collagenase  (Worthington Biochemical)


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    Structured Review

    Worthington Biochemical collagenase
    Collagenase, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 96/100, based on 191 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/collagenase/product/Worthington Biochemical
    Average 96 stars, based on 191 article reviews
    Price from $9.99 to $1999.99
    collagenase - by Bioz Stars, 2020-05
    96/100 stars

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    Modification:

    Article Title: Histone deacetylase inhibition reduces cardiac connexin43 expression and gap junction communication
    Article Snippet: .. Neonatal murine atrial and ventricular tissues were dissociated separately in a Ca2 + - and Mg2 + -free collagenase balanced salt solution (dulbecco’s modified saline [DMS8 ], in mM: NaCl, 116; KCl, 5.4, NaH2 PO4 , 1.0; and dextrose, 5.5) containing ≈1 mg/ml of purified collagenase (type II), 5.5 μg/ml deoxyribonuclease I (Worthington Biochemical Corp., Lakewood, NJ, USA), and 1 mg/ml bovine serum albumin (BSA, fraction V, Sigma Chemical Corp., St. Louis, MO, USA; , , ). ..

    Protease Inhibitor:

    Article Title: Sensory neuron diversity in the inner ear is shaped by activity
    Article Snippet: .. Pieces of the cochlea were then digested first with collagenase (25 min at 37 °C) then 40 U/ml papain (25 min at 37 °C) (Worthington, ) before passing through a discontinuous density gradient of ovomucoid protease inhibitor (Worthington, ). .. The crude dissociation extract was passed through a 40 mm cell strainer (Corning, Inc., 352340) and placed in a petri dish with a glass bottom microwell (Cellvis, D60-14-1N) for manual collection.

    Incubation:

    Article Title: Soluble TNFα Signaling within the Spinal Cord Contributes to the Development of Autonomic Dysreflexia and Ensuing Vascular and Immune Dysfunction after Spinal Cord Injury
    Article Snippet: .. After trimming the roots, the DRGs were incubated with collagenase (2000 U/ml) and neutral protease (25 U/ml; Worthington Biochemical) in HBSS (Invitrogen) at 37°C for 30 min. DRGs were rinsed several times with HBSS and then gently triturated in culture media that consisted of Neurobasal-A, B-27, GlutaMax, and penicillin/streptomycin (Invitrogen). .. After two rounds of low-speed spins (2000 rpm × 2 min), the pellet containing the dissociated DRG neurons was resuspended in culture media containing 20 μ m of the antimitotic agent 5-fluoro-2′-deoxyuridine (Sigma-Aldrich) and plated onto glass coverslips coated with poly-L-lysine (0.1 mg/ml; Sigma-Aldrich) at a density of 2000 neurons/ml.

    Article Title: Histone demethylase LSD1 deficiency and biological sex: impact on blood pressure and aldosterone production
    Article Snippet: .. The capsules were suspended in Krebs Ringer bicarbonate solution (Sigma-Aldrich) (0.1% BSA, 200 mg glucose/dl, L-glutamine, 3.7 mmol/L of K+ ) (KRBGA) solution with collagenase (3.7 mg/mL) and DNAase (0.05 mg/mL) (Worthington Biochemical, Freehold, NJ, USA) for 60-min incubation at 37°C under 95% O2 and 5% CO2 . .. Isolated ZG cells underwent three rounds of brief washing and centrifugation followed by determination of cell count.

    Purification:

    Article Title: Histone deacetylase inhibition reduces cardiac connexin43 expression and gap junction communication
    Article Snippet: .. Neonatal murine atrial and ventricular tissues were dissociated separately in a Ca2 + - and Mg2 + -free collagenase balanced salt solution (dulbecco’s modified saline [DMS8 ], in mM: NaCl, 116; KCl, 5.4, NaH2 PO4 , 1.0; and dextrose, 5.5) containing ≈1 mg/ml of purified collagenase (type II), 5.5 μg/ml deoxyribonuclease I (Worthington Biochemical Corp., Lakewood, NJ, USA), and 1 mg/ml bovine serum albumin (BSA, fraction V, Sigma Chemical Corp., St. Louis, MO, USA; , , ). ..

