laminin antibody  (Novus Biologicals)

 
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  • 93
    Name:
    Laminin Antibody
    Description:
    The Laminin Antibody from Novus Biologicals is a rabbit polyclonal antibody to Laminin This antibody reacts with human mouse rat invertebrate rabbit sheep The Laminin Antibody has been validated for the following applications Western Blot Immunohistochemistry Immunocytochemistry Immunofluorescence Immunohistochemistry Paraffin Immunohistochemistry Frozen
    Catalog Number:
    nb300-144
    Price:
    379
    Host:
    Rabbit
    Purity:
    IgG purified
    Conjugate:
    Unconjugated
    Immunogen:
    Laminin isolated from mouse EHS tumor. [UniProt# P19137]
    Size:
    0 1 ml
    Category:
    Primary Antibodies
    Isotype:
    IgG
    Buy from Supplier


    Structured Review

    Novus Biologicals laminin antibody
    Laminin Antibody
    The Laminin Antibody from Novus Biologicals is a rabbit polyclonal antibody to Laminin This antibody reacts with human mouse rat invertebrate rabbit sheep The Laminin Antibody has been validated for the following applications Western Blot Immunohistochemistry Immunocytochemistry Immunofluorescence Immunohistochemistry Paraffin Immunohistochemistry Frozen
    https://www.bioz.com/result/laminin antibody/product/Novus Biologicals
    Average 93 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    laminin antibody - by Bioz Stars, 2020-07
    93/100 stars

    Images

    1) Product Images from "Dynamic Assembly of Human Salivary Stem/Progenitor Microstructures Requires Coordinated α1β1 Integrin-Mediated Motility"

    Article Title: Dynamic Assembly of Human Salivary Stem/Progenitor Microstructures Requires Coordinated α1β1 Integrin-Mediated Motility

    Journal: Frontiers in Cell and Developmental Biology

    doi: 10.3389/fcell.2019.00224

    Schematic of molecular interplay during de novo microstructure organization. Secreted basement membrane proteins are directionally secreted and organized by hS/PCs at the periphery of the growing microstructure. The initial growth and coordinated movement during this maturation phase depends on β 1 integrin activation by hS/PC-secreted ligands: laminin, collagen IV, and perlecan/HSPG2. Adhesive interactions between integrins on cells and matrix or hydrogel networks surrounding them can generate traction forces large enough to drive coordinated revolutions of entire multicellular structures.
    Figure Legend Snippet: Schematic of molecular interplay during de novo microstructure organization. Secreted basement membrane proteins are directionally secreted and organized by hS/PCs at the periphery of the growing microstructure. The initial growth and coordinated movement during this maturation phase depends on β 1 integrin activation by hS/PC-secreted ligands: laminin, collagen IV, and perlecan/HSPG2. Adhesive interactions between integrins on cells and matrix or hydrogel networks surrounding them can generate traction forces large enough to drive coordinated revolutions of entire multicellular structures.

    Techniques Used: Activation Assay

    hS/PCs sequentially secrete basement membrane proteins during microstructure reorganization and function. Encapsulated hS/PCs in HA-PEGDA hydrogels initially produce laminin (red) (A–C) and collagen IV (green) (D–F) even at the single-cell state (A,D) . Perlecan (green) (G–I) secretion follows to stabilize the laminin and collagen IV networks. Scalebar = 20 μm in all confocal micrographs.
    Figure Legend Snippet: hS/PCs sequentially secrete basement membrane proteins during microstructure reorganization and function. Encapsulated hS/PCs in HA-PEGDA hydrogels initially produce laminin (red) (A–C) and collagen IV (green) (D–F) even at the single-cell state (A,D) . Perlecan (green) (G–I) secretion follows to stabilize the laminin and collagen IV networks. Scalebar = 20 μm in all confocal micrographs.

    Techniques Used:

    2) Product Images from "Antibodies generated against streptococci protect in a mouse model of disseminated aspergillosis"

    Article Title: Antibodies generated against streptococci protect in a mouse model of disseminated aspergillosis

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    doi: 10.4049/jimmunol.1401940

