laminin antibody  (Novus Biologicals)

 
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    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
    Category:
    Primary Antibodies
    Purity:
    IgG purified
    Conjugate:
    Unconjugated
    Immunogen:
    Laminin isolated from mouse EHS tumor. [UniProt# P19137]
    Size:
    0 1 ml
    Host:
    Rabbit
    Isotype:
    IgG
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    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 1 article reviews
    Price from $9.99 to $1999.99
    laminin antibody - by Bioz Stars, 2021-07
    93/100 stars

    Images

    1) Product Images from "The molecular and metabolic program for adaptation of white adipocytes to cool physiologic temperatures"

    Article Title: The molecular and metabolic program for adaptation of white adipocytes to cool physiologic temperatures

    Journal: bioRxiv

    doi: 10.1101/2020.10.16.342220

    Lipid unsaturation and SCD1 expression are induced by cool environmental temperatures. ( a ) Increased proportion of unsaturated lipid in BMAT TAG of distal tibia and caudal vertebra of rats housed at 22°C. Rats were housed from birth to 11 weeks of age at standard room temperature (22°C) or thermoneutrality (29 °C). Lipid composition of TAG for proximal (pTib) and distal tibia (dTib), and indicated caudal vertebra (CV) were determined by gas chromatography. ( n = 6 except CV4 and 13; n = 3). ( b ) Expression of SCD1 is elevated in CV from animals housed at 22°C compared to 29°C. SCD1 protein levels were normalized to adiponectin ( n = 7-9). ( c - e ) Mice were housed from birth to 13 weeks of age at 22°C or 29°C. After weaning, posterior hair was removed. ( c ) The subdermal temperature of mice housed at each temperature ( n = 7, 8). ( d ) Elevated SCD1 expression in subcutaneous WAT depots of mice at 22 °C. SCD1 protein expression was normalized to geometric mean value of the following proteins; adiponectin, perilipin, HSP70, and laminin ( n = 7 or 8). ( e ) Increased proportion of unsaturated lipid in TAG of gluteal WAT of mice housed at 22°C ( n = 5). Data are presented as mean ± s.d. * p
    Figure Legend Snippet: Lipid unsaturation and SCD1 expression are induced by cool environmental temperatures. ( a ) Increased proportion of unsaturated lipid in BMAT TAG of distal tibia and caudal vertebra of rats housed at 22°C. Rats were housed from birth to 11 weeks of age at standard room temperature (22°C) or thermoneutrality (29 °C). Lipid composition of TAG for proximal (pTib) and distal tibia (dTib), and indicated caudal vertebra (CV) were determined by gas chromatography. ( n = 6 except CV4 and 13; n = 3). ( b ) Expression of SCD1 is elevated in CV from animals housed at 22°C compared to 29°C. SCD1 protein levels were normalized to adiponectin ( n = 7-9). ( c - e ) Mice were housed from birth to 13 weeks of age at 22°C or 29°C. After weaning, posterior hair was removed. ( c ) The subdermal temperature of mice housed at each temperature ( n = 7, 8). ( d ) Elevated SCD1 expression in subcutaneous WAT depots of mice at 22 °C. SCD1 protein expression was normalized to geometric mean value of the following proteins; adiponectin, perilipin, HSP70, and laminin ( n = 7 or 8). ( e ) Increased proportion of unsaturated lipid in TAG of gluteal WAT of mice housed at 22°C ( n = 5). Data are presented as mean ± s.d. * p

    Techniques Used: Expressing, Gas Chromatography, Mouse Assay

    2) Product Images from "Ex-vivo recellularisation and stem cell differentiation of a decellularised rat dental pulp matrix"

    Article Title: Ex-vivo recellularisation and stem cell differentiation of a decellularised rat dental pulp matrix