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    Worthington Biochemical collagenase type 2
    The role of the hexosamine biosynthesis pathway (HBP) in blunting autophagic signaling. Representative western blots showing Beclin-1 and LC3 protein in cardiomyocytes from non-diabetic (Con) and <t>type</t> 2 diabetic ( db/db ) under basal conditions and in response
    Collagenase Type 2, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 99/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/collagenase type 2/product/Worthington Biochemical
    Average 99 stars, based on 22 article reviews
    Price from $9.99 to $1999.99
    collagenase type 2 - by Bioz Stars, 2020-05
    99/100 stars
      Buy from Supplier

    99
    Worthington Biochemical collagenase type 1
    Identification of TSP 1 cleavage sites for MT 1‐ MMP Western blot of TSP1 expression (developed with an antibody against an epitope nearby the N‐terminus; Lee et al , 2006 ) in lysates from siCtrl and siMT1‐silenced HUVEC. MT1‐MMP and tubulin are included as silencing and loading controls, respectively. The arrowhead marks full‐length TSP1 and the asterisk the N‐terminal TSP1 fragment. Western blot of in vitro digested TSP1 (developed with the same antibody as in A) incubated with increasing amounts of recombinant human MT1‐MMP catalytic domain. rhMT1‐MMP catalytic domain is also included. The arrowhead marks full‐length TSP1 and the asterisk the N‐terminal TSP1 fragment generated by MT1‐MMP cleavage. In silico model of the membrane‐anchored MT1‐MMP dimer (blue/orange) and TSP1 <t>type</t> 1 repeat domains 2 and 3 (green). Yellow marks the catalytic pocket in the MT1‐MMP protease, and red indicates the two selected cleavage sites in TSP1. Scheme depicting the TSP1 domain structure with the binding sequences to CD36, CD47, and αvβ3 integrin, as well as the positions of the identified cleavage sites for MT1‐MMP. DAF‐FM mean fluorescence intensity (MFI) in HUVEC expressing MT1‐MMP siRNA and left untreated or treated with 200 ng of full‐length TSP1 or the E123CaG‐1 fragment; n = 128–184 cells analyzed per condition in two independent experiments. Data are shown as individual cell values and mean ± SEM and were tested by the Kruskal–Wallis test; * P
    Collagenase Type 1, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 99/100, based on 141 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/collagenase type 1/product/Worthington Biochemical
    Average 99 stars, based on 141 article reviews
    Price from $9.99 to $1999.99
    collagenase type 1 - by Bioz Stars, 2020-05
    99/100 stars
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    Image Search Results


    The role of the hexosamine biosynthesis pathway (HBP) in blunting autophagic signaling. Representative western blots showing Beclin-1 and LC3 protein in cardiomyocytes from non-diabetic (Con) and type 2 diabetic ( db/db ) under basal conditions and in response

    Journal: Life sciences

    Article Title: Cardiac O-GlcNAcylation blunts autophagic signaling in the diabetic heart

    doi: 10.1016/j.lfs.2012.06.011

    Figure Lengend Snippet: The role of the hexosamine biosynthesis pathway (HBP) in blunting autophagic signaling. Representative western blots showing Beclin-1 and LC3 protein in cardiomyocytes from non-diabetic (Con) and type 2 diabetic ( db/db ) under basal conditions and in response

    Article Snippet: Briefly, hearts were rapidly excised from heparinized and anesthetized mice, perfused retrogradely with Ca2+ -free perfusion buffer consisting of (in mM) 0.6 KH2 PO4 , 0.6 Na2 HPO4 , 1.2 MgSO4 • 7H2 O, 0.032 phenol red, 12 NaHCO3 , 10 KHCO3 , 10 HEPES, 30 taurine, 10 2,3-butanedione monoxime, and 5.5 glucose, pH 7.46, followed by buffer containing 12.5 μM CaCl2 and 0.4 mg/ml collagenase type 2 (Worthington).