    SMB19 Tg mice have low or undectable A.f. fungal burden in their targeted tissues following A.f. challenge (A-E) Immunofluorescence analysis on frozen sections of cerebrum from C57BL/6J (A), μMT mice (B) J558 Tg (C) mice 4 days following i.v. infection with A.f. compared to SMB19 Tg at 4 days (D), or 60 days (E). (G-K) Analysis of kidney tissue from C57BL/6J (G), μMT mice (H), J558 Tg (I) compared to SMB19 Tg at 4 days (J) and 60 days (K) after i.v. infection with A.f. Sections are stained with anti-MAC1 (red), anti-Ly6G (green), anti-β-1,3 glucan (white), and anti-laminin (blue). White arrows indicate morphologically distinct hyphae in tissues from WT C57BL/6J, μMT and J558 Tg mice or anti-β-1-3 glucan remnants in SMB19 treated mice. (F, L) Quantitative PCR analysis of fungal burden in brain (F) or kidney (L) of WT C57BL/6J (black), μMT (red), SMB19 Tg (green), and J558 Tg (blue) mice at the indicated times after infection with A.f. Data represent the mean + SEM from 2 independent experiments with 3 mice per group. nd= not detectable. The Y axis represents the number of A.f. conidial equivalents per g of infected tissue extrapolated from cycle threshold calibration curves generated by the inclusion of known numbers of A.f. conidia into naive tissue preparations.
    Figure Legend Snippet: SMB19 Tg mice have low or undectable A.f. fungal burden in their targeted tissues following A.f. challenge (A-E) Immunofluorescence analysis on frozen sections of cerebrum from C57BL/6J (A), μMT mice (B) J558 Tg (C) mice 4 days following i.v. infection with A.f. compared to SMB19 Tg at 4 days (D), or 60 days (E). (G-K) Analysis of kidney tissue from C57BL/6J (G), μMT mice (H), J558 Tg (I) compared to SMB19 Tg at 4 days (J) and 60 days (K) after i.v. infection with A.f. Sections are stained with anti-MAC1 (red), anti-Ly6G (green), anti-β-1,3 glucan (white), and anti-laminin (blue). White arrows indicate morphologically distinct hyphae in tissues from WT C57BL/6J, μMT and J558 Tg mice or anti-β-1-3 glucan remnants in SMB19 treated mice. (F, L) Quantitative PCR analysis of fungal burden in brain (F) or kidney (L) of WT C57BL/6J (black), μMT (red), SMB19 Tg (green), and J558 Tg (blue) mice at the indicated times after infection with A.f. Data represent the mean + SEM from 2 independent experiments with 3 mice per group. nd= not detectable. The Y axis represents the number of A.f. conidial equivalents per g of infected tissue extrapolated from cycle threshold calibration curves generated by the inclusion of known numbers of A.f. conidia into naive tissue preparations.

    Techniques Used: Mouse Assay, Immunofluorescence, Infection, Staining, Real-time Polymerase Chain Reaction, Generated

    Related Articles

    Functional Assay:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: .. To further explore the functional interaction between MCAM and laminin 411 we examined the ability of mMCAM-expressed cells to capture recombinant laminin 411 from solution. mMCAM-transfected CHO cells were incubated with laminin 411 washed and then exposed to a pan laminin antibody to detect binding of laminin to the surface of the cells. .. We found that the mMCAM-transfected CHO cells, but not parental CHO cells, captured laminin on their cell surface, and this interaction was inhibited by anti-mMCAM clone 15 ( ). hMCAM-transfected CHO cells showed similar binding to recombinant laminin 411, which was inhibited by anti-hMCAM clone 17 (data not shown).

    Recombinant:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: .. To further explore the functional interaction between MCAM and laminin 411 we examined the ability of mMCAM-expressed cells to capture recombinant laminin 411 from solution. mMCAM-transfected CHO cells were incubated with laminin 411 washed and then exposed to a pan laminin antibody to detect binding of laminin to the surface of the cells. .. We found that the mMCAM-transfected CHO cells, but not parental CHO cells, captured laminin on their cell surface, and this interaction was inhibited by anti-mMCAM clone 15 ( ). hMCAM-transfected CHO cells showed similar binding to recombinant laminin 411, which was inhibited by anti-hMCAM clone 17 (data not shown).

    Labeling:

    Article Title: BMP and Activin Membrane Bound Inhibitor Regulates the Extracellular Matrix in the Trabecular Meshwork
    Article Snippet: .. Cells were labeled overnight at 4°C with rabbit anti-fibronectin (EMD Millipore, Billerica, MA, USA) 1:500 dilution, anti-laminin (Novus Biologicals, LL, Littleton, CO, USA) 1:250 dilution, anti-collagen-1 (Novus Biologicals) 1:250 dilution, anti-collagen-4 (Novus Biologicals) 1:350 dilution, and α-smooth muscle actin (Abcam, Cambridge, MA, USA) 1:500 dilution in Superblock Blocking Buffer in PBS (Thermo Fisher Scientific). .. Coverslips were incubated for 2 hours using Alexa-Fluor-labeled anti-rabbit or anti-mouse antibodies (Life Technologies, Carlsbad, CA, USA) 1:1000 dilution.

    Article Title: Crosstalk Between Transforming Growth Factor Beta-2 and Toll-Like Receptor 4 in the Trabecular Meshwork
    Article Snippet: .. Cells were labeled overnight at 4°C with rabbit anti-fibronectin (EMD Millipore, Billerica, MA, USA) 1:1000 dilution, anti-laminin (Novus Biologicals, Littleton, CO, USA) 1:250 dilution, and anti-collagen-1 (Novus Biologicals) 1:250 dilution in Superblock Blocking Buffer in PBS. .. Coverslips were incubated for 2 hours using Alexa Fluor–labeled anti-rabbit (Life Technologies, Carlsbad, CA, USA) 1:1000 dilution.