    Journal: Scientific Reports

    doi: 10.1038/s41598-020-78477-x

    Non-collagenous structures assessment. Representative images of rat dental pulp tissues stained with alcian blue, labelled with fibronectin, laminin and α-gal antibodies. Control tissues reveal a rich glycosaminoglycans rich matrix and a positive immunoreactivity to fibronectin, laminin proteins and α-gal. Following decellularisation, preservation of glycosaminoglycans, fibronectin and laminin proteins with negative α-gal staining was evident. α-gal alpha-1,3 galactose. Scale bars are at 50 µm.
    Figure Legend Snippet: Non-collagenous structures assessment. Representative images of rat dental pulp tissues stained with alcian blue, labelled with fibronectin, laminin and α-gal antibodies. Control tissues reveal a rich glycosaminoglycans rich matrix and a positive immunoreactivity to fibronectin, laminin proteins and α-gal. Following decellularisation, preservation of glycosaminoglycans, fibronectin and laminin proteins with negative α-gal staining was evident. α-gal alpha-1,3 galactose. Scale bars are at 50 µm.

    Techniques Used: Staining, Preserving

    3) 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:

    4) Product Images from "The molecular and metabolic program by which white adipocytes adapt to cool physiologic temperatures"

    Article Title: The molecular and metabolic program by which white adipocytes adapt to cool physiologic temperatures

    Journal: PLoS Biology

    doi: 10.1371/journal.pbio.3000988

    Lipid unsaturation and SCD1 expression are induced by cool environmental temperatures. ( A, B ) Rats were housed from birth to 11 weeks of age at standard room temperature (22°C) or thermoneutrality (29°C). ( A ) Increased proportion of unsaturated lipid in BMAT TAG of dTib and CV of rats housed at 22°C. Lipid composition of TAG for pTib and dTib and indicated CV were determined by GC ( n = 6 except CV4 and CV13; n = 3). Desaturation index (16:1 + 18:1)/(16:0 + 18:0) is shown at top of graph. ( B ) Expression of SCD1 is elevated in CV from animals housed at 22°C compared to 29°C. SCD1 protein levels were normalized to adiponectin ( n = 7–9). ( C – E ) Mice were housed from birth to 13 weeks of age at 22°C or 29°C. After weaning, posterior hair was removed weekly. ( C ) The subdermal temperature of mice housed at each temperature ( n = 7, 8). ( D ) Elevated SCD1 expression in subcutaneous WAT depots of mice at 22°C. SCD1 protein expression was normalized to geometric mean value of the following proteins; adiponectin and laminin (shown), as well as perilipin, and HSP70 ( n = 8 or 9). ( E ) Increased proportion of unsaturated lipid in TAG of gluteal WAT of mice housed at 22°C compared to 29°C ( n = 5). Data are presented as mean ± SD. * p
    Figure Legend Snippet: Lipid unsaturation and SCD1 expression are induced by cool environmental temperatures. ( A, B ) Rats were housed from birth to 11 weeks of age at standard room temperature (22°C) or thermoneutrality (29°C). ( A ) Increased proportion of unsaturated lipid in BMAT TAG of dTib and CV of rats housed at 22°C. Lipid composition of TAG for pTib and dTib and indicated CV were determined by GC ( n = 6 except CV4 and CV13; n = 3). Desaturation index (16:1 + 18:1)/(16:0 + 18:0) is shown at top of graph. ( B ) Expression of SCD1 is elevated in CV from animals housed at 22°C compared to 29°C. SCD1 protein levels were normalized to adiponectin ( n = 7–9). ( C – E ) Mice were housed from birth to 13 weeks of age at 22°C or 29°C. After weaning, posterior hair was removed weekly. ( C ) The subdermal temperature of mice housed at each temperature ( n = 7, 8). ( D ) Elevated SCD1 expression in subcutaneous WAT depots of mice at 22°C. SCD1 protein expression was normalized to geometric mean value of the following proteins; adiponectin and laminin (shown), as well as perilipin, and HSP70 ( n = 8 or 9). ( E ) Increased proportion of unsaturated lipid in TAG of gluteal WAT of mice housed at 22°C compared to 29°C ( n = 5). Data are presented as mean ± SD. * p

