosis factor-alpha (TNF-α), and interleukin-1-beta (IL-1β). The harvested tissues were fixed overnight in a 4% paraformaldehyde (PFA) solution and decalcified by using a decalcification solution (RapidCal Immuno; BBC Biochemical, Mount Vernon, WA, USA) for 2 weeks. Then, discs were embedded within paraffin wax and sectioned longitudinally using a microtome (Leica) into sections of 5–10 µm thickness. For the immuno-staining, the first sections were dewaxed, rehydrated, and after that stained with primary antibodies against aggrecan (ab36861; Abcam, Cambridge, UK, 1:1000), type II collagen (ab34712; Abcam, Cambridge, UK, 1:100), CGRP (ab47027; Abcam, Cambridge, UK, 1:200), Tie2 (NBP2-20636; Novus Biologicals, Littleton, CO, USA, 1:200), brachyury (sc-166962; Santa Cruz, Dallas, TX, USA, 1:200), human nuclei antibody (MAB1281; Sigma Aldrich, St. Louis, MO, USA, 1:200), TNF-α (ab6671; Abcam, Cambridge, UK, 1:200), MMP-13 (ab39012; Abcam, Cambridge, UK, 1:200), and IL-1β (AF-501-NA; Novus Biologicals, Littleton, CO, USA, 1:200). Then, after 24 h of incubation, sections were washed with phosphate-buffered saline with Tween 20 and again incubated with the secondary antibody anti-Rb horseradish peroxidase (Roche Diagnostics Ltd., Basel, Switzerland), and Alexa Fluor 488 (A11034; Invitrogen, Waltham, MA, USA, 1:400), Alexa Fluor 488 (A11029; Invitrogen, Waltham, MA, USA, 1:400), Alexa Fluor 568 (A10042; Invitrogen, Waltham, MA, USA, 1:400), and Alexa Fluor 647 (A21469; Invitrogen, Waltham, MA, USA, 1:400)-conjugated secondary antibodies. After that, specimens were carried out for the washing step, then the specimens were counterstained with 4′, 6-diamidino-2-phenylindole (DAPI) (Abcam, Cambridge, UK, 1:1000) and incubated for 10 min. The sections were mounted and finally examined using a fluorescence microscope (Zeiss 880, Oberkochen, Germany, and Leica SP5, Wetzlar, Germany). The percentages of the positive area for aggrecan and type II collagen and positive cell number relative to DAPI for CGRP, Tie 2, brachyury, MMP-13, human nuclei antibody, TNF-α, and IL-1β were calculated using ImageJ software (Version 1.50b, https://imagej.nih.gov/ij/ (accessed on 10 November 2022)).
Bhujel B., Yang S.S., Kim H.R., Kim S.B., Min B.H., Choi B.H, & Han I. (2023). An Injectable Engineered Cartilage Gel Improves Intervertebral Disc Repair in a Rat Nucleotomy Model. International Journal of Molecular Sciences, 24(4), 3146.
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Publication 2023
Aggrecans alexa 568 alexa fluor 488 Alexa Fluor 647 Antibodies Antibodies, Anti-Idiotypic Biological Factors Brachyury protein Calcitonin Calcitonin Receptor Carbon dioxide Cell Nucleus Coccyx Collagen Type II Diagnosis Fluorescent Antibody Technique Genes Homo sapiens Horseradish Peroxidase Immunoglobulins Inhalation Interleukin-1 beta Matrix Metalloproteinase 13 Microscopy, Fluorescence Microtomy Novus Ovum Implantation Paraffin paraform Phosphates Proteins Rattus Saline Solution Staph protein A receptor Tissues TNF protein, human Tween 20

Top products related to «Matrix Metalloproteinase 13»

1
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
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Collagenase type 1 by Merck Group
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Collagenase type I is an enzyme used in laboratory settings to break down collagen, a structural protein found in various tissues. It is commonly used in cell isolation and tissue dissociation procedures.
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Streptomycin is a broad-spectrum antibiotic used in laboratory settings. It functions as a protein synthesis inhibitor, targeting the 30S subunit of bacterial ribosomes, which plays a crucial role in the translation of genetic information into proteins. Streptomycin is commonly used in microbiological research and applications that require selective inhibition of bacterial growth.
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Penicillin by Thermo Fisher Scientific
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Penicillin is a type of antibiotic used in laboratory settings. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Penicillin functions by disrupting the bacterial cell wall, leading to cell death.
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Collagenase type III is a purified enzyme derived from Clostridium histolyticum. It is used for the digestion and dissociation of connective tissue, such as cartilage and other extracellular matrices.
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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.
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Collagenase type 1 by Worthington
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Collagenase type I is an enzyme used to digest collagen, which is a key structural component of the extracellular matrix. It is commonly used in cell isolation and tissue dissociation procedures.
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α mem by Thermo Fisher Scientific
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α-MEM is a cell culture medium formulated for the growth and maintenance of mammalian cells. It provides a balanced salt solution, amino acids, vitamins, and other nutrients required for cell proliferation.
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Dispase by Merck Group
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Dispase is an enzyme primarily used for tissue dissociation and cell isolation. It is effective in disrupting the extracellular matrix, enabling the separation of cells from connective tissues.
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Collagenase by Merck Group
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Collagenase is an enzyme that breaks down collagen, the primary structural protein found in the extracellular matrix of various tissues. It is commonly used in cell isolation and tissue dissociation procedures.

More about "Matrix Metalloproteinase 13"

Matrix Metalloproteinase 13 (MMP-13), also known as collagenase-3, is a member of the matrix metalloproteinase (MMP) family.
This enzyme plays a crucial role in the breakdown and remodeling of the extracellular matrix (ECM), which is the structural network that supports and surrounds cells within tissues.
MMP-13 is particularly important in the context of tissue remodeling, degradation, and various pathological conditions.
MMP-13 has been implicated in a number of disease states, including osteoarthritis, cancer, and cardiovascular disease.
In osteoarthritis, MMP-13 contributes to the degradation of articular cartilage, leading to joint damage and pain.
In cancer, MMP-13 can facilitate tumor invasion and metastasis by breaking down the ECM.
Additionally, MMP-13 has been associated with the development and progression of cardiovascular diseases, such as atherosclerosis.
Optimizing research on MMP-13 can be facilitated by using tools like PubCompare.ai, which utilizes AI-driven comparisons to identify the best protocols from literature, preprints, and patents.
This approach can enhance the reproducibility and accuracy of MMP-13 studies, streamlining the research process and helping researchers discover the optimal tools and techniques for investigating this important enzyme.
When studying MMP-13, researchers may utilize various cell culture components, such as fetal bovine serum (FBS), collagenase type I, streptomycin, penicillin, collagenase type III, penicillin/streptomycin, α-MEM, and dispase.
These reagents can be used to isolate, culture, and manipulate cells expressing MMP-13, enabling the investigation of its biological functions and its role in different pathological conditions.
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