    Techniques: Western Blot

    The temporal progression of body weight (A) and survival (B) following either sham or trans-aortic constriction surgery to induce a pressure overload (PO) in non-diabetic (control), high fat-fed, or high fat-fed and STZ treated type 2 diabetic rats. †

    Journal: Life sciences

    Article Title: Cardiac O-GlcNAcylation blunts autophagic signaling in the diabetic heart

    doi: 10.1016/j.lfs.2012.06.011

    Figure Lengend Snippet: The temporal progression of body weight (A) and survival (B) following either sham or trans-aortic constriction surgery to induce a pressure overload (PO) in non-diabetic (control), high fat-fed, or high fat-fed and STZ treated type 2 diabetic rats. †

    Article Snippet: Briefly, hearts were rapidly excised from heparinized and anesthetized mice, perfused retrogradely with Ca2+ -free perfusion buffer consisting of (in mM) 0.6 KH2 PO4 , 0.6 Na2 HPO4 , 1.2 MgSO4 • 7H2 O, 0.032 phenol red, 12 NaHCO3 , 10 KHCO3 , 10 HEPES, 30 taurine, 10 2,3-butanedione monoxime, and 5.5 glucose, pH 7.46, followed by buffer containing 12.5 μM CaCl2 and 0.4 mg/ml collagenase type 2 (Worthington).

    Techniques:

    Identification of TSP 1 cleavage sites for MT 1‐ MMP Western blot of TSP1 expression (developed with an antibody against an epitope nearby the N‐terminus; Lee et al , 2006 ) in lysates from siCtrl and siMT1‐silenced HUVEC. MT1‐MMP and tubulin are included as silencing and loading controls, respectively. The arrowhead marks full‐length TSP1 and the asterisk the N‐terminal TSP1 fragment. Western blot of in vitro digested TSP1 (developed with the same antibody as in A) incubated with increasing amounts of recombinant human MT1‐MMP catalytic domain. rhMT1‐MMP catalytic domain is also included. The arrowhead marks full‐length TSP1 and the asterisk the N‐terminal TSP1 fragment generated by MT1‐MMP cleavage. In silico model of the membrane‐anchored MT1‐MMP dimer (blue/orange) and TSP1 type 1 repeat domains 2 and 3 (green). Yellow marks the catalytic pocket in the MT1‐MMP protease, and red indicates the two selected cleavage sites in TSP1. Scheme depicting the TSP1 domain structure with the binding sequences to CD36, CD47, and αvβ3 integrin, as well as the positions of the identified cleavage sites for MT1‐MMP. DAF‐FM mean fluorescence intensity (MFI) in HUVEC expressing MT1‐MMP siRNA and left untreated or treated with 200 ng of full‐length TSP1 or the E123CaG‐1 fragment; n = 128–184 cells analyzed per condition in two independent experiments. Data are shown as individual cell values and mean ± SEM and were tested by the Kruskal–Wallis test; * P

    Journal: EMBO Molecular Medicine

    Article Title: Endothelial MT1‐ MMP targeting limits intussusceptive angiogenesis and colitis via TSP1/nitric oxide axis

    doi: 10.15252/emmm.201910862

    Figure Lengend Snippet: Identification of TSP 1 cleavage sites for MT 1‐ MMP Western blot of TSP1 expression (developed with an antibody against an epitope nearby the N‐terminus; Lee et al , 2006 ) in lysates from siCtrl and siMT1‐silenced HUVEC. MT1‐MMP and tubulin are included as silencing and loading controls, respectively. The arrowhead marks full‐length TSP1 and the asterisk the N‐terminal TSP1 fragment. Western blot of in vitro digested TSP1 (developed with the same antibody as in A) incubated with increasing amounts of recombinant human MT1‐MMP catalytic domain. rhMT1‐MMP catalytic domain is also included. The arrowhead marks full‐length TSP1 and the asterisk the N‐terminal TSP1 fragment generated by MT1‐MMP cleavage. In silico model of the membrane‐anchored MT1‐MMP dimer (blue/orange) and TSP1 type 1 repeat domains 2 and 3 (green). Yellow marks the catalytic pocket in the MT1‐MMP protease, and red indicates the two selected cleavage sites in TSP1. Scheme depicting the TSP1 domain structure with the binding sequences to CD36, CD47, and αvβ3 integrin, as well as the positions of the identified cleavage sites for MT1‐MMP. DAF‐FM mean fluorescence intensity (MFI) in HUVEC expressing MT1‐MMP siRNA and left untreated or treated with 200 ng of full‐length TSP1 or the E123CaG‐1 fragment; n = 128–184 cells analyzed per condition in two independent experiments. Data are shown as individual cell values and mean ± SEM and were tested by the Kruskal–Wallis test; * P

    Article Snippet: Briefly, after fat removal under a microscope, aortas were incubated for 5 min at 37°C in collagenase solution (collagenase type I, 3.33 mg/ml, Worthington, LS004194), thus allowing removal of the adventitia with forceps.