    Techniques Used: Expressing, Mouse Assay

    5) 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

    Incubation:

    Article Title: Insights into the Mechanisms Involved in Strong Hemorrhage and Dermonecrosis Induced by Atroxlysin-Ia, a PI-Class Snake Venom Metalloproteinase
    Article Snippet: For Western Blotting, after SDS-PAGE the proteins were electro-transferred to nitrocellulose membranes for 1 h (30 V and 60 mA). .. Membranes were blocked for 2 h with 5% low-fat milk in TBS (Tris-buffered saline) and incubated overnight at 4 °C with 0.35 µg/mL rabbit polyclonal anti-laminin (Novus Biologicals, Littleton, CO, USA), 10 µg/mL rabbit polyclonal anti-collagen IV (Fitzgerald, Acton, MA , USA), or 0.6 µg/mL goat polyclonal anti-nidogen 1(R & D Systems, Minneapolis, MN, USA). .. After incubation the membranes were washed with TBS and incubated with peroxidase-conjugated anti-rabbit IgG (1:1000) or anti-goat IgG (1:250) (Sigma-Aldrich, St. Louis, MO, USA) at room temperature for 1 h and the reactive bands were detected by incubation with 4-chloro-a-naphthol (Sigma-Aldrich, St. Louis, MO, USA) and H2 O2 .

    Article Title: A Model of Germinal Matrix Hemorrhage in Preterm Rat Pups
    Article Snippet: Antigen retrieval was performed by boiling sections in 0.01 M citrate buffer (pH6.0) for 10 min followed by incubating in serum-free protein blocking solution (Agilent DAKO) for 30 min. .. Sections were then incubated in a mixture of rabbit anti-laminin antibodies (Novus Biologicals, cat#NB300-144; 1:200) and mouse anti-claudin5 antibodies (Thermo Fisher Scientific, cat#35-2500; 1:200) overnight in fridge. .. The next day, section were incubated in appropriate alexa-488 and -594 conjugated secondary antibodies for 2 h at room temperature.

    Article Title: Insights into the Mechanisms Involved in Strong Hemorrhage and Dermonecrosis Induced by Atroxlysin-Ia, a PI-Class Snake Venom Metalloproteinase
    Article Snippet: The sections were blocked by incubating for 2 h at room temperature with PBS containing 1% triton X-100, 5% normal goat serum, 1% BSA, 0.5% glycine and 0.5% fish skin gelatin. .. After this, sections were incubated with rabbit polyclonal anti-laminin (Novus Biologicals, Littleton CO, USA), 10 µg/mL rabbit polyclonal anti-collagen IV (Fitzgerald, Acton, MA, USA) for 18 h at 4 °C. .. The sections were washed with PBS and incubated with TRITC-labeled (Tetramethyl Rhodamine Isothiocyanate) goat anti-rabbit IgG (Jackson ImmunoResearch, West Grove, PA, USA) and 4′,6-diamidino-2-phenylindole (DAPI) (Molecular Probes, Thermo Fisher Scientific, Waltham, MA, USA), at a 1:100 and 1:5000 dilution respectively, for 90 min at room temperature.

