fibronectin  (Millipore)

 
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    Name:
    Fibronectin bovine plasma
    Description:
    Fibronectin FN is a multifunctional glycoprotein the gene of which is localized to human chromosome 2q34 36 This gene spans 75kb and contains 50 exons It exists as two major isoforms one soluble and one insoluble form The former is present in plasma whereas the insoluble form resides in tissues and extracellular matrix ECM of cartilage There are around 20 different forms of FN due to alternative splicing of a variable region and two type III exons called Extra Domains A and B
    Catalog Number:
    f4759
    Price:
    None
    Applications:
    Fibronectin from bovine plasma is used for the following applications:. Used for coating the glass coverslips for the culture of decidual stromal cells (DEC). Cell movement assays (culture plates were coated with fibronectin). Cell spreading and immunofluorescence . Protein specificity. Integration of sensor films into microfluidic chips. Histological and Immunohistochemical (IHC) analyses. Used in primary cell cultures from patients with lung carcinoma
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    Structured Review

    Millipore fibronectin
    Clonogenic adult progenitor cells were isolated from normal and osteoarthritic cartilage. ( A , B ) <t>Fibronectin-adhered</t> colonies from normal (N-CPC) and osteoarthritic (OA-CPC) cartilage were stained with crystal violet dye. ( C ) Number of colonies were quantified based on initial seeding density, box plots demonstrate the percentage mean of clonogenic cells from OA cartilage digests (n = 11) was 2.80% ( ±0.29%) compared to 1.47% ( ±0.16%) for normal cartilage digests (n = 11). The approximately 2-fold increase was statistically significant (*) using T-test (P = 0.0001).
    Fibronectin FN is a multifunctional glycoprotein the gene of which is localized to human chromosome 2q34 36 This gene spans 75kb and contains 50 exons It exists as two major isoforms one soluble and one insoluble form The former is present in plasma whereas the insoluble form resides in tissues and extracellular matrix ECM of cartilage There are around 20 different forms of FN due to alternative splicing of a variable region and two type III exons called Extra Domains A and B
    https://www.bioz.com/result/fibronectin/product/Millipore
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    fibronectin - by Bioz Stars, 2021-03
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    Images

    1) Product Images from "Characterisation of a divergent progenitor cell sub-populations in human osteoarthritic cartilage: the role of telomere erosion and replicative senescence"

    Article Title: Characterisation of a divergent progenitor cell sub-populations in human osteoarthritic cartilage: the role of telomere erosion and replicative senescence

    Journal: Scientific Reports

    doi: 10.1038/srep41421

    Clonogenic adult progenitor cells were isolated from normal and osteoarthritic cartilage. ( A , B ) Fibronectin-adhered colonies from normal (N-CPC) and osteoarthritic (OA-CPC) cartilage were stained with crystal violet dye. ( C ) Number of colonies were quantified based on initial seeding density, box plots demonstrate the percentage mean of clonogenic cells from OA cartilage digests (n = 11) was 2.80% ( ±0.29%) compared to 1.47% ( ±0.16%) for normal cartilage digests (n = 11). The approximately 2-fold increase was statistically significant (*) using T-test (P = 0.0001).
    Figure Legend Snippet: Clonogenic adult progenitor cells were isolated from normal and osteoarthritic cartilage. ( A , B ) Fibronectin-adhered colonies from normal (N-CPC) and osteoarthritic (OA-CPC) cartilage were stained with crystal violet dye. ( C ) Number of colonies were quantified based on initial seeding density, box plots demonstrate the percentage mean of clonogenic cells from OA cartilage digests (n = 11) was 2.80% ( ±0.29%) compared to 1.47% ( ±0.16%) for normal cartilage digests (n = 11). The approximately 2-fold increase was statistically significant (*) using T-test (P = 0.0001).

    Techniques Used: Isolation, Staining

    2) Product Images from "Breast Cancer Antiestrogen Resistance 3 (BCAR3) – p130Cas Interactions Promote Adhesion Disassembly and Invasion in Breast Cancer Cells"

    Article Title: Breast Cancer Antiestrogen Resistance 3 (BCAR3) – p130Cas Interactions Promote Adhesion Disassembly and Invasion in Breast Cancer Cells

    Journal: Oncogene

    doi: 10.1038/onc.2016.123

    BCAR3/Cas interactions are required for BCAR3 dependent Rac activity BT549 cells were transfected with plasmids encoding GFP, GFP-WT BCAR3, or GFP-L744E/R748E BCAR3 and incubated for 24 hours. Cells were held in suspension for 90 minutes, then plated on 10μg/ml fibronectin for 1 hour. (A) GTP-bound Rac1 was isolated from whole cell lysates by incubation with PAK-1-binding domain agarose. Bound proteins (middle panel) and total Rac1 (bottom panel) were detected by immunoblotting with a Rac1 antibody, and BCAR3 expression was confirmed with a BCAR3-specific antibody (top panel). (B) Quantification of the relative GTP-Rac1 level is shown. Data presented are the mean ± SEM of 3 independent experiments.
    Figure Legend Snippet: BCAR3/Cas interactions are required for BCAR3 dependent Rac activity BT549 cells were transfected with plasmids encoding GFP, GFP-WT BCAR3, or GFP-L744E/R748E BCAR3 and incubated for 24 hours. Cells were held in suspension for 90 minutes, then plated on 10μg/ml fibronectin for 1 hour. (A) GTP-bound Rac1 was isolated from whole cell lysates by incubation with PAK-1-binding domain agarose. Bound proteins (middle panel) and total Rac1 (bottom panel) were detected by immunoblotting with a Rac1 antibody, and BCAR3 expression was confirmed with a BCAR3-specific antibody (top panel). (B) Quantification of the relative GTP-Rac1 level is shown. Data presented are the mean ± SEM of 3 independent experiments.

