dispase  (Worthington Biochemical)


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    Name:
    Neutral Protease Dispase Purified
    Description:
    Animal Origin Free Chromatographically purified A lyophilized powder
    Catalog Number:
    ls02100
    Price:
    70
    Size:
    10 mg
    Source:
    Bacillus polymyxa
    Cas Number:
    42613.33.2
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    Structured Review

    Worthington Biochemical dispase
    Two distinct cell fragments found within a myofibrillar pellet after homogenization and centrifugation of <t>dispase</t> pellet (Scale line = 2μm) in panel (a) and (b). The sarcolemma and interfibrillar (IFM) mitochondria are identified.
    Animal Origin Free Chromatographically purified A lyophilized powder
    https://www.bioz.com/result/dispase/product/Worthington Biochemical
    Average 97 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    dispase - by Bioz Stars, 2021-01
    97/100 stars

    Images

    1) Product Images from "Isolation of mitochondrial subpopulations from skeletal muscle: optimizing recovery and preserving integrity."

    Article Title: Isolation of mitochondrial subpopulations from skeletal muscle: optimizing recovery and preserving integrity.

    Journal: Acta physiologica (Oxford, England)

    doi: 10.1111/apha.13182

    Two distinct cell fragments found within a myofibrillar pellet after homogenization and centrifugation of dispase pellet (Scale line = 2μm) in panel (a) and (b). The sarcolemma and interfibrillar (IFM) mitochondria are identified.
    Figure Legend Snippet: Two distinct cell fragments found within a myofibrillar pellet after homogenization and centrifugation of dispase pellet (Scale line = 2μm) in panel (a) and (b). The sarcolemma and interfibrillar (IFM) mitochondria are identified.

    Techniques Used: Homogenization, Centrifugation

    Two distinct fragments of a cell found within the skeletal muscle pellet treated with dispase protease (Scale line = 2μm) in panel (a) and (b). The sarcolemma, subsarcolemmal (SSM) and interfibrillar (IFM) mitochondria are identified.
    Figure Legend Snippet: Two distinct fragments of a cell found within the skeletal muscle pellet treated with dispase protease (Scale line = 2μm) in panel (a) and (b). The sarcolemma, subsarcolemmal (SSM) and interfibrillar (IFM) mitochondria are identified.

    Techniques Used:

    2) Product Images from "Conformational Changes in the Adenovirus Hexon Subunit Responsible for Regulating Cytoplasmic Dynein Recruitment"

    Article Title: Conformational Changes in the Adenovirus Hexon Subunit Responsible for Regulating Cytoplasmic Dynein Recruitment

    Journal: Journal of Virology

    doi: 10.1128/JVI.02889-14

    Dispase treatment reduces capsid redistribution to the nucleus. (A) pH-dependent dispase cleavage of AdV5 capsid hexon. Purified AdV5 capsids were treated with dispase at pH 7.4 or pH 4.4 or kept at pH 4.4 alone before being boiled in PSB and subjected
    Figure Legend Snippet: Dispase treatment reduces capsid redistribution to the nucleus. (A) pH-dependent dispase cleavage of AdV5 capsid hexon. Purified AdV5 capsids were treated with dispase at pH 7.4 or pH 4.4 or kept at pH 4.4 alone before being boiled in PSB and subjected

    Techniques Used: Purification

    Dispase hydrolysis inhibits low-pH effects on hexon structure and dynein binding. (A) Purified hexon was tested for dissociation after dispase treatment. Dispase exposure of hexon at low pH resulted in two major digestion products (85 kDa [I] and 15 kDa
    Figure Legend Snippet: Dispase hydrolysis inhibits low-pH effects on hexon structure and dynein binding. (A) Purified hexon was tested for dissociation after dispase treatment. Dispase exposure of hexon at low pH resulted in two major digestion products (85 kDa [I] and 15 kDa

    Techniques Used: Binding Assay, Purification

    The AdV5 hexon HVR1 mutant is inhibited in dynein binding and cytoplasmic transport. (A) Dispase insensitivity of mutant hexon. Immunopurified hexons of wild-type (WT) AdV5, AdV5HVR48(1), and WT AdV48 were tested for dissociation after dispase treatment.
    Figure Legend Snippet: The AdV5 hexon HVR1 mutant is inhibited in dynein binding and cytoplasmic transport. (A) Dispase insensitivity of mutant hexon. Immunopurified hexons of wild-type (WT) AdV5, AdV5HVR48(1), and WT AdV48 were tested for dissociation after dispase treatment.