    Article Title: Ex-vivo recellularisation and stem cell differentiation of a decellularised rat dental pulp matrix
    Article Snippet: Immunohistochemistry analysisFollowing dewaxing and rehydration (as mentioned above), antigen retrieval methods were performed using either; (1) Bond enzyme pre-treatment kit (AR9551, Leica Biosystems Newcastle Ltd.) by incubating slides for 15 min at 37 °C or (2) Heat-induced antigen unmasking solution [Tris–EDTA buffer solution (pH 9.0) or citric acid buffer solution (pH 6.0)] (Vector Laboratories Ltd.) in an automated pressure cook for 2 min under full pressure as per manufacturer’s instructions. .. Following antigen retrieval, slides were then incubated at room temperature for 1 h with the following primary antibodies; mouse monoclonal antibodies against collagen type I (1:100, ab90395, Abcam, Cambridge, United Kingdom), collagen type III (1:200, ab6310, Abcam), fibronectin (1:50, ab6328, Abcam,), Alpha-1,3 Galactose (α-gal, 1:200, ALX-801–090, Enzo Life Sciences, Inc., Lausen, Switzerland), major histocompatibility class II RT1B (1:200, Bio-Rad Laboratories Ltd, Hertfordshire, United Kingdom), and rabbit polyclonal laminin antibody (1:400, NB300-144, Novus Biologicals, Abingdon, United Kingdom) were used to assess collagen matrix, xenoepitope expression, specific cellular and basement proteins components. .. Secondary antibody staining (immunolabelling) using either ImmPRESS Excel peroxidase anti-mouse (MP-7602, Vector Laboratories Ltd.) or horseradish peroxidase anti-rabbit polymer (MP-7401, Vector Laboratories Ltd.) were used following manufacturer’s instructions.

    Expressing:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: In sections of EAE brain, hMCAM-Fc stained the endothelial basement membrane, but not the parenchymal basement membrane ( ). .. 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: Ex-vivo recellularisation and stem cell differentiation of a decellularised rat dental pulp matrix
    Article Snippet: Immunohistochemistry analysisFollowing dewaxing and rehydration (as mentioned above), antigen retrieval methods were performed using either; (1) Bond enzyme pre-treatment kit (AR9551, Leica Biosystems Newcastle Ltd.) by incubating slides for 15 min at 37 °C or (2) Heat-induced antigen unmasking solution [Tris–EDTA buffer solution (pH 9.0) or citric acid buffer solution (pH 6.0)] (Vector Laboratories Ltd.) in an automated pressure cook for 2 min under full pressure as per manufacturer’s instructions. .. Following antigen retrieval, slides were then incubated at room temperature for 1 h with the following primary antibodies; mouse monoclonal antibodies against collagen type I (1:100, ab90395, Abcam, Cambridge, United Kingdom), collagen type III (1:200, ab6310, Abcam), fibronectin (1:50, ab6328, Abcam,), Alpha-1,3 Galactose (α-gal, 1:200, ALX-801–090, Enzo Life Sciences, Inc., Lausen, Switzerland), major histocompatibility class II RT1B (1:200, Bio-Rad Laboratories Ltd, Hertfordshire, United Kingdom), and rabbit polyclonal laminin antibody (1:400, NB300-144, Novus Biologicals, Abingdon, United Kingdom) were used to assess collagen matrix, xenoepitope expression, specific cellular and basement proteins components. .. Secondary antibody staining (immunolabelling) using either ImmPRESS Excel peroxidase anti-mouse (MP-7602, Vector Laboratories Ltd.) or horseradish peroxidase anti-rabbit polymer (MP-7401, Vector Laboratories Ltd.) were used following manufacturer’s instructions.

    Staining:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: In sections of EAE brain, hMCAM-Fc stained the endothelial basement membrane, but not the parenchymal basement membrane ( ). .. 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: Protein was extracted from the whole right hemisphere, separated on 6–12% glycine gels, and transferred onto polyvinylidene difluoride membranes (Millipore, Bedford, MA). .. 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: Laminin binding assay Parental CHO cells, lacking MCAM expression, or CHO cells stably transfected with mouse MCAM (CHO.mMCAM) were incubated for 30 minutes in the presence of recombinant laminin 411 or recombinant laminin 511 (20 µg/mL, Biolamina, Stockholm, Sweden) at 37°C . .. Cells were washed thoroughly and laminin binding to the surface of cells was detected with fluorescently labeled pan laminin antibody (Novus Biologicals) by flow cytometry. ..