    Techniques Used: Activity Assay, Transfection, Incubation, Isolation, Binding Assay, Expressing

    BCAR3 localization in adhesions does not require a functional SH2 domain or interaction with Cas (A) BT549 cells were transfected with plasmids encoding WT GFP-BCAR3, R171V GFP-BCAR3, L744E/R748E GFP-BCAR3 or R171V/L744E/R748E GFP-BCAR3. Cells were incubated for 24 hours prior to plating on 10μg/ml fibronectin-coated coverslips for 4 hours. Cells were fixed, stained with polyclonal Cas antibodies (panels b, e, h, k), and subjected to TIRF microscopy to visualize adhesions. Merged images are shown in the right panels and insets show higher magnifications of the designated areas. (B) BT549 cells were transfected with plasmids encoding GFP, WT GFP-BCAR3, R171V GFP-BCAR3, L744E/R748E GFP-BCAR3 or R171V/L744E/R748E GFP-BCAR3 and lysed in a non-denaturing buffer 24 hours post-transfection. Total cell protein and Cas immune complexes (generated from 50X more protein than the lysates) were immunoblotted with antibodies to detect the indicated proteins. Left and right panels are identical exposures from the same film.
    Figure Legend Snippet: BCAR3 localization in adhesions does not require a functional SH2 domain or interaction with Cas (A) BT549 cells were transfected with plasmids encoding WT GFP-BCAR3, R171V GFP-BCAR3, L744E/R748E GFP-BCAR3 or R171V/L744E/R748E GFP-BCAR3. Cells were incubated for 24 hours prior to plating on 10μg/ml fibronectin-coated coverslips for 4 hours. Cells were fixed, stained with polyclonal Cas antibodies (panels b, e, h, k), and subjected to TIRF microscopy to visualize adhesions. Merged images are shown in the right panels and insets show higher magnifications of the designated areas. (B) BT549 cells were transfected with plasmids encoding GFP, WT GFP-BCAR3, R171V GFP-BCAR3, L744E/R748E GFP-BCAR3 or R171V/L744E/R748E GFP-BCAR3 and lysed in a non-denaturing buffer 24 hours post-transfection. Total cell protein and Cas immune complexes (generated from 50X more protein than the lysates) were immunoblotted with antibodies to detect the indicated proteins. Left and right panels are identical exposures from the same film.

    Techniques Used: Functional Assay, Transfection, Incubation, Staining, Microscopy, Generated

    Direct interaction between BCAR3 and Cas is required for efficient dissociation of BCAR3 from adhesions BT549 breast cancer cells were co-transfected with plasmids encoding WT or L744E /R748E (L/R) GFP-BCAR3 and mCherry-Cas, incubated for 24 hours, and then plated on 2μg/ml fibronectin-coated glass-bottomed TIRF dishes for 30–40 minutes prior to visualizing adhesion dynamics via live-imaging TIRF microscopy. (A, B) Representative time-lapse images show incorporation into adhesions (arrowheads) and dissociation (arrows) of the indicated proteins over the specified time course. Scale bars = 100μm. (C, D) Representative fluorescence intensity time tracings of BCAR3 (black) and Cas (magenta) present in adhesions from cells expressing WT (C) or L744ER748E (D) GFP-BCAR3. Dashed boxes/line indicate the incorporation (I), stability (S), and dissociation (D) phases of adhesion dynamics. (E, F) Quantitative analysis of the incorporation (E) and dissociation (F) rates of WT GFP-BCAR3 (bar 1), L744E/R748E (L/R) GFP-BCAR3 (bar 2), Cas co-expressed with WT GFP-BCAR3 (bar 3), and Cas co-expressed with L744E/R748E (L/R) GFP-BCAR3 (bar 4). Data presented are the mean ± SEM of 35 adhesions from 3 WT and L744E/R748E GFP-BCAR3 expressing cells from 3 independent experiments. *, p
    Figure Legend Snippet: Direct interaction between BCAR3 and Cas is required for efficient dissociation of BCAR3 from adhesions BT549 breast cancer cells were co-transfected with plasmids encoding WT or L744E /R748E (L/R) GFP-BCAR3 and mCherry-Cas, incubated for 24 hours, and then plated on 2μg/ml fibronectin-coated glass-bottomed TIRF dishes for 30–40 minutes prior to visualizing adhesion dynamics via live-imaging TIRF microscopy. (A, B) Representative time-lapse images show incorporation into adhesions (arrowheads) and dissociation (arrows) of the indicated proteins over the specified time course. Scale bars = 100μm. (C, D) Representative fluorescence intensity time tracings of BCAR3 (black) and Cas (magenta) present in adhesions from cells expressing WT (C) or L744ER748E (D) GFP-BCAR3. Dashed boxes/line indicate the incorporation (I), stability (S), and dissociation (D) phases of adhesion dynamics. (E, F) Quantitative analysis of the incorporation (E) and dissociation (F) rates of WT GFP-BCAR3 (bar 1), L744E/R748E (L/R) GFP-BCAR3 (bar 2), Cas co-expressed with WT GFP-BCAR3 (bar 3), and Cas co-expressed with L744E/R748E (L/R) GFP-BCAR3 (bar 4). Data presented are the mean ± SEM of 35 adhesions from 3 WT and L744E/R748E GFP-BCAR3 expressing cells from 3 independent experiments. *, p

    Techniques Used: Transfection, Incubation, Imaging, Microscopy, Fluorescence, Expressing