    Incubation:

    Article Title: Carbon monoxide-releasing molecule-3 protects against ischemic stroke by suppressing neuroinflammation and alleviating blood-brain barrier disruption
    Article Snippet: .. After being washed in PBS, the sections were incubated in PBST (0.3% Triton X-100 in PBS), blocked in 1% bovine serum albumin (BSA)/PBST, and subsequently incubated with the following primary antibodies overnight at 4 °C: goat anti-Iba1 (1:1000, Abcam, Cambridge, MA, USA), rat anti-CD31 (1:500, Abcam), rabbit anti-ZO-1 (1:150, Proteintech, Sanying Biotechnology, Wuhan, China), rabbit anti-laminin (1:1000, Novus Biologicals, Littleton, CO, USA), rat anti-PDGFRβ (1:1000, Abcam), rabbit anti-MMP-9 (1:1000, Abcam). ..

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: .. To further explore the functional interaction between MCAM and laminin 411 we examined the ability of mMCAM-expressed cells to capture recombinant laminin 411 from solution. mMCAM-transfected CHO cells were incubated with laminin 411 washed and then exposed to a pan laminin antibody to detect binding of laminin to the surface of the cells. .. We found that the mMCAM-transfected CHO cells, but not parental CHO cells, captured laminin on their cell surface, and this interaction was inhibited by anti-mMCAM clone 15 ( ). hMCAM-transfected CHO cells showed similar binding to recombinant laminin 411, which was inhibited by anti-hMCAM clone 17 (data not shown).

    Article Title: Dynamic Assembly of Human Salivary Stem/Progenitor Microstructures Requires Coordinated α1β1 Integrin-Mediated Motility
    Article Snippet: .. Samples were incubated with primary antibodies against basement membrane proteins: laminin (NB300-144; Novus Biologicals, 1:200), collagen IV (NBP1-97716, 1:200; Novus Biologicals), perlecan/HSPG2 (NBP1-05170, 1:200; Novus Biologicals), or β1 integrin (NB100-63255, 1:200; Novus Biologicals), followed by appropriate secondary antibodies conjugated to Alexa Fluor 488 (A11029; Life Technologies/ThermoFisher), Alexa Fluor 568 (A11011; Life Technologies/ThermoFisher) to tag proteins of interest. .. Nuclear [4′,6-diamidino-2-phenylindole (DAPI); 40011; Biotium] and filamentous actin (A22287; Life Technologies/ThermoFisher) counterstains were used prior to mounting (P36930; Life Technologies/ThermoFisher), if necessary, and confocal imaging (A1; Nikon Instruments) of specimens.

    Blocking Assay:

    Article Title: BMP and Activin Membrane Bound Inhibitor Regulates the Extracellular Matrix in the Trabecular Meshwork
    Article Snippet: .. Cells were labeled overnight at 4°C with rabbit anti-fibronectin (EMD Millipore, Billerica, MA, USA) 1:500 dilution, anti-laminin (Novus Biologicals, LL, Littleton, CO, USA) 1:250 dilution, anti-collagen-1 (Novus Biologicals) 1:250 dilution, anti-collagen-4 (Novus Biologicals) 1:350 dilution, and α-smooth muscle actin (Abcam, Cambridge, MA, USA) 1:500 dilution in Superblock Blocking Buffer in PBS (Thermo Fisher Scientific). .. Coverslips were incubated for 2 hours using Alexa-Fluor-labeled anti-rabbit or anti-mouse antibodies (Life Technologies, Carlsbad, CA, USA) 1:1000 dilution.

    Article Title: Crosstalk Between Transforming Growth Factor Beta-2 and Toll-Like Receptor 4 in the Trabecular Meshwork
    Article Snippet: .. Cells were labeled overnight at 4°C with rabbit anti-fibronectin (EMD Millipore, Billerica, MA, USA) 1:1000 dilution, anti-laminin (Novus Biologicals, Littleton, CO, USA) 1:250 dilution, and anti-collagen-1 (Novus Biologicals) 1:250 dilution in Superblock Blocking Buffer in PBS. .. Coverslips were incubated for 2 hours using Alexa Fluor–labeled anti-rabbit (Life Technologies, Carlsbad, CA, USA) 1:1000 dilution.

    Expressing:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: .. This expression pattern has been noted for the 411 isoform of laminin, while both membranes are stained by a pan laminin antibody . .. Expression of the MCAM ligand colocalized with a laminin 411 (α4 chain) specific antibody ( ) suggesting that laminin 411 might be a specific ligand for MCAM.