    Techniques Used: Mutagenesis, Binding Assay

    Related Articles

    Incubation:

    Article Title: ADAM17 Deletion in Thymic Epithelial Cells Alters Aire Expression without Affecting T Cell Developmental Progression
    Article Snippet: .. After 4 digestions, 0.125% (w/v) dispase (Worthington Biochemical) was added to the digestion buffer and thymi were incubated for an additional 15 minutes. .. After the final digestion, cells were incubated in PBS containing 5 mM EDTA + 1% FCS + 0.02% (w/v) NaN3 for 10 minutes on ice.

    Article Title: A Selective Cell Population from Dermis Strengthens Bone Regeneration
    Article Snippet: .. Next, the specimen was incubated in 8 U/ml Dispase (Worthington Biochemical, Lakewood, NJ, http://www.worthington-biochem.com ) at 4°C overnight. .. The dermis was separated from the epidermis, cut into small pieces, and further digested in 2 mg/ml collagenase (NB4 [PZ activity, 0.170 U/mg]; SERVA Electrophoresis, Germany, http://www.serva.de ), which was diluted in Dulbecco's modified Eagle's medium–low glucose (DMEM‐lg) (Thermo Fisher Scientific Life Sciences, Waltham, MA, http://www.thermofisher.com ) at 37°C for 3 hours in a shaking water bath.

    Article Title: High-resolution transcriptional dissection of in vivo Atoh1-mediated hair cell conversion in mature cochleae identifies Isl1 as a co-reprogramming factor
    Article Snippet: .. Single-cell RNA-seq Cochleae were dissected out and incubated in solution (50% accutase (Innovative Cell Technologies, San Diego), 0.02% Trypsin(Thermofisher), 125 μg/ml Thermolysin (SIGMA-ALDRICH)) at 37°C for 3 min. 0.02 mg/ml collagenase IV (SIGMA-ALDRICH) and dispase (Worthington Biochemicals Corp) were further added to the enzyme solution and incubated for 4 min at 37°C. ..

    Article Title: Homology‐guided mutational analysis reveals the functional requirements for antinociceptive specificity of collapsin response mediator protein 2‐derived peptides
    Article Snippet: .. DRGs were then collected, trimmed at their roots and digested in 3 mL bicarbonate‐free, serum‐free, sterile DMEM (Cat#11965; Thermo Fisher Scientific) solution containing neutral protease (3.125 mg·mL−1 , Cat#LS02104, Worthington, Lakewood, NJ, USA) and collagenase Type I (5 mg·mL−1 , Cat# , Worthington) and incubated for 60 min at 37°C under gentle agitation. .. Dissociated DRG neurons (~1.5 × 106 ) were then gently centrifuged to collect cells and washed with DRG media DMEM containing 1% penicillin/streptomycin sulfate from 10 000 μg·mL−1 stock, 30 ng·mL−1 nerve growth factor and 10% fetal bovine serum (Hyclone) before plating onto poly‐ d ‐lysine‐ and laminin‐coated glass 12 or 15 mm coverslips.