    Direct interaction between BCAR3 and Cas is required for efficient dissociation of talin from adhesions BT549 invasive breast cancer cells were co-transfected with plasmids encoding WT or L744E/R748E (L/R) GFP-BCAR3 and mCherry-talin, incubated for 24 hours, and then plated on 2μg/ml fibronectin-coated glass-bottomed TIRF dishes for 30–40 minutes prior to visualizing adhesion dynamics via live-imaging TIRF. (A, B) Representative time-lapse images show incorporation into adhesions (arrowheads) and dissociation (arrows) of the indicated proteins over the specified time course. Scale bars = 100μm. (C, D) Representative fluorescence intensity time tracings of BCAR3 (black) and talin (magenta) present in adhesions from cells expressing WT (C) or L744E/R748E (L/R) GFP-BCAR3 (D). Dashed boxes/line indicate the incorporation (I), stability (S), and dissociation (D) phases of adhesion dynamics. (E, F) Quantitative analysis of the incorporation (E) and dissociation (F) rates of WT GFP-BCAR3 (bar 1), L744E/R748E (L/R) GFP-BCAR3 (bar 2), Talin co-expressed with WT GFP-BCAR3 (bar 3), and Talin co-expressed with L744E/R748E (L/R) GFP-BCAR3 (bar 4). Data presented are the mean ± SEM of ≥14 adhesions from 5 separate WT BCAR3/talin or 3 separate L744E/R748E BCAR3/talin movies generated from 3 independent experiments. *, p
    Figure Legend Snippet: Direct interaction between BCAR3 and Cas is required for efficient dissociation of talin from adhesions BT549 invasive breast cancer cells were co-transfected with plasmids encoding WT or L744E/R748E (L/R) GFP-BCAR3 and mCherry-talin, incubated for 24 hours, and then plated on 2μg/ml fibronectin-coated glass-bottomed TIRF dishes for 30–40 minutes prior to visualizing adhesion dynamics via live-imaging TIRF. (A, B) Representative time-lapse images show incorporation into adhesions (arrowheads) and dissociation (arrows) of the indicated proteins over the specified time course. Scale bars = 100μm. (C, D) Representative fluorescence intensity time tracings of BCAR3 (black) and talin (magenta) present in adhesions from cells expressing WT (C) or L744E/R748E (L/R) GFP-BCAR3 (D). Dashed boxes/line indicate the incorporation (I), stability (S), and dissociation (D) phases of adhesion dynamics. (E, F) Quantitative analysis of the incorporation (E) and dissociation (F) rates of WT GFP-BCAR3 (bar 1), L744E/R748E (L/R) GFP-BCAR3 (bar 2), Talin co-expressed with WT GFP-BCAR3 (bar 3), and Talin co-expressed with L744E/R748E (L/R) GFP-BCAR3 (bar 4). Data presented are the mean ± SEM of ≥14 adhesions from 5 separate WT BCAR3/talin or 3 separate L744E/R748E BCAR3/talin movies generated from 3 independent experiments. *, p

    Techniques Used: Transfection, Incubation, Imaging, Fluorescence, Expressing, Generated

    3) Product Images from "Src-inducible association of CrkL with procaspase-8 promotes cell migration"

    Article Title: Src-inducible association of CrkL with procaspase-8 promotes cell migration

    Journal: Cell Adhesion & Migration

    doi: 10.4161/cam.25284

    Figure 1. Identification of an interaction between Caspase-8 and Crk proteins. ( A ) Serum starved NB7 ( Casp8 −/− ) and NB7C8 (Casp8 reconstituted) cells were trypsinized and held in suspension (Susp) or allowed to attach to fibronectin for 10, 30, or 60 min and lysates probed with indicated antibodies. ( B ) NB7C8 cells were subjected to immunoprecipitation with antisera to caspase-8 after spreading on a fibronectin substrate for 30 min (FN), or after being held in suspension (Susp) and probed for indicated proteins. ( C ) Similarly treated NB7C8 cells were subjected to Crk protein-immunoprecipitation and immunoblotting for the proteins indicated. NB7 cells with genetic deletion of caspase-8 were used as controls to clearly differentiate the procaspase-8 band from precipitating Ig. ( D ) Immobilized recombinant SH2 domains of Crk-I/II, CrkL or Syk were probed with recombinant caspase-8 catalytic domain treated with recombinant Src kinase (phosphocasp-8) or not (casp-8) (mean ± SE, * P
    Figure Legend Snippet: Figure 1. Identification of an interaction between Caspase-8 and Crk proteins. ( A ) Serum starved NB7 ( Casp8 −/− ) and NB7C8 (Casp8 reconstituted) cells were trypsinized and held in suspension (Susp) or allowed to attach to fibronectin for 10, 30, or 60 min and lysates probed with indicated antibodies. ( B ) NB7C8 cells were subjected to immunoprecipitation with antisera to caspase-8 after spreading on a fibronectin substrate for 30 min (FN), or after being held in suspension (Susp) and probed for indicated proteins. ( C ) Similarly treated NB7C8 cells were subjected to Crk protein-immunoprecipitation and immunoblotting for the proteins indicated. NB7 cells with genetic deletion of caspase-8 were used as controls to clearly differentiate the procaspase-8 band from precipitating Ig. ( D ) Immobilized recombinant SH2 domains of Crk-I/II, CrkL or Syk were probed with recombinant caspase-8 catalytic domain treated with recombinant Src kinase (phosphocasp-8) or not (casp-8) (mean ± SE, * P

    Techniques Used: Immunoprecipitation, Recombinant

    Figure 2. CrkL promotes recruitment of caspase-8 to the periphery. ( A ) NB7C8 cells expressing CrkL shRNA or control shRNA were allowed to spread on fibronectin coated coverslips, then fixed cells were stained for procaspase-8 and with phalloidin to identify actin-rich adhesion ruffles, then imaged by confocal microscopy. Representative images are shown. Scale bars indicate 10 μm. ( B ) Recruitment of caspase-8 to adhesion ruffles was evaluated ( n = 20/group, mean ± SE, * P
    Figure Legend Snippet: Figure 2. CrkL promotes recruitment of caspase-8 to the periphery. ( A ) NB7C8 cells expressing CrkL shRNA or control shRNA were allowed to spread on fibronectin coated coverslips, then fixed cells were stained for procaspase-8 and with phalloidin to identify actin-rich adhesion ruffles, then imaged by confocal microscopy. Representative images are shown. Scale bars indicate 10 μm. ( B ) Recruitment of caspase-8 to adhesion ruffles was evaluated ( n = 20/group, mean ± SE, * P