    Techniques: Western Blot, Expressing, In Vitro, Incubation, Recombinant, Generated, In Silico, Binding Assay, Fluorescence

    Product of DSP protein coated on glass slides. A . Coomassie-stained SDS-PAGE gel for analysis of expression of the recombinant COOH-terminal dentin sialoprotein (rC-DSP) protein. The sample in DL21 cells was grown 3 h with 1 mM IPTG induction after reaching O.D.600 of 0.6. The rC-DSP was purified by the column described in the materials and methods. B . Expression of purified rC-DSP was confirmed by Western blotting analysis using goat polyclonal anti-DSP antibody (Santa Cruz Biotechnology Inc.). D - E . Collagen type I and rC-DSP proteins were coated on glass slides for overnight at 37°C. For scanning electron microscopy, the samples were washed and dried as well as treated with sodium deoxycholate. Then the samples were observed under scanning electron microscope (SEM). Fibril matrix was visible on the collagen type I coated slide ( D ) and rC-DSP coated slide ( E ), but no control slide ( C ). Also, there were different morphologies between rC-DSP and collagen type I.

    Journal: PLoS ONE

    Article Title: Domain of Dentine Sialoprotein Mediates Proliferation and Differentiation of Human Periodontal Ligament Stem Cells

    doi: 10.1371/journal.pone.0081655

    Figure Lengend Snippet: Product of DSP protein coated on glass slides. A . Coomassie-stained SDS-PAGE gel for analysis of expression of the recombinant COOH-terminal dentin sialoprotein (rC-DSP) protein. The sample in DL21 cells was grown 3 h with 1 mM IPTG induction after reaching O.D.600 of 0.6. The rC-DSP was purified by the column described in the materials and methods. B . Expression of purified rC-DSP was confirmed by Western blotting analysis using goat polyclonal anti-DSP antibody (Santa Cruz Biotechnology Inc.). D - E . Collagen type I and rC-DSP proteins were coated on glass slides for overnight at 37°C. For scanning electron microscopy, the samples were washed and dried as well as treated with sodium deoxycholate. Then the samples were observed under scanning electron microscope (SEM). Fibril matrix was visible on the collagen type I coated slide ( D ) and rC-DSP coated slide ( E ), but no control slide ( C ). Also, there were different morphologies between rC-DSP and collagen type I.

    Article Snippet: These cells were digested for 1 h at 37°C in a solution of 3 mg⁄ml collagenase type I and 4 mg⁄ml of dispase (Worthington Biochem, Freehold, NJ).

    Techniques: Staining, SDS Page, Expressing, Recombinant, Purification, Western Blot, Electron Microscopy, Microscopy

    [A] Digestion of BAT with collagenase I produces an adipose fraction harboring brown adipocytes and a stromal fraction composed primarily of endothelium separated by a fluid portion. [B] Deep-red fluorescence intensity images of centrifugation tubes containing

    Journal: Journal of materials chemistry. B, Materials for biology and medicine

    Article Title: Fluorescence Imaging of Interscapular Brown Adipose Tissue in Living Mice †

    doi: 10.1039/C4TB01914H

    Figure Lengend Snippet: [A] Digestion of BAT with collagenase I produces an adipose fraction harboring brown adipocytes and a stromal fraction composed primarily of endothelium separated by a fluid portion. [B] Deep-red fluorescence intensity images of centrifugation tubes containing

    Article Snippet: The minced tissue was digested with 2 mg/ml Collagenase I (Worthington Biochemical Corporation) in Hanks' Balanced Salt Solution (HBSS) (1.3 mM CaCl2 , 0.5 mM MgCl2 •6H2 O, 0.5 mM MgSO4 •7H2 O, 5.3 mM KCl, 0.40 mM KH2 PO4 , 4.2 mM NaHCO3 , 140 mM, NaCl, 0.3 mM Na2 HPO4 , pH 7.5) at 37 °C for 2 hours.

    Techniques: Fluorescence, Centrifugation