    Article Title: Conformational Changes in the Adenovirus Hexon Subunit Responsible for Regulating Cytoplasmic Dynein Recruitment
    Article Snippet: .. For controlled proteolysis, hexon or AdV capsids were incubated with a 6-fold molar excess of dispase (neutral protease; Worthington Biochemicals, Freehold, NJ) over hexon in dispase buffer (100 mM Trizma-maleate, 120 mM NaCl, 2.5 mM CaCl2 ), and the pH was adjusted to either pH 7.4 (neutral) or pH 4.4 (acidic) for 5 min at 37°C until the reaction was stopped by the addition of either protein sample buffer (PSB) or 5 mM EDTA to the mixture. .. Sedimentation analysis of hexon was performed on linear 5 to 20% sucrose gradients of a volume of 1.4 ml in Tris-maleate buffer (50 mM Trizma-maleate, 10 mM NaCl, 1 mM EDTA, and 0.1% Tween 20) at the indicated pH values.

    RNA Sequencing Assay:

    Article Title: High-resolution transcriptional dissection of in vivo Atoh1-mediated hair cell conversion in mature cochleae identifies Isl1 as a co-reprogramming factor
    Article Snippet: .. Single-cell RNA-seq Cochleae were dissected out and incubated in solution (50% accutase (Innovative Cell Technologies, San Diego), 0.02% Trypsin(Thermofisher), 125 μg/ml Thermolysin (SIGMA-ALDRICH)) at 37°C for 3 min. 0.02 mg/ml collagenase IV (SIGMA-ALDRICH) and dispase (Worthington Biochemicals Corp) were further added to the enzyme solution and incubated for 4 min at 37°C. ..

    Chloramphenicol Acetyltransferase Assay:

    Article Title: Homology‐guided mutational analysis reveals the functional requirements for antinociceptive specificity of collapsin response mediator protein 2‐derived peptides
    Article Snippet: .. DRGs were then collected, trimmed at their roots and digested in 3 mL bicarbonate‐free, serum‐free, sterile DMEM (Cat11965; Thermo Fisher Scientific) solution containing neutral protease (3.125 mg·mL−1 , Cat#LS02104, Worthington, Lakewood, NJ, USA) and collagenase Type I (5 mg·mL−1 , Cat# , Worthington) and incubated for 60 min at 37°C under gentle agitation. .. Dissociated DRG neurons (~1.5 × 106 ) were then gently centrifuged to collect cells and washed with DRG media DMEM containing 1% penicillin/streptomycin sulfate from 10 000 μg·mL−1 stock, 30 ng·mL−1 nerve growth factor and 10% fetal bovine serum (Hyclone) before plating onto poly‐ d ‐lysine‐ and laminin‐coated glass 12 or 15 mm coverslips.

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  • 97
    Worthington Biochemical dispase
    Two distinct cell fragments found within a myofibrillar pellet after homogenization and centrifugation of <t>dispase</t> pellet (Scale line = 2μm) in panel (a) and (b). The sarcolemma and interfibrillar (IFM) mitochondria are identified.
    Dispase, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 97/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dispase/product/Worthington Biochemical
    Average 97 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    dispase - by Bioz Stars, 2021-01
    97/100 stars
      Buy from Supplier

    90
    Worthington Biochemical colg plus colh plus dispase ii
    Satellite cells isolated using recombinant collagenase retain surface antigens. (A) After mouse muscles were processed with <t>ColG</t> and <t>ColH,</t> mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression. The purple box represents the satellite cell population. The SM/C-2.6 + fraction was divided into the high positive fraction (pink box) and the low positive fraction (blue box). (B) Expression of integrins on the cell surface was evaluated by flow cytometry. Green lines indicate α7 and β1 integrin expression pattern. Gray histograms represent the matched control. (C) After mouse muscles were processed with conventional collagenase II, mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression. The purple box represents the satellite cell population. (D) Expression of integrins on the cell surface was evaluated by flow cytometry. Green lines indicate α7 and β1 integrin expression patterns. Gray histograms represent the matched control. (E) Quantitative analysis of mRNA expression of Pax7. The mRNA expression of each gene was normalized using HPRT mRNA expression. n = 3. Error bars, s.e.m.; ***p
    Colg Plus Colh Plus Dispase Ii, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/colg plus colh plus dispase ii/product/Worthington Biochemical
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    colg plus colh plus dispase ii - by Bioz Stars, 2021-01
    90/100 stars
      Buy from Supplier

    Image Search Results


    Two distinct cell fragments found within a myofibrillar pellet after homogenization and centrifugation of dispase pellet (Scale line = 2μm) in panel (a) and (b). The sarcolemma and interfibrillar (IFM) mitochondria are identified.