    Staining:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: .. This expression pattern has been noted for the 411 isoform of laminin, while both membranes are stained by a pan laminin antibody . .. Expression of the MCAM ligand colocalized with a laminin 411 (α4 chain) specific antibody ( ) suggesting that laminin 411 might be a specific ligand for MCAM.

    Article Title: Carbon monoxide-releasing molecule-3 protects against ischemic stroke by suppressing neuroinflammation and alleviating blood-brain barrier disruption
    Article Snippet: .. Membranes were blocked in 5% nonfat milk in Tris-buffered saline (TBS) with 0.1% Tween-20 (TBST) for 1 h at room temperature and stained overnight at 4 °C with one of the following primary antibodies: rabbit anti-NeuN (1:1000, Abcam), rabbit anti-MAP2 (1:200, Proteintech), rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH; 1:2000, Proteintech), goat anti-Iba-1 (1:1000, Abcam), rabbit anti-TNF-α (1:1000, Cell Signaling Technology, Danvers, MA, USA), rabbit anti-IL1β (1:200, Proteintech), rabbit anti-ZO-1 (1:200, Proteintech), rabbit anti-laminin (1:1000, Novus Biologicals), rat anti-PDGFRβ (1:1000, Abcam), rabbit anti-MMP-9 (1:50, Santa Cruz). ..

    Binding Assay:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: .. To further explore the functional interaction between MCAM and laminin 411 we examined the ability of mMCAM-expressed cells to capture recombinant laminin 411 from solution. mMCAM-transfected CHO cells were incubated with laminin 411 washed and then exposed to a pan laminin antibody to detect binding of laminin to the surface of the cells. .. We found that the mMCAM-transfected CHO cells, but not parental CHO cells, captured laminin on their cell surface, and this interaction was inhibited by anti-mMCAM clone 15 ( ). hMCAM-transfected CHO cells showed similar binding to recombinant laminin 411, which was inhibited by anti-hMCAM clone 17 (data not shown).

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  • 85
    Novus Biologicals rabbit anti laminin 111
    <t>Laminin-111-modified</t> nanofibers increase ductal (SIMS) and acinar (SMGC1O) cell proliferation without affecting cell viability. Total cell number graphs showing increased (A) SIMS cell and (B) SMGC10 cell proliferation for cells cultured on laminin-111-modified
    Rabbit Anti Laminin 111, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti laminin 111/product/Novus Biologicals
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti laminin 111 - by Bioz Stars, 2020-07
    85/100 stars
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    93
    Novus Biologicals rabbit anti laminin
    CORM-3 increases the expression of ZO-1 and <t>laminin</t> on day 3 after cerebral infarction. a Representative images show double immunofluorescence staining of CD31/ZO-1-positive cells in peri-infarction zones. Insets show high-magnification images of the boxed areas. Scale bar = 50 μm. b Quantification of ZO-1-positive area/CD31-positive area in peri-infarction zones (* p
    Rabbit Anti Laminin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti laminin/product/Novus Biologicals
    Average 93 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    rabbit anti laminin - by Bioz Stars, 2020-07
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      Buy from Supplier

    85
    Novus Biologicals monoclonal rat anti reticular fibroblast antibodies
    (A) Examples of monomorphic (top) and polymorphic (bottom) ventricular tachycardia induced by programmed stimulation using a single (top) or two (bottom) extra stimuli. Shown are three simultaneously recorded MAP recordings obtained from the right ventricular (MAP RV), left ventricular septal (MAP LVsept), and left ventricular free wall (MAP LVfree) epicardium. In the lower panel, the left ventricular free wall is recorded from the infarcted area and shows the typical alterations found in infarcted scar tissue: loss of the action potential dome and slow activation. Asterisks indicate stimulus artifacts in the right ventricular MAP recording. (B) Number of hearts with induced ventricular tachycardias ( > 10 consecutive premature ventricular activations) as a function of the number of extra stimuli (S2, first extra stimulus; S3, second extra stimulus) shown for hearts with G-CSF/SCF (black bars) and hearts from non-G-CSF/SCF control animals (gray bars). Ventricular tachycardia induction was less likely in G-CSF/SCF-treated hearts than in controls. (C) Left: Representative immunohistological sections of normal myocardium (top panels) and the border zone of the infarction (bottom panels) in untreated (left panels) and G-CSF/SCF-treated (right panels) hearts. Bright red immunofluorescence, connexin43; dark red, autofluorescence of myocytes; green, immunofluorescence detection of a fibrous tissue marker <t>(rat</t> <t>anti-reticular</t> <t>fibroblast</t> antibody; refer to Materials and methods, and see supplemental Materials and methods for a 3D visualization of connexin43 localization in the intercellular connections). Right (diagram): Mean connexin43 expression measured as connexin43 + area in relation to the whole area of myocardial tissue in the field of view. Connexin43 expression was markedly reduced in the border zone of the myocardial infarction. G-CSF/SCF increased connexin43 expression in the border zone without affecting connexin43 expression in normal myocardium.
    Monoclonal Rat Anti Reticular Fibroblast Antibodies, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal rat anti reticular fibroblast antibodies/product/Novus Biologicals
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    Image Search Results