    Techniques Used: Expressing, shRNA, Staining, Confocal Microscopy

    Figure 3. Role of Src kinase in the caspase-8-CrkL interaction. ( A ) Serum-starved NB7C8 cells were treated with increasing concentrations of dasatinib and allowed to attach to a fibronectin substrate for 30 min. ( B ) Lysates of adherent NB7C8 cells were prepared as in ( A ) with or without 30 nM dasatinib treatment and assessed for changes in activity and expression of Src and FAK. ( C ) Lysates of adherent NB7C8 cells were prepared as in ( A ) with or without 30 nM dasatinib treatment and probed with recombinant CrkL SH2 domain to assess conditional ability to bind caspase-8. ( D ) Murine embryonic fibroblasts (MEF) with indicated genetic deletions were allowed to attach to a fibronectin substrate and whole cell lysate (WCL) probed for indicated proteins, or with recombinant CrkL SH2 domain, which was then assessed for ability to interact with indicated proteins. +, FAK-GFP reconstitution. ( E ) NB7C8 cells expressing c-Src shRNA or control shRNA were allowed to spread on fibronectin-coated coverslips, and lysates probed with recombinant CrkL SH2 domain to assess interaction with indicated proteins.
    Figure Legend Snippet: Figure 3. Role of Src kinase in the caspase-8-CrkL interaction. ( A ) Serum-starved NB7C8 cells were treated with increasing concentrations of dasatinib and allowed to attach to a fibronectin substrate for 30 min. ( B ) Lysates of adherent NB7C8 cells were prepared as in ( A ) with or without 30 nM dasatinib treatment and assessed for changes in activity and expression of Src and FAK. ( C ) Lysates of adherent NB7C8 cells were prepared as in ( A ) with or without 30 nM dasatinib treatment and probed with recombinant CrkL SH2 domain to assess conditional ability to bind caspase-8. ( D ) Murine embryonic fibroblasts (MEF) with indicated genetic deletions were allowed to attach to a fibronectin substrate and whole cell lysate (WCL) probed for indicated proteins, or with recombinant CrkL SH2 domain, which was then assessed for ability to interact with indicated proteins. +, FAK-GFP reconstitution. ( E ) NB7C8 cells expressing c-Src shRNA or control shRNA were allowed to spread on fibronectin-coated coverslips, and lysates probed with recombinant CrkL SH2 domain to assess interaction with indicated proteins.

    Techniques Used: Activity Assay, Expressing, Recombinant, shRNA

    4) Product Images from "The microRNA-200/Zeb1 axis regulates ECM-dependent β1-integrin/FAK signaling, cancer cell invasion and metastasis through CRKL"

    Article Title: The microRNA-200/Zeb1 axis regulates ECM-dependent β1-integrin/FAK signaling, cancer cell invasion and metastasis through CRKL

    Journal: Scientific Reports

    doi: 10.1038/srep18652

    CRKL regulates FAK/Src complex formation at focal adhesions and the invasive/metastatic phenotype. ( a ) qRT-PCR and Western blot ( b ) analysis of 344SQ_shCRKL knockdown cells showed a decrease in FAK signaling. ( c ) CRKL knockdown decreased adhesion to fibronectin and 2D Transwell migration/invasion ( d ). ( e ) Immunofluorescent staining and biochemical fractionation ( f ) of CRKL knockdown cells for activated Src Y 418 , CRKL Y 207 , PaxY 118 , and p-FAK Y 861 in the focal adhesion complex at the membrane. An average of 20–30 cells was counted for the presence of focal adhesions and data are presented per cell. Scale bar is 200 μm. *p
    Figure Legend Snippet: CRKL regulates FAK/Src complex formation at focal adhesions and the invasive/metastatic phenotype. ( a ) qRT-PCR and Western blot ( b ) analysis of 344SQ_shCRKL knockdown cells showed a decrease in FAK signaling. ( c ) CRKL knockdown decreased adhesion to fibronectin and 2D Transwell migration/invasion ( d ). ( e ) Immunofluorescent staining and biochemical fractionation ( f ) of CRKL knockdown cells for activated Src Y 418 , CRKL Y 207 , PaxY 118 , and p-FAK Y 861 in the focal adhesion complex at the membrane. An average of 20–30 cells was counted for the presence of focal adhesions and data are presented per cell. Scale bar is 200 μm. *p

    Techniques Used: Quantitative RT-PCR, Western Blot, Migration, Staining, Fractionation

    5) Product Images from "Lactosylceramide synthases encoded by B4galt5 and 6 genes are pivotal for neuronal generation and myelin formation in mice"

    Article Title: Lactosylceramide synthases encoded by B4galt5 and 6 genes are pivotal for neuronal generation and myelin formation in mice

    Journal: PLoS Genetics

    doi: 10.1371/journal.pgen.1007545

    Proliferation, adhesion to ECMs, and neurite outgrowth in neurosphere cultures. (A) Proliferation in neurosphere cultures prepared from wild-type (wt, n = 3) and double knockout (DKO, n = 3) mice, from passage 1 to passage 3. (B–D) Cell number quantification in neurospheres prepared from wt (n = 3) and DKO (n = 3) mice that adhered to culture dishes coated with laminin (B), fibronectin (C), and collagen IV (D) at the concentrations indicated. (E) Neuronal cells, stained using anti-βIII-tubulin, differentiated from neurospheres from wt (upper) and DKO (lower) mice. Note that the neurite/axon length and number of branches were lower in DKO neuronal cells than in wt cells. (F) Distribution of the longest neurite length from an individual wt and DKO cell. (G) Mean length of the longest neurite of wt (n = 87) and DKO (n = 101) neuronal cells. (H) Mean of the total number of neuronal branching points per cell in wt (n = 23) and DKO (n = 20) neuronal cells. (I) Western blot analysis of neurospheres prepared from wt (n = 3) and DKO (n = 3) mice using anti-pTrkA (Y490ph), TrkA, pLyn (Y396ph), and Lyn antibodies. (J, K) The relative levels of pTrkA/TrkA (J) and pLyn/Lyn (K) of wt and DKO neurospheres are shown. The protein levels in wt neurospheres were normalized to 1. *, p
    Figure Legend Snippet: Proliferation, adhesion to ECMs, and neurite outgrowth in neurosphere cultures. (A) Proliferation in neurosphere cultures prepared from wild-type (wt, n = 3) and double knockout (DKO, n = 3) mice, from passage 1 to passage 3. (B–D) Cell number quantification in neurospheres prepared from wt (n = 3) and DKO (n = 3) mice that adhered to culture dishes coated with laminin (B), fibronectin (C), and collagen IV (D) at the concentrations indicated. (E) Neuronal cells, stained using anti-βIII-tubulin, differentiated from neurospheres from wt (upper) and DKO (lower) mice. Note that the neurite/axon length and number of branches were lower in DKO neuronal cells than in wt cells. (F) Distribution of the longest neurite length from an individual wt and DKO cell. (G) Mean length of the longest neurite of wt (n = 87) and DKO (n = 101) neuronal cells. (H) Mean of the total number of neuronal branching points per cell in wt (n = 23) and DKO (n = 20) neuronal cells. (I) Western blot analysis of neurospheres prepared from wt (n = 3) and DKO (n = 3) mice using anti-pTrkA (Y490ph), TrkA, pLyn (Y396ph), and Lyn antibodies. (J, K) The relative levels of pTrkA/TrkA (J) and pLyn/Lyn (K) of wt and DKO neurospheres are shown. The protein levels in wt neurospheres were normalized to 1. *, p