    Journal: Acta physiologica (Oxford, England)

    Article Title: Isolation of mitochondrial subpopulations from skeletal muscle: optimizing recovery and preserving integrity.

    doi: 10.1111/apha.13182

    Figure Lengend Snippet: Two distinct cell fragments found within a myofibrillar pellet after homogenization and centrifugation of dispase pellet (Scale line = 2μm) in panel (a) and (b). The sarcolemma and interfibrillar (IFM) mitochondria are identified.

    Article Snippet: Reagents: Dispase (neutral protease) was obtained from Worthington Biochemical Corporation (Lakewood, NJ, USA).

    Techniques: Homogenization, Centrifugation

    Two distinct fragments of a cell found within the skeletal muscle pellet treated with dispase protease (Scale line = 2μm) in panel (a) and (b). The sarcolemma, subsarcolemmal (SSM) and interfibrillar (IFM) mitochondria are identified.

    Journal: Acta physiologica (Oxford, England)

    Article Title: Isolation of mitochondrial subpopulations from skeletal muscle: optimizing recovery and preserving integrity.

    doi: 10.1111/apha.13182

    Figure Lengend Snippet: Two distinct fragments of a cell found within the skeletal muscle pellet treated with dispase protease (Scale line = 2μm) in panel (a) and (b). The sarcolemma, subsarcolemmal (SSM) and interfibrillar (IFM) mitochondria are identified.

    Article Snippet: Reagents: Dispase (neutral protease) was obtained from Worthington Biochemical Corporation (Lakewood, NJ, USA).

    Techniques:

    Dispase treatment reduces capsid redistribution to the nucleus. (A) pH-dependent dispase cleavage of AdV5 capsid hexon. Purified AdV5 capsids were treated with dispase at pH 7.4 or pH 4.4 or kept at pH 4.4 alone before being boiled in PSB and subjected

    Journal: Journal of Virology

    Article Title: Conformational Changes in the Adenovirus Hexon Subunit Responsible for Regulating Cytoplasmic Dynein Recruitment

    doi: 10.1128/JVI.02889-14

    Figure Lengend Snippet: Dispase treatment reduces capsid redistribution to the nucleus. (A) pH-dependent dispase cleavage of AdV5 capsid hexon. Purified AdV5 capsids were treated with dispase at pH 7.4 or pH 4.4 or kept at pH 4.4 alone before being boiled in PSB and subjected

    Article Snippet: For controlled proteolysis, hexon or AdV capsids were incubated with a 6-fold molar excess of dispase (neutral protease; Worthington Biochemicals, Freehold, NJ) over hexon in dispase buffer (100 mM Trizma-maleate, 120 mM NaCl, 2.5 mM CaCl2 ), and the pH was adjusted to either pH 7.4 (neutral) or pH 4.4 (acidic) for 5 min at 37°C until the reaction was stopped by the addition of either protein sample buffer (PSB) or 5 mM EDTA to the mixture.

    Techniques: Purification

    Dispase hydrolysis inhibits low-pH effects on hexon structure and dynein binding. (A) Purified hexon was tested for dissociation after dispase treatment. Dispase exposure of hexon at low pH resulted in two major digestion products (85 kDa [I] and 15 kDa

    Journal: Journal of Virology

    Article Title: Conformational Changes in the Adenovirus Hexon Subunit Responsible for Regulating Cytoplasmic Dynein Recruitment

    doi: 10.1128/JVI.02889-14

    Figure Lengend Snippet: Dispase hydrolysis inhibits low-pH effects on hexon structure and dynein binding. (A) Purified hexon was tested for dissociation after dispase treatment. Dispase exposure of hexon at low pH resulted in two major digestion products (85 kDa [I] and 15 kDa

    Article Snippet: For controlled proteolysis, hexon or AdV capsids were incubated with a 6-fold molar excess of dispase (neutral protease; Worthington Biochemicals, Freehold, NJ) over hexon in dispase buffer (100 mM Trizma-maleate, 120 mM NaCl, 2.5 mM CaCl2 ), and the pH was adjusted to either pH 7.4 (neutral) or pH 4.4 (acidic) for 5 min at 37°C until the reaction was stopped by the addition of either protein sample buffer (PSB) or 5 mM EDTA to the mixture.