    Laminin-111-modified nanofibers increase ductal (SIMS) and acinar (SMGC1O) cell proliferation without affecting cell viability. Total cell number graphs showing increased (A) SIMS cell and (B) SMGC10 cell proliferation for cells cultured on laminin-111-modified

    Journal: Biomaterials

    Article Title: Selective functionalization of nanofiber scaffolds to regulate salivary gland epithelial cell proliferation and polarity

    doi: 10.1016/j.biomaterials.2012.08.021

    Figure Lengend Snippet: Laminin-111-modified nanofibers increase ductal (SIMS) and acinar (SMGC1O) cell proliferation without affecting cell viability. Total cell number graphs showing increased (A) SIMS cell and (B) SMGC10 cell proliferation for cells cultured on laminin-111-modified

    Article Snippet: Primary antibodies used included mouse anti-ZO-1 (Invitrogen Cat No. 339100), mouse anti-occludin (Invitrogen Cat No. 33-1500), rabbit anti-aquaporin 5 (Alamone labs Cat No. (AQP5-005), rat anti-CD49f (Integrin α6) (BD Pharmingen Cat No. 555734), and rabbit anti-laminin-111 (Novus Biologicals 300-144).

    Techniques: Modification, Cell Culture

    Laminin-111 modification of nanofibers enhances polarity of SMGC10 salivary gland acinar cells. Cells were immunostained for (A) ZO-1 and (B) occludin, as indicators of apicobasal polarity. Single apical and basal confocal images and XZ projections indicate

    Journal: Biomaterials

    Article Title: Selective functionalization of nanofiber scaffolds to regulate salivary gland epithelial cell proliferation and polarity

    doi: 10.1016/j.biomaterials.2012.08.021

    Figure Lengend Snippet: Laminin-111 modification of nanofibers enhances polarity of SMGC10 salivary gland acinar cells. Cells were immunostained for (A) ZO-1 and (B) occludin, as indicators of apicobasal polarity. Single apical and basal confocal images and XZ projections indicate

    Article Snippet: Primary antibodies used included mouse anti-ZO-1 (Invitrogen Cat No. 339100), mouse anti-occludin (Invitrogen Cat No. 33-1500), rabbit anti-aquaporin 5 (Alamone labs Cat No. (AQP5-005), rat anti-CD49f (Integrin α6) (BD Pharmingen Cat No. 555734), and rabbit anti-laminin-111 (Novus Biologicals 300-144).

    Techniques: Modification

    Bifunctional nanofibers induce an intermediate polarity phenotype in SIMS ductal cells. SIMS cells were cultured for 48 hours on nanofibers, chitosan-coated fibers, laminin-111-coated fibers, or chitosan and laminin-111- coated fibers. Cells were immunostained

    Journal: Biomaterials

    Article Title: Selective functionalization of nanofiber scaffolds to regulate salivary gland epithelial cell proliferation and polarity

    doi: 10.1016/j.biomaterials.2012.08.021

    Figure Lengend Snippet: Bifunctional nanofibers induce an intermediate polarity phenotype in SIMS ductal cells. SIMS cells were cultured for 48 hours on nanofibers, chitosan-coated fibers, laminin-111-coated fibers, or chitosan and laminin-111- coated fibers. Cells were immunostained

    Article Snippet: Primary antibodies used included mouse anti-ZO-1 (Invitrogen Cat No. 339100), mouse anti-occludin (Invitrogen Cat No. 33-1500), rabbit anti-aquaporin 5 (Alamone labs Cat No. (AQP5-005), rat anti-CD49f (Integrin α6) (BD Pharmingen Cat No. 555734), and rabbit anti-laminin-111 (Novus Biologicals 300-144).

    Techniques: Cell Culture

    PLGA fiber scaffolds modified with chitosan and/or laminin-111 post-electrospinning. Fluorescence microscopy of unmodified, FITC-chitosan modified, laminin-111-modified, and chitosan- and laminin-111-modified PLGA fiber scaffolds prepared with the post-electrospinning

    Journal: Biomaterials

    Article Title: Selective functionalization of nanofiber scaffolds to regulate salivary gland epithelial cell proliferation and polarity

    doi: 10.1016/j.biomaterials.2012.08.021

    Figure Lengend Snippet: PLGA fiber scaffolds modified with chitosan and/or laminin-111 post-electrospinning. Fluorescence microscopy of unmodified, FITC-chitosan modified, laminin-111-modified, and chitosan- and laminin-111-modified PLGA fiber scaffolds prepared with the post-electrospinning

    Article Snippet: Primary antibodies used included mouse anti-ZO-1 (Invitrogen Cat No. 339100), mouse anti-occludin (Invitrogen Cat No. 33-1500), rabbit anti-aquaporin 5 (Alamone labs Cat No. (AQP5-005), rat anti-CD49f (Integrin α6) (BD Pharmingen Cat No. 555734), and rabbit anti-laminin-111 (Novus Biologicals 300-144).