    Techniques Used: Double Knockout, Mouse Assay, Staining, Western Blot

    6) Product Images from "Combined Beta-Agonists and Corticosteroids Do Not Inhibit Extracellular Matrix Protein Production In Vitro"

    Article Title: Combined Beta-Agonists and Corticosteroids Do Not Inhibit Extracellular Matrix Protein Production In Vitro

    Journal: Journal of Allergy

    doi: 10.1155/2012/403059

    Effect of combined corticosteroids and LABA on TGF β -induced fibronectin in nonasthmatic bronchial rings. Immunohistochemical detection of fibronectin (brown staining) basally or following stimulation with TGF β in the presence or absence of drugs in nonasthmatic tissue sections.
    Figure Legend Snippet: Effect of combined corticosteroids and LABA on TGF β -induced fibronectin in nonasthmatic bronchial rings. Immunohistochemical detection of fibronectin (brown staining) basally or following stimulation with TGF β in the presence or absence of drugs in nonasthmatic tissue sections.

    Techniques Used: Immunohistochemistry, Staining

    Effect of combined corticosteroids and LABAs on the deposition of fibronectin in the absence (a) or presence of TGF β (b) for 48 hrs, respectively. Data are mean ± SEM from n = 6 asthmatic (black bars) and nonasthmatic (white bars) ASM cell lines. *Significantly different from nondrug-treated control P
    Figure Legend Snippet: Effect of combined corticosteroids and LABAs on the deposition of fibronectin in the absence (a) or presence of TGF β (b) for 48 hrs, respectively. Data are mean ± SEM from n = 6 asthmatic (black bars) and nonasthmatic (white bars) ASM cell lines. *Significantly different from nondrug-treated control P

    Techniques Used:

    7) Product Images from "Hypobaric hypoxia induced renal damage is mediated by altering redox pathway"

    Article Title: Hypobaric hypoxia induced renal damage is mediated by altering redox pathway

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0195701

    Immunohistochemical analysis of tubulointerstitial injury and other cellular changes under hypobaric hypoxia. (A) Tubular apoptosis by tunnel method. (B) Renal injury by Kim-1. (C) Hypoxia response by HIF-1alpha. (D-E) Fibrosis: Collagen-1 and Fibronectin. (F) Macrophage infiltration CD14. Data represented here is Mean ± S. E. M. Values are significant if P
    Figure Legend Snippet: Immunohistochemical analysis of tubulointerstitial injury and other cellular changes under hypobaric hypoxia. (A) Tubular apoptosis by tunnel method. (B) Renal injury by Kim-1. (C) Hypoxia response by HIF-1alpha. (D-E) Fibrosis: Collagen-1 and Fibronectin. (F) Macrophage infiltration CD14. Data represented here is Mean ± S. E. M. Values are significant if P

    Techniques Used: Immunohistochemistry, IF-P

    8) Product Images from "Insights into Biomechanical and Proteomic Characteristics of Small Diameter Vascular Grafts Utilizing the Human Umbilical Artery"

    Article Title: Insights into Biomechanical and Proteomic Characteristics of Small Diameter Vascular Grafts Utilizing the Human Umbilical Artery

    Journal: Biomedicines

    doi: 10.3390/biomedicines8080280

    Indirect immunofluorescence and scanning electron microscopy (SEM) analysis in human umbilical arteries (hUAs). Indirect immunofluorescence against collagen type I ( A , D ) and fibronectin ( B , E ) in combination with DAPI staining in native and decellularized (decel) hUAs, respectively. Blue spots in images A and B represent the presence of cell nuclei. Images were obtained with original magnification 10× and scale bars 100 μm. SEM analysis of native ( C ) and decellularized ( F ) hUAs. White arrows in image C, indicate the presence of cellular populations. White arrows in image F, indicate the preservation of ECM proteins, while no cellular populations are evident. Images were obtained with original magnification 40× and scale bars 25 μm.
    Figure Legend Snippet: Indirect immunofluorescence and scanning electron microscopy (SEM) analysis in human umbilical arteries (hUAs). Indirect immunofluorescence against collagen type I ( A , D ) and fibronectin ( B , E ) in combination with DAPI staining in native and decellularized (decel) hUAs, respectively. Blue spots in images A and B represent the presence of cell nuclei. Images were obtained with original magnification 10× and scale bars 100 μm. SEM analysis of native ( C ) and decellularized ( F ) hUAs. White arrows in image C, indicate the presence of cellular populations. White arrows in image F, indicate the preservation of ECM proteins, while no cellular populations are evident. Images were obtained with original magnification 40× and scale bars 25 μm.

    Techniques Used: Immunofluorescence, Electron Microscopy, Staining, Preserving

    9) Product Images from "The extracellular matrix modulates H2O2 degradation and redox signaling in endothelial cells"

    Article Title: The extracellular matrix modulates H2O2 degradation and redox signaling in endothelial cells

    Journal: Redox Biology

    doi: 10.1016/j.redox.2015.09.006

    H 2 O 2 consumption rates of HUVEC in different ECMs. Comparison of H 2 O 2 consumption rates (slope*(reaction volume)/(number of plated cells)) of HUVEC plated on dishes coated with gelatin, fibronectin or laminin, showed that consumption of H 2 O 2 by these cells was lower in the presence of laminin when compared with gelatin (values show the mean and SEM; N =3–8; Tukey test, ** p =0.005).
    Figure Legend Snippet: H 2 O 2 consumption rates of HUVEC in different ECMs. Comparison of H 2 O 2 consumption rates (slope*(reaction volume)/(number of plated cells)) of HUVEC plated on dishes coated with gelatin, fibronectin or laminin, showed that consumption of H 2 O 2 by these cells was lower in the presence of laminin when compared with gelatin (values show the mean and SEM; N =3–8; Tukey test, ** p =0.005).

    Techniques Used:

    10) Product Images from "A convenient protocol for establishing a human cell culture model of the outer retina."

    Article Title: A convenient protocol for establishing a human cell culture model of the outer retina.