    Techniques: Binding Assay, Purification

    The AdV5 hexon HVR1 mutant is inhibited in dynein binding and cytoplasmic transport. (A) Dispase insensitivity of mutant hexon. Immunopurified hexons of wild-type (WT) AdV5, AdV5HVR48(1), and WT AdV48 were tested for dissociation after dispase treatment.

    Journal: Journal of Virology

    Article Title: Conformational Changes in the Adenovirus Hexon Subunit Responsible for Regulating Cytoplasmic Dynein Recruitment

    doi: 10.1128/JVI.02889-14

    Figure Lengend Snippet: The AdV5 hexon HVR1 mutant is inhibited in dynein binding and cytoplasmic transport. (A) Dispase insensitivity of mutant hexon. Immunopurified hexons of wild-type (WT) AdV5, AdV5HVR48(1), and WT AdV48 were tested for dissociation after dispase treatment.

    Article Snippet: For controlled proteolysis, hexon or AdV capsids were incubated with a 6-fold molar excess of dispase (neutral protease; Worthington Biochemicals, Freehold, NJ) over hexon in dispase buffer (100 mM Trizma-maleate, 120 mM NaCl, 2.5 mM CaCl2 ), and the pH was adjusted to either pH 7.4 (neutral) or pH 4.4 (acidic) for 5 min at 37°C until the reaction was stopped by the addition of either protein sample buffer (PSB) or 5 mM EDTA to the mixture.

    Techniques: Mutagenesis, Binding Assay

    Satellite cells isolated using recombinant collagenase retain surface antigens. (A) After mouse muscles were processed with ColG and ColH, mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression. The purple box represents the satellite cell population. The SM/C-2.6 + fraction was divided into the high positive fraction (pink box) and the low positive fraction (blue box). (B) Expression of integrins on the cell surface was evaluated by flow cytometry. Green lines indicate α7 and β1 integrin expression pattern. Gray histograms represent the matched control. (C) After mouse muscles were processed with conventional collagenase II, mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression. The purple box represents the satellite cell population. (D) Expression of integrins on the cell surface was evaluated by flow cytometry. Green lines indicate α7 and β1 integrin expression patterns. Gray histograms represent the matched control. (E) Quantitative analysis of mRNA expression of Pax7. The mRNA expression of each gene was normalized using HPRT mRNA expression. n = 3. Error bars, s.e.m.; ***p

    Journal: Regenerative Therapy

    Article Title: Technical advantage of recombinant collagenase for isolation of muscle stem cells

    doi: 10.1016/j.reth.2017.06.001

    Figure Lengend Snippet: Satellite cells isolated using recombinant collagenase retain surface antigens. (A) After mouse muscles were processed with ColG and ColH, mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression. The purple box represents the satellite cell population. The SM/C-2.6 + fraction was divided into the high positive fraction (pink box) and the low positive fraction (blue box). (B) Expression of integrins on the cell surface was evaluated by flow cytometry. Green lines indicate α7 and β1 integrin expression pattern. Gray histograms represent the matched control. (C) After mouse muscles were processed with conventional collagenase II, mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression. The purple box represents the satellite cell population. (D) Expression of integrins on the cell surface was evaluated by flow cytometry. Green lines indicate α7 and β1 integrin expression patterns. Gray histograms represent the matched control. (E) Quantitative analysis of mRNA expression of Pax7. The mRNA expression of each gene was normalized using HPRT mRNA expression. n = 3. Error bars, s.e.m.; ***p

    Article Snippet: After mouse muscles had been processed with ColG plus ColH plus Dispase II, ColG plus ColH, (i) collagenase type II (Worthington), (ii) collagenase type II (Gibco), (iii) collagenase type A (Worthington), (iv) collagenase STEMxyme1 (Worthington), and (v) collagenase STEMxyme2 (Worthington), mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression.