    Techniques: Modification, Fluorescence, Microscopy

    Laminin-111 modification of nanofibers enhances polarity of SIMS cells. Cells were immunostained for (A) ZO-1 and (B) occludin as indicators of apicobasal polarity. Single apical and basal confocal images and XZ projections indicate that both ZO-1 and

    Journal: Biomaterials

    Article Title: Selective functionalization of nanofiber scaffolds to regulate salivary gland epithelial cell proliferation and polarity

    doi: 10.1016/j.biomaterials.2012.08.021

    Figure Lengend Snippet: Laminin-111 modification of nanofibers enhances polarity of SIMS cells. Cells were immunostained for (A) ZO-1 and (B) occludin as indicators of apicobasal polarity. Single apical and basal confocal images and XZ projections indicate that both ZO-1 and

    Article Snippet: Primary antibodies used included mouse anti-ZO-1 (Invitrogen Cat No. 339100), mouse anti-occludin (Invitrogen Cat No. 33-1500), rabbit anti-aquaporin 5 (Alamone labs Cat No. (AQP5-005), rat anti-CD49f (Integrin α6) (BD Pharmingen Cat No. 555734), and rabbit anti-laminin-111 (Novus Biologicals 300-144).

    Techniques: Modification

    CORM-3 increases the expression of ZO-1 and laminin on day 3 after cerebral infarction. a Representative images show double immunofluorescence staining of CD31/ZO-1-positive cells in peri-infarction zones. Insets show high-magnification images of the boxed areas. Scale bar = 50 μm. b Quantification of ZO-1-positive area/CD31-positive area in peri-infarction zones (* p

    Journal: Journal of Neuroinflammation

    Article Title: Carbon monoxide-releasing molecule-3 protects against ischemic stroke by suppressing neuroinflammation and alleviating blood-brain barrier disruption

    doi: 10.1186/s12974-018-1226-1

    Figure Lengend Snippet: CORM-3 increases the expression of ZO-1 and laminin on day 3 after cerebral infarction. a Representative images show double immunofluorescence staining of CD31/ZO-1-positive cells in peri-infarction zones. Insets show high-magnification images of the boxed areas. Scale bar = 50 μm. b Quantification of ZO-1-positive area/CD31-positive area in peri-infarction zones (* p

    Article Snippet: After being washed in PBS, the sections were incubated in PBST (0.3% Triton X-100 in PBS), blocked in 1% bovine serum albumin (BSA)/PBST, and subsequently incubated with the following primary antibodies overnight at 4 °C: goat anti-Iba1 (1:1000, Abcam, Cambridge, MA, USA), rat anti-CD31 (1:500, Abcam), rabbit anti-ZO-1 (1:150, Proteintech, Sanying Biotechnology, Wuhan, China), rabbit anti-laminin (1:1000, Novus Biologicals, Littleton, CO, USA), rat anti-PDGFRβ (1:1000, Abcam), rabbit anti-MMP-9 (1:1000, Abcam).

    Techniques: Expressing, Double Immunofluorescence Staining

    mMCAM colocalizes with laminin 411 on the choroid plexus, and shows no specific binding to tissues from LAMA4−/− mice. (A) Staining of healthy mouse choroid plexus with anti-laminin, anti-laminin α4 and mMCAM-Fc (B) Staining of healthy brain tissues from LAMA4−/− mice with anti-laminin and mMCAM-Fc.

    Journal: PLoS ONE

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS

    doi: 10.1371/journal.pone.0040443

    Figure Lengend Snippet: mMCAM colocalizes with laminin 411 on the choroid plexus, and shows no specific binding to tissues from LAMA4−/− mice. (A) Staining of healthy mouse choroid plexus with anti-laminin, anti-laminin α4 and mMCAM-Fc (B) Staining of healthy brain tissues from LAMA4−/− mice with anti-laminin and mMCAM-Fc.

    Article Snippet: To further explore the functional interaction between MCAM and laminin 411 we examined the ability of mMCAM-expressed cells to capture recombinant laminin 411 from solution. mMCAM-transfected CHO cells were incubated with laminin 411 washed and then exposed to a pan laminin antibody to detect binding of laminin to the surface of the cells.