    Labeling:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: Laminin binding assay Parental CHO cells, lacking MCAM expression, or CHO cells stably transfected with mouse MCAM (CHO.mMCAM) were incubated for 30 minutes in the presence of recombinant laminin 411 or recombinant laminin 511 (20 µg/mL, Biolamina, Stockholm, Sweden) at 37°C . .. Cells were washed thoroughly and laminin binding to the surface of cells was detected with fluorescently labeled pan laminin antibody (Novus Biologicals) by flow cytometry. ..

    Flow Cytometry:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: Laminin binding assay Parental CHO cells, lacking MCAM expression, or CHO cells stably transfected with mouse MCAM (CHO.mMCAM) were incubated for 30 minutes in the presence of recombinant laminin 411 or recombinant laminin 511 (20 µg/mL, Biolamina, Stockholm, Sweden) at 37°C . .. Cells were washed thoroughly and laminin binding to the surface of cells was detected with fluorescently labeled pan laminin antibody (Novus Biologicals) by flow cytometry. ..

    Cytometry:

    Article Title: Laminin-411 Is a Vascular Ligand for MCAM and Facilitates TH17 Cell Entry into the CNS
    Article Snippet: Laminin binding assay Parental CHO cells, lacking MCAM expression, or CHO cells stably transfected with mouse MCAM (CHO.mMCAM) were incubated for 30 minutes in the presence of recombinant laminin 411 or recombinant laminin 511 (20 µg/mL, Biolamina, Stockholm, Sweden) at 37°C . .. Cells were washed thoroughly and laminin binding to the surface of cells was detected with fluorescently labeled pan laminin antibody (Novus Biologicals) by flow cytometry. ..

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  • 90
    Novus Biologicals anti laminin
    Effect of TGFβ2, cFN-EDA, LPS, and TLR4 signaling inhibition on <t>laminin</t> expression in primary human TM cells. NTM cells ( n = 3 primary human cell strains) were grown to confluency and left untreated for control ( A ), or treated with ( B , D , F , H , J , L ) TGFβ2 (5 ng/mL), ( E – H ) cFN-EDA (10 μg/mL), or ( I – L ) LPS (100 ng/mL). NTM cells involving TLR4 signaling inhibition were pretreated with TAK-242 (15 μM) for 2 hours ( C , D , G , H , K , L ), followed by treatment with ( D , H , L ) TGFβ2 (5 ng/mL), ( G , H ) cFN-EDA (10 μg/mL), and/or ( K , L ) LPS (100 ng/mL) in serum-free medium with TAK-242 (15 μM) for 48 hours. Immunocytochemistry studies revealed that TGFβ2, cFN-EDA, and LPS increases laminin expression compared to controls. Treatment with TGFβ2 and activation of TLR4 with cFN-EDA or LPS increased the staining signal when compared to TGFβ2 alone. Inhibition of TLR4 signaling via TAK-242 blocked the effect of all treatments. Scale bar represents 100 μm.
    Anti Laminin, supplied by Novus Biologicals, 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/anti laminin/product/Novus Biologicals
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti laminin - by Bioz Stars, 2021-07
    90/100 stars
      Buy from Supplier