    Journal: F1000Research

    doi: 10.12688/f1000research.15409.1

    Attachment and growth of ARPE-19 cells with or without an underlying fibronectin matrix. We tested effects of an extracellular matrix (ECM) such as fibronectin on the ability of cells to form a monolayer on transwell membranes. Inserts coated with fibronectin [ A , C , E ] or those without any coating [ B , D , F ] were imaged over several days after seeding. No differences were observed in cell attachment or growth. Contact inhibition proceeded cell differentiation after approximately 10 days in culture. Scale bars correspond to 200μm.
    Figure Legend Snippet: Attachment and growth of ARPE-19 cells with or without an underlying fibronectin matrix. We tested effects of an extracellular matrix (ECM) such as fibronectin on the ability of cells to form a monolayer on transwell membranes. Inserts coated with fibronectin [ A , C , E ] or those without any coating [ B , D , F ] were imaged over several days after seeding. No differences were observed in cell attachment or growth. Contact inhibition proceeded cell differentiation after approximately 10 days in culture. Scale bars correspond to 200μm.

    Techniques Used: Cell Attachment Assay, Inhibition, Cell Differentiation

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    Incubation:

    Article Title: Calcium-sensing Receptor Modulates Cell Adhesion and Migration via Integrins *
    Article Snippet: The cytoplasmic and cell surface fractions were separated by SDS-PAGE and immunoblotted using various antibodies. .. 96-Well flat bottom plates coated with various concentrations of fibronectin (catalog no. F1141, Sigma) were washed and blocked with 2% filtered BSA solution for 1 h at room temperature. rMTC cells were dissociated, washed, resuspended in assay buffer (serum-free DMEM supplemented with 20 m m HEPES and 0.1% BSA (pH 7.4)), and incubated at 37 °C in a humidified 5% CO2 incubator for 20 min to allow the cells to recover from the process of detachment. .. In parallel, the wells were aspirated, washed, and incubated with 50 μl of 2× DMSO, NPS R-568, or NPS 89636.

    Article Title: Cell-like pressure sensors reveal increase of mechanical stress towards the core of multicellular spheroids under compression
    Article Snippet: Subsequently, beads were incubated with EDC (26 mg ml−1 , Sigma Aldrich E6383) in a MES buffer for 2 h under gentle agitation. .. After, beads were washed three times with MES buffer and incubated over night with fibronectin (Sigma Aldrich F1141) at the concentration of 40 μg ml−1 . ..

    Activation Assay:

    Article Title: Simple and Inexpensive Paper-Based Astrocyte Co-culture to Improve Survival of Low-Density Neuronal Networks
    Article Snippet: .. After activation, the papers were transferred into a sterile 24-well plate under the laminar flow hood and immersed in one of the following surface functionalizing solutions: 10 μg/mL of laminin (L-2020, Sigma-Aldrich) in Neurobasal medium, 20 μg/mL of fibronectin (F1141, Sigma-Aldrich) in Neurobasal medium, or 200 μL of Matrigel (Corning Matrigel Basement Membrane Matrix; 354230, Chemie Brunschwig AG, Switzerland) diluted to 2 mg/mL in ice cold serum-free medium. .. After 45 min of incubation at room temperature, the papers were rinsed with supplemented Neurobasal medium and kept in Neurobasal medium and 2% penicillin streptomycin until seeding.

    Flow Cytometry:

    Article Title: Simple and Inexpensive Paper-Based Astrocyte Co-culture to Improve Survival of Low-Density Neuronal Networks
    Article Snippet: .. After activation, the papers were transferred into a sterile 24-well plate under the laminar flow hood and immersed in one of the following surface functionalizing solutions: 10 μg/mL of laminin (L-2020, Sigma-Aldrich) in Neurobasal medium, 20 μg/mL of fibronectin (F1141, Sigma-Aldrich) in Neurobasal medium, or 200 μL of Matrigel (Corning Matrigel Basement Membrane Matrix; 354230, Chemie Brunschwig AG, Switzerland) diluted to 2 mg/mL in ice cold serum-free medium. .. After 45 min of incubation at room temperature, the papers were rinsed with supplemented Neurobasal medium and kept in Neurobasal medium and 2% penicillin streptomycin until seeding.

    Hood:

    Article Title: Simple and Inexpensive Paper-Based Astrocyte Co-culture to Improve Survival of Low-Density Neuronal Networks
    Article Snippet: .. After activation, the papers were transferred into a sterile 24-well plate under the laminar flow hood and immersed in one of the following surface functionalizing solutions: 10 μg/mL of laminin (L-2020, Sigma-Aldrich) in Neurobasal medium, 20 μg/mL of fibronectin (F1141, Sigma-Aldrich) in Neurobasal medium, or 200 μL of Matrigel (Corning Matrigel Basement Membrane Matrix; 354230, Chemie Brunschwig AG, Switzerland) diluted to 2 mg/mL in ice cold serum-free medium. .. After 45 min of incubation at room temperature, the papers were rinsed with supplemented Neurobasal medium and kept in Neurobasal medium and 2% penicillin streptomycin until seeding.

    Concentration Assay:

    Article Title: Cell-like pressure sensors reveal increase of mechanical stress towards the core of multicellular spheroids under compression
    Article Snippet: Subsequently, beads were incubated with EDC (26 mg ml−1 , Sigma Aldrich E6383) in a MES buffer for 2 h under gentle agitation. .. After, beads were washed three times with MES buffer and incubated over night with fibronectin (Sigma Aldrich F1141) at the concentration of 40 μg ml−1 . ..

    other:

    Article Title: The calpain small subunit regulates cell-substrate mechanical interactions during fibroblast migration
    Article Snippet: Flexible polyacrylamide substrates were prepared and coated with bovine plasma fibronectin (Sigma) at 5 μg/cm2 , as described previously ( ).

    Article Title: Laterally confined growth of cells induces nuclear reprogramming in the absence of exogenous biochemical factors
    Article Snippet: Briefly, 1,800 μm2 rectangles (aspect ratio 1:5) (RE), 1,800 μm2 circles (BC), and 500 μm2 circles fibronectin (Sigma F1141-2MG) micropatterns (area = 1,800 μm2 and aspect ratio = 1:5) were made on uncoated Ibidi dishes (81151).