    Techniques: Binding Assay, Mouse Assay, Staining

    Laminin 411 functions as a ligand for MCAM. (A) CHO cells transfected with hMCAM were incubated with recombinant laminin 411. Laminin binding to the surface of the cells was detected with an anti-laminin antibody (left panel), while no binding was detected to CHO cells lacking MCAM expression (center panel). Recombinant laminin 511 did not bind to MCAM expressing CHO cells, and binding of laminin 411 was specifically inhibited by preincubation of the cells with anti-hMCAM (clone 17, right panel). (B) Human CD4+CD45RO+ memory T cells were purified and incubated with TCR stimulation in the presence of TGFβ and IL1β to induce hMCAM expression (approximately 50% expressed hMCAM, similar to Figure 2A ). Cells were incubated in plates coated with either laminin 411 or laminin 511 in the presence of either hMCAM-Fc or anti-hMCAM and specific binding of the cells to the laminin was determined. * indicates p

    Journal: PLoS ONE

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS

    doi: 10.1371/journal.pone.0040443

    Figure Lengend Snippet: Laminin 411 functions as a ligand for MCAM. (A) CHO cells transfected with hMCAM were incubated with recombinant laminin 411. Laminin binding to the surface of the cells was detected with an anti-laminin antibody (left panel), while no binding was detected to CHO cells lacking MCAM expression (center panel). Recombinant laminin 511 did not bind to MCAM expressing CHO cells, and binding of laminin 411 was specifically inhibited by preincubation of the cells with anti-hMCAM (clone 17, right panel). (B) Human CD4+CD45RO+ memory T cells were purified and incubated with TCR stimulation in the presence of TGFβ and IL1β to induce hMCAM expression (approximately 50% expressed hMCAM, similar to Figure 2A ). Cells were incubated in plates coated with either laminin 411 or laminin 511 in the presence of either hMCAM-Fc or anti-hMCAM and specific binding of the cells to the laminin was determined. * indicates p

    Article Snippet: To further explore the functional interaction between MCAM and laminin 411 we examined the ability of mMCAM-expressed cells to capture recombinant laminin 411 from solution. mMCAM-transfected CHO cells were incubated with laminin 411 washed and then exposed to a pan laminin antibody to detect binding of laminin to the surface of the cells.

    Techniques: Transfection, Incubation, Recombinant, Binding Assay, Expressing, Purification

    hMCAM binds to a ligand in the ECM with identical staining to laminin α4. Calcein labeled, hMCAM expressing MOLT 4 cells were preincubated with either isotype control (A) or anti-hMCAM (clone 17) (B) followed by incubation on tissue sections from healthy mice. After gentle washing of unbound cells, and mounting with DAPI, bound cells were visualized by fluorescent microscopy. Healthy mouse brain sections containing choroid plexus were stained with fluorescently labeled mMCAM-Fc protein and pan-laminin antibody. Staining of mMCAM-Fc was detected on choroid plexus (C) as well as the vasculature throughout the tissues (D). Fluorescently labeled mMCAM-Fc protein was preincubated with either isotype control (E) or anti-mMCAM (clone 15) (F) before addition to tissue sections of healthy mouse brain. Healthy mouse tissues were stained with fluorescently labeled mMCAM-Fc and CD31 (G) anti-mMCAM and pan laminin (H) or anti-mMCAM alone (I). Tissues from mice with active EAE were stained with fluorescently labeled mMCAM-Fc and pan-laminin (J) or mMCAM-Fc and an antibody specific to the α4 chain of laminin (K).

    Journal: PLoS ONE

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS

    doi: 10.1371/journal.pone.0040443

    Figure Lengend Snippet: hMCAM binds to a ligand in the ECM with identical staining to laminin α4. Calcein labeled, hMCAM expressing MOLT 4 cells were preincubated with either isotype control (A) or anti-hMCAM (clone 17) (B) followed by incubation on tissue sections from healthy mice. After gentle washing of unbound cells, and mounting with DAPI, bound cells were visualized by fluorescent microscopy. Healthy mouse brain sections containing choroid plexus were stained with fluorescently labeled mMCAM-Fc protein and pan-laminin antibody. Staining of mMCAM-Fc was detected on choroid plexus (C) as well as the vasculature throughout the tissues (D). Fluorescently labeled mMCAM-Fc protein was preincubated with either isotype control (E) or anti-mMCAM (clone 15) (F) before addition to tissue sections of healthy mouse brain. Healthy mouse tissues were stained with fluorescently labeled mMCAM-Fc and CD31 (G) anti-mMCAM and pan laminin (H) or anti-mMCAM alone (I). Tissues from mice with active EAE were stained with fluorescently labeled mMCAM-Fc and pan-laminin (J) or mMCAM-Fc and an antibody specific to the α4 chain of laminin (K).

    Article Snippet: To further explore the functional interaction between MCAM and laminin 411 we examined the ability of mMCAM-expressed cells to capture recombinant laminin 411 from solution. mMCAM-transfected CHO cells were incubated with laminin 411 washed and then exposed to a pan laminin antibody to detect binding of laminin to the surface of the cells.