    93
    Novus Biologicals laminin antibody
    Lipid unsaturation and SCD1 expression are induced by cool environmental temperatures. ( a ) Increased proportion of unsaturated lipid in BMAT TAG of distal tibia and caudal vertebra of rats housed at 22°C. Rats were housed from birth to 11 weeks of age at standard room temperature (22°C) or thermoneutrality (29 °C). Lipid composition of TAG for proximal (pTib) and distal tibia (dTib), and indicated caudal vertebra (CV) were determined by gas chromatography. ( n = 6 except CV4 and 13; n = 3). ( b ) Expression of SCD1 is elevated in CV from animals housed at 22°C compared to 29°C. SCD1 protein levels were normalized to adiponectin ( n = 7-9). ( c - e ) Mice were housed from birth to 13 weeks of age at 22°C or 29°C. After weaning, posterior hair was removed. ( c ) The subdermal temperature of mice housed at each temperature ( n = 7, 8). ( d ) Elevated SCD1 expression in subcutaneous WAT depots of mice at 22 °C. SCD1 protein expression was normalized to geometric mean value of the following proteins; adiponectin, perilipin, HSP70, and <t>laminin</t> ( n = 7 or 8). ( e ) Increased proportion of unsaturated lipid in TAG of gluteal WAT of mice housed at 22°C ( n = 5). Data are presented as mean ± s.d. * p
    Laminin Antibody, supplied by Novus Biologicals, 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/laminin antibody/product/Novus Biologicals
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    laminin antibody - by Bioz Stars, 2021-07
    93/100 stars
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    92
    Novus Biologicals laminin
    Pharmacologic inhibition of CX 3 CR1 results in formation of leaky microvessels within experimental plaque. A, Drug (F1) study protocol: Carotid artery was ligated in the C57BL6J mice (wt mice) and animals were treated with a selective CX 3 CR1 inhibitor (F1) (from second week post carotid ligation for another two weeks). B, Representative cross sectional images of carotid artery from C57BL6J mice treated with saline or a selective CX 3 CR1 inhibitor (F1) and stained for <t>laminin</t> (B; Basement membrane; Red), or CD42b (D; Platelets; Red), CX 3 CR1 (GFP; Green) and DAPI (Nucleus; Blue). B C, Significantly greater number of CX 3 CR1 positive microvessels were covered by basement membrane laminin in saline treated C57BL6J mice compared to F1 treated mice. D E, Increased platelet CD42b staining was observed in the neointimal interstitial space in the F1 treated mice compared to saline treated mice (Scale bar: 50 µm). In addition the leaky microvessel phenotype in mice treated with F1 was confirmed by presence of intravenously administered (tail vein) 2–2.5 µm diameter microspheres (red spheres) in the neointimal lesion (F G). IgG control staining for isotype-matched antibodies shown. Data is represented as mean ± SEM of 15 plaque sections/mice (n = 4 independently performed experiments); * denotes p
    Laminin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/laminin/product/Novus Biologicals
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    laminin - by Bioz Stars, 2021-07
    92/100 stars
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    92
    Novus Biologicals anti pan laminin
    mMCAM colocalizes with <t>laminin</t> 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.
    Anti Pan Laminin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti pan laminin/product/Novus Biologicals
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti pan laminin - by Bioz Stars, 2021-07
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    Effect of TGFβ2, cFN-EDA, LPS, and TLR4 signaling inhibition on laminin expression in primary human TM cells. NTM cells ( n = 3 primary human cell strains) were grown to confluency and left untreated for control ( A ), or treated with ( B , D , F , H , J , L ) TGFβ2 (5 ng/mL), ( E – H ) cFN-EDA (10 μg/mL), or ( I – L ) LPS (100 ng/mL). NTM cells involving TLR4 signaling inhibition were pretreated with TAK-242 (15 μM) for 2 hours ( C , D , G , H , K , L ), followed by treatment with ( D , H , L ) TGFβ2 (5 ng/mL), ( G , H ) cFN-EDA (10 μg/mL), and/or ( K , L ) LPS (100 ng/mL) in serum-free medium with TAK-242 (15 μM) for 48 hours. Immunocytochemistry studies revealed that TGFβ2, cFN-EDA, and LPS increases laminin expression compared to controls. Treatment with TGFβ2 and activation of TLR4 with cFN-EDA or LPS increased the staining signal when compared to TGFβ2 alone. Inhibition of TLR4 signaling via TAK-242 blocked the effect of all treatments. Scale bar represents 100 μm.