    Cell Culture:

    Article Title: The Microenvironment of Decellularized Extracellular Matrix from Heart Failure Myocardium Alters the Balance between Angiogenic and Fibrotic Signals from Stromal Primitive Cells
    Article Snippet: Immunostaining and Fluorescence Microscopy Analyses An amount of 2.5 × 105 CPCs/cm2 were seeded on dECM-NH or dECM-PH mounted on 35 mm culture dishes and cultured under standard culture conditions in the same cell culture medium used for hydration. .. As a control, 2.5 × 105 cells/cm2 were seeded on fibronectin-coated 35 mm culture dishes and cultured in the same conditions. .. Cells were checked daily by an Olympus CKX41 inverted microscope equipped with a Colorview IIIu digital camera (Olympus Corporation, Tokyo, Japan).

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  • 93
    Millipore fibronectin fragments
    Disruption of Hap–Hap interactions does not decrease Hap-mediated binding to <t>fibronectin.</t> ELISA showing binding of DB117 derivatives expressing Hap with deletions in the β-loops required for Hap–Hap interactions. Δ751–789
    Fibronectin Fragments, supplied by Millipore, 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/fibronectin fragments/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fibronectin fragments - by Bioz Stars, 2021-03
    93/100 stars
      Buy from Supplier

    93
    Millipore mouse anti cellular fibronectin monoclonal
    Immunocytochemistry of <t>fibronectin</t> expression in A549 cells stimulated without (a) or with 5 ng/ml (b, c, d) of TGF-β1 without (b), or with 100 (c) or 500 μg/ml (d) of pirfenidone for 48 h. Original magnification: x400. Pirfenidone decreased fibronectin over-expression induced by TGF-β1. Loss of epithelial marker E-cadherin mRNA in A549 cells caused by TGF-β1 (5 ng/ml) was also normalized by pirfenidone, but the difference did not reach significance ( e ).
    Mouse Anti Cellular Fibronectin Monoclonal, supplied by Millipore, 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/mouse anti cellular fibronectin monoclonal/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse anti cellular fibronectin monoclonal - by Bioz Stars, 2021-03
    93/100 stars
      Buy from Supplier



    Image Search Results


    Disruption of Hap–Hap interactions does not decrease Hap-mediated binding to fibronectin. ELISA showing binding of DB117 derivatives expressing Hap with deletions in the β-loops required for Hap–Hap interactions. Δ751–789

    Journal: Microbiology

    Article Title: Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin

    doi: 10.1099/mic.0.077784-0

    Figure Lengend Snippet: Disruption of Hap–Hap interactions does not decrease Hap-mediated binding to fibronectin. ELISA showing binding of DB117 derivatives expressing Hap with deletions in the β-loops required for Hap–Hap interactions. Δ751–789

    Article Snippet: Commercial fibronectin fragments were obtained from Sigma (45 kDa F0162, full-length F2006).

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Expressing

    Hap S binds to FNIII (1–2) . (a) Schematic representation of the domain structure and interactions of fibronectin. (b) Far-Western dot blot assay showing binding of purified Hap S to immobilized purified full-length fibronectin or fibronectin fragments.

    Journal: Microbiology

    Article Title: Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin

    doi: 10.1099/mic.0.077784-0

    Figure Lengend Snippet: Hap S binds to FNIII (1–2) . (a) Schematic representation of the domain structure and interactions of fibronectin. (b) Far-Western dot blot assay showing binding of purified Hap S to immobilized purified full-length fibronectin or fibronectin fragments.

    Article Snippet: Commercial fibronectin fragments were obtained from Sigma (45 kDa F0162, full-length F2006).

    Techniques: Western Blot, Dot Blot, Binding Assay, Purification

    The Hap ECM binding domain is responsible for bacterial binding to FNIII (1–2) . ELISA showing the binding of H. influenzae strain DB117 expressing either plasmid alone (pLS88), HapΔ26-525 or HapΔ26-725 to full-length fibronectin

    Journal: Microbiology

    Article Title: Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin

    doi: 10.1099/mic.0.077784-0

    Figure Lengend Snippet: The Hap ECM binding domain is responsible for bacterial binding to FNIII (1–2) . ELISA showing the binding of H. influenzae strain DB117 expressing either plasmid alone (pLS88), HapΔ26-525 or HapΔ26-725 to full-length fibronectin

    Article Snippet: Commercial fibronectin fragments were obtained from Sigma (45 kDa F0162, full-length F2006).

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Expressing, Plasmid Preparation

    Gram-positive bacterial FnBP motifs contribute to Hap-fibronectin binding. (a) Amino acid sequence of Hap residues 525–725. The putative acidic fibronectin-binding residues are highlighted in grey, and glycine residues that follow are underlined.

    Journal: Microbiology

    Article Title: Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin

    doi: 10.1099/mic.0.077784-0

    Figure Lengend Snippet: Gram-positive bacterial FnBP motifs contribute to Hap-fibronectin binding. (a) Amino acid sequence of Hap residues 525–725. The putative acidic fibronectin-binding residues are highlighted in grey, and glycine residues that follow are underlined.

    Article Snippet: Commercial fibronectin fragments were obtained from Sigma (45 kDa F0162, full-length F2006).

    Techniques: Binding Assay, Sequencing

    ) highlighting the predicted fibronectin-binding domains mutated in this study. (b) Top-down view of the Hap prism structure. The crystal structure of Hap S is shown in green.

    Journal: Microbiology

    Article Title: Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin

    doi: 10.1099/mic.0.077784-0

    Figure Lengend Snippet: ) highlighting the predicted fibronectin-binding domains mutated in this study. (b) Top-down view of the Hap prism structure. The crystal structure of Hap S is shown in green.

    Article Snippet: Commercial fibronectin fragments were obtained from Sigma (45 kDa F0162, full-length F2006).

    Techniques: Binding Assay

    Immunocytochemistry of fibronectin expression in A549 cells stimulated without (a) or with 5 ng/ml (b, c, d) of TGF-β1 without (b), or with 100 (c) or 500 μg/ml (d) of pirfenidone for 48 h. Original magnification: x400. Pirfenidone decreased fibronectin over-expression induced by TGF-β1. Loss of epithelial marker E-cadherin mRNA in A549 cells caused by TGF-β1 (5 ng/ml) was also normalized by pirfenidone, but the difference did not reach significance ( e ).