    Techniques: Staining, Labeling, Expressing, Incubation, Mouse Assay, Microscopy

    (A) Examples of monomorphic (top) and polymorphic (bottom) ventricular tachycardia induced by programmed stimulation using a single (top) or two (bottom) extra stimuli. Shown are three simultaneously recorded MAP recordings obtained from the right ventricular (MAP RV), left ventricular septal (MAP LVsept), and left ventricular free wall (MAP LVfree) epicardium. In the lower panel, the left ventricular free wall is recorded from the infarcted area and shows the typical alterations found in infarcted scar tissue: loss of the action potential dome and slow activation. Asterisks indicate stimulus artifacts in the right ventricular MAP recording. (B) Number of hearts with induced ventricular tachycardias ( > 10 consecutive premature ventricular activations) as a function of the number of extra stimuli (S2, first extra stimulus; S3, second extra stimulus) shown for hearts with G-CSF/SCF (black bars) and hearts from non-G-CSF/SCF control animals (gray bars). Ventricular tachycardia induction was less likely in G-CSF/SCF-treated hearts than in controls. (C) Left: Representative immunohistological sections of normal myocardium (top panels) and the border zone of the infarction (bottom panels) in untreated (left panels) and G-CSF/SCF-treated (right panels) hearts. Bright red immunofluorescence, connexin43; dark red, autofluorescence of myocytes; green, immunofluorescence detection of a fibrous tissue marker (rat anti-reticular fibroblast antibody; refer to Materials and methods, and see supplemental Materials and methods for a 3D visualization of connexin43 localization in the intercellular connections). Right (diagram): Mean connexin43 expression measured as connexin43 + area in relation to the whole area of myocardial tissue in the field of view. Connexin43 expression was markedly reduced in the border zone of the myocardial infarction. G-CSF/SCF increased connexin43 expression in the border zone without affecting connexin43 expression in normal myocardium.

    Journal: The Journal of Experimental Medicine

    Article Title: G-CSF/SCF reduces inducible arrhythmias in the infarcted heart potentially via increased connexin43 expression and arteriogenesis

    doi: 10.1084/jem.20051151

    Figure Lengend Snippet: (A) Examples of monomorphic (top) and polymorphic (bottom) ventricular tachycardia induced by programmed stimulation using a single (top) or two (bottom) extra stimuli. Shown are three simultaneously recorded MAP recordings obtained from the right ventricular (MAP RV), left ventricular septal (MAP LVsept), and left ventricular free wall (MAP LVfree) epicardium. In the lower panel, the left ventricular free wall is recorded from the infarcted area and shows the typical alterations found in infarcted scar tissue: loss of the action potential dome and slow activation. Asterisks indicate stimulus artifacts in the right ventricular MAP recording. (B) Number of hearts with induced ventricular tachycardias ( > 10 consecutive premature ventricular activations) as a function of the number of extra stimuli (S2, first extra stimulus; S3, second extra stimulus) shown for hearts with G-CSF/SCF (black bars) and hearts from non-G-CSF/SCF control animals (gray bars). Ventricular tachycardia induction was less likely in G-CSF/SCF-treated hearts than in controls. (C) Left: Representative immunohistological sections of normal myocardium (top panels) and the border zone of the infarction (bottom panels) in untreated (left panels) and G-CSF/SCF-treated (right panels) hearts. Bright red immunofluorescence, connexin43; dark red, autofluorescence of myocytes; green, immunofluorescence detection of a fibrous tissue marker (rat anti-reticular fibroblast antibody; refer to Materials and methods, and see supplemental Materials and methods for a 3D visualization of connexin43 localization in the intercellular connections). Right (diagram): Mean connexin43 expression measured as connexin43 + area in relation to the whole area of myocardial tissue in the field of view. Connexin43 expression was markedly reduced in the border zone of the myocardial infarction. G-CSF/SCF increased connexin43 expression in the border zone without affecting connexin43 expression in normal myocardium.

    Article Snippet: The following primary antibodies were used: rat anti–mouse CD45 as a marker for blood cells (AB3088; Abcam Limited), monoclonal anti–troponin T as a marker of differentiated cardiomyocytes (cardiac isoform AB-1, clone 13-11; Lab Vision), rabbit anti–rat connexin43 polyclonal antibodies for the detection of gap junctions (71-0700; Zytomed GmbH), monoclonal rat anti-reticular fibroblast antibodies (clone ER-TR7; Novus Biologicals Inc.), rabbit smooth muscle anti-actin antibody for the detection of arteries and arterioles (RB-9010; Lab Vision Corporation), rabbit c-kit (SCF receptor) antibody (sc-168; Santa Cruz Biotechnology, Inc.), and rabbit anti–G-CSFR antibody (sc-694; Santa Cruz Biotechnology, Inc.).

    Techniques: Activation Assay, Immunofluorescence, Marker, Expressing