    Techniques: Isolation, Recombinant, FACS, Expressing, Flow Cytometry, Cytometry

    Transplanted satellite cells digested with recombinant collagenase have an improved regenerative capacity. (A) Comparison of the muscle regeneration efficiency between cells digested with ColG and ColH and those digested with conventional collagenase II. EGFP + satellite cells were sorted and injected into C57BL/6 mouse TA muscles. The muscles were treated with CTX 24 h before cell transplantation. A total of 5.0 × 10 5 cells were injected per TA muscle. Two weeks after the injection, cross-sections were stained with an anti-laminin α2 antibody (white) and DAPI [42] . (B) Enlarged view of Fig. A. (C) The number of regenerated GFP+ fibers. n = 3. Error bars, s.e.m.; *p

    Journal: Regenerative Therapy

    Article Title: Technical advantage of recombinant collagenase for isolation of muscle stem cells

    doi: 10.1016/j.reth.2017.06.001

    Figure Lengend Snippet: Transplanted satellite cells digested with recombinant collagenase have an improved regenerative capacity. (A) Comparison of the muscle regeneration efficiency between cells digested with ColG and ColH and those digested with conventional collagenase II. EGFP + satellite cells were sorted and injected into C57BL/6 mouse TA muscles. The muscles were treated with CTX 24 h before cell transplantation. A total of 5.0 × 10 5 cells were injected per TA muscle. Two weeks after the injection, cross-sections were stained with an anti-laminin α2 antibody (white) and DAPI [42] . (B) Enlarged view of Fig. A. (C) The number of regenerated GFP+ fibers. n = 3. Error bars, s.e.m.; *p

    Article Snippet: After mouse muscles had been processed with ColG plus ColH plus Dispase II, ColG plus ColH, (i) collagenase type II (Worthington), (ii) collagenase type II (Gibco), (iii) collagenase type A (Worthington), (iv) collagenase STEMxyme1 (Worthington), and (v) collagenase STEMxyme2 (Worthington), mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression.

    Techniques: Recombinant, Injection, Transplantation Assay, Staining

    Recombinant collagenase causes less damage to muscle mononuclear cells. (A) After mouse muscles were processed with ColG and ColH and conventional collagenase II, mononuclear cells were isolated from these muscles and subjected to FACS analysis. A PI-FACS histogram was generated to detect membrane damage. (B) Quantitative analysis of the percentage of PI + dead cells. n = 3. Error bars, s.e.m.; *p

    Journal: Regenerative Therapy

    Article Title: Technical advantage of recombinant collagenase for isolation of muscle stem cells

    doi: 10.1016/j.reth.2017.06.001

    Figure Lengend Snippet: Recombinant collagenase causes less damage to muscle mononuclear cells. (A) After mouse muscles were processed with ColG and ColH and conventional collagenase II, mononuclear cells were isolated from these muscles and subjected to FACS analysis. A PI-FACS histogram was generated to detect membrane damage. (B) Quantitative analysis of the percentage of PI + dead cells. n = 3. Error bars, s.e.m.; *p

    Article Snippet: After mouse muscles had been processed with ColG plus ColH plus Dispase II, ColG plus ColH, (i) collagenase type II (Worthington), (ii) collagenase type II (Gibco), (iii) collagenase type A (Worthington), (iv) collagenase STEMxyme1 (Worthington), and (v) collagenase STEMxyme2 (Worthington), mononuclear cells were isolated from these muscles and subjected to FACS analysis of SM/C-2.6 expression.

    Techniques: Recombinant, Isolation, FACS, Generated