    Journal: BMC Pulmonary Medicine

    Article Title: Pirfenidone inhibits TGF-?1-induced over-expression of collagen type I and heat shock protein 47 in A549 cells

    doi: 10.1186/1471-2466-12-24

    Figure Lengend Snippet: Immunocytochemistry of fibronectin expression in A549 cells stimulated without (a) or with 5 ng/ml (b, c, d) of TGF-β1 without (b), or with 100 (c) or 500 μg/ml (d) of pirfenidone for 48 h. Original magnification: x400. Pirfenidone decreased fibronectin over-expression induced by TGF-β1. Loss of epithelial marker E-cadherin mRNA in A549 cells caused by TGF-β1 (5 ng/ml) was also normalized by pirfenidone, but the difference did not reach significance ( e ).

    Article Snippet: Immunocytochemistry After a 48-h incubation as detailed above, cultured cells were fixed with acetone for 10 min and stained using the alkaline phosphatase anti-alkaline phosphatase method with goat anti-human collagen type I polyclonal (CHEMICON, Temecula, CA), mouse anti-human HSP47 (Stressgen, Victoria, Canada) and mouse anti-cellular fibronectin monoclonal (CHEMICON) antibodies.

    Techniques: Immunocytochemistry, Expressing, Over Expression, Marker

    Hematoxylin and eosin stained corneal sections and expression of CD11b, fibronectin and HSP47 four weeks post-implantation. Hematoxylin and eosin stained sections of the 4mm pocket (A1), 6mm pocket (B1), 8mm pocket (C1) and 8mm flocket (D1) groups showed no inflammatory cells or fibrotic capsule formation around the inlay. No CD11b, fibronectin or HSP 47 positive cells were detected in the 4mm pocket (A2-4), 6mm pocket (B2-4J), 8mm pocket (C2-4) and 8mm flocket (D2-4) groups, respectively. Scale bar 100 μm. (arrow points to the inlay) Row 1 represents hematoxylin and eosin, row 2 CD11b, row 3 fibronectin and row 4 HSP47 corneal sections.

    Journal: PLoS ONE

    Article Title: Early wound healing and refractive response of different pocket configurations following presbyopic inlay implantation

    doi: 10.1371/journal.pone.0172014

    Figure Lengend Snippet: Hematoxylin and eosin stained corneal sections and expression of CD11b, fibronectin and HSP47 four weeks post-implantation. Hematoxylin and eosin stained sections of the 4mm pocket (A1), 6mm pocket (B1), 8mm pocket (C1) and 8mm flocket (D1) groups showed no inflammatory cells or fibrotic capsule formation around the inlay. No CD11b, fibronectin or HSP 47 positive cells were detected in the 4mm pocket (A2-4), 6mm pocket (B2-4J), 8mm pocket (C2-4) and 8mm flocket (D2-4) groups, respectively. Scale bar 100 μm. (arrow points to the inlay) Row 1 represents hematoxylin and eosin, row 2 CD11b, row 3 fibronectin and row 4 HSP47 corneal sections.

    Article Snippet: The antibodies were mouse monoclonal antibody against cellular fibronectin (5 μg/mL; Millipore Corp., Billerica, MA, USA), rat monoclonal antibody against CD11b (20 μg/ml; BD Pharmingen, Franklin Lakes, NJ, USA) and mouse monoclonal antibody against heat shock protein 47 (HSP47) (1 μg/ml Enzo Life Sciences, Switzerland).

    Techniques: Staining, Expressing

    Expression of tenascin-C, fibronectin, α-SMA, HSP47, and CD90 for the L and L + C groups at different time points. The staining was distinct for tenascin-C (TN; A) and fibronectin (FN; B) in all eyes at 1 month, and the extent was lesser in the L + C group than L group. There was minimal staining of α-SMA at all time points in all eyes (C). Significant upregulation of HSP47 was observed in all eyes (D), with comparable expression in L and L + C groups. Moderate expression of CD90 at 1 month in all eyes was seen (E). The staining for all the markers resolved with time. Nuclei were counterstained with DAPI ( blue ). Original magnification: 100×. Scale bar : 500 µm.

    Journal: Translational Vision Science & Technology

    Article Title: Tissue Responses and Wound Healing following Laser Scleral Microporation for Presbyopia Therapy

    doi: 10.1167/tvst.9.4.6

    Figure Lengend Snippet: Expression of tenascin-C, fibronectin, α-SMA, HSP47, and CD90 for the L and L + C groups at different time points. The staining was distinct for tenascin-C (TN; A) and fibronectin (FN; B) in all eyes at 1 month, and the extent was lesser in the L + C group than L group. There was minimal staining of α-SMA at all time points in all eyes (C). Significant upregulation of HSP47 was observed in all eyes (D), with comparable expression in L and L + C groups. Moderate expression of CD90 at 1 month in all eyes was seen (E). The staining for all the markers resolved with time. Nuclei were counterstained with DAPI ( blue ). Original magnification: 100×. Scale bar : 500 µm.

    Article Snippet: The following primary antibodies were then added and incubated for 2 hours at room temperature: mouse monoclonal antibody against cellular fibronectin (MAB-1940; Millipore, Billerica, MA, USA) diluted 1∶100, tenascin-C (SC-20932; Santa Cruz Biotechnology, Dallas, TA, USA) diluted 1∶200, mouse monoclonal antibody against heat shock protein 47 (HSP47) (ADI-SPA-470; Enzo Life Sciences, Lausen, Switzerland) diluted 1:200, rabbit polyclonal antibody against CD11b (AB-133357; Abcam, Cambridge, UK) diluted 1:100, mouse monoclonal antibody against α–smooth muscle actin (α-SMA) (M0851; Dako, Glostrup, Denmark) diluted 1:100, mouse monoclonal antibody against CD45 (Ab-10558; Abcam) diluted 1:100, mouse monoclonal antibody against CD31 (Ab-199012; Abcam) diluted 1:100, mouse monoclonal antibody against CD90 (LS-B3139; LifeSpan Biosciences, CA, USA) diluted 1:100 and growth-associated protein-43 (GAP43) (NB300-143; Novus Biologicals, Littleton, CO, USA) diluted 1∶500, telomerase (MA5-16034, Thermofisher, Waltham, MA, USA) diluted 1:100, and P63 (Sc8431; Santa Cruz Biotechnology, Dallas, TA, USA) diluted 1:50.

    Techniques: Expressing, Staining