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Crosstalk Between Transforming Growth Factor Beta-2 and Toll-Like Receptor 4 in the Trabecular Meshwork

    doi: 10.1167/iovs.16-21331

    Figure Lengend Snippet: Effect of TGFβ2, cFN-EDA, LPS, and TLR4 signaling inhibition on laminin expression in primary human TM cells. NTM cells ( n = 3 primary human cell strains) were grown to confluency and left untreated for control ( A ), or treated with ( B , D , F , H , J , L ) TGFβ2 (5 ng/mL), ( E – H ) cFN-EDA (10 μg/mL), or ( I – L ) LPS (100 ng/mL). NTM cells involving TLR4 signaling inhibition were pretreated with TAK-242 (15 μM) for 2 hours ( C , D , G , H , K , L ), followed by treatment with ( D , H , L ) TGFβ2 (5 ng/mL), ( G , H ) cFN-EDA (10 μg/mL), and/or ( K , L ) LPS (100 ng/mL) in serum-free medium with TAK-242 (15 μM) for 48 hours. Immunocytochemistry studies revealed that TGFβ2, cFN-EDA, and LPS increases laminin expression compared to controls. Treatment with TGFβ2 and activation of TLR4 with cFN-EDA or LPS increased the staining signal when compared to TGFβ2 alone. Inhibition of TLR4 signaling via TAK-242 blocked the effect of all treatments. Scale bar represents 100 μm.

    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.

    Techniques: Inhibition, Expressing, Immunocytochemistry, Activation Assay, Staining

    Lipid unsaturation and SCD1 expression are induced by cool environmental temperatures. ( a ) Increased proportion of unsaturated lipid in BMAT TAG of distal tibia and caudal vertebra of rats housed at 22°C. Rats were housed from birth to 11 weeks of age at standard room temperature (22°C) or thermoneutrality (29 °C). Lipid composition of TAG for proximal (pTib) and distal tibia (dTib), and indicated caudal vertebra (CV) were determined by gas chromatography. ( n = 6 except CV4 and 13; n = 3). ( b ) Expression of SCD1 is elevated in CV from animals housed at 22°C compared to 29°C. SCD1 protein levels were normalized to adiponectin ( n = 7-9). ( c - e ) Mice were housed from birth to 13 weeks of age at 22°C or 29°C. After weaning, posterior hair was removed. ( c ) The subdermal temperature of mice housed at each temperature ( n = 7, 8). ( d ) Elevated SCD1 expression in subcutaneous WAT depots of mice at 22 °C. SCD1 protein expression was normalized to geometric mean value of the following proteins; adiponectin, perilipin, HSP70, and laminin ( n = 7 or 8). ( e ) Increased proportion of unsaturated lipid in TAG of gluteal WAT of mice housed at 22°C ( n = 5). Data are presented as mean ± s.d. * p

    Journal: bioRxiv

    Article Title: The molecular and metabolic program for adaptation of white adipocytes to cool physiologic temperatures

    doi: 10.1101/2020.10.16.342220

    Figure Lengend Snippet: Lipid unsaturation and SCD1 expression are induced by cool environmental temperatures. ( a ) Increased proportion of unsaturated lipid in BMAT TAG of distal tibia and caudal vertebra of rats housed at 22°C. Rats were housed from birth to 11 weeks of age at standard room temperature (22°C) or thermoneutrality (29 °C). Lipid composition of TAG for proximal (pTib) and distal tibia (dTib), and indicated caudal vertebra (CV) were determined by gas chromatography. ( n = 6 except CV4 and 13; n = 3). ( b ) Expression of SCD1 is elevated in CV from animals housed at 22°C compared to 29°C. SCD1 protein levels were normalized to adiponectin ( n = 7-9). ( c - e ) Mice were housed from birth to 13 weeks of age at 22°C or 29°C. After weaning, posterior hair was removed. ( c ) The subdermal temperature of mice housed at each temperature ( n = 7, 8). ( d ) Elevated SCD1 expression in subcutaneous WAT depots of mice at 22 °C. SCD1 protein expression was normalized to geometric mean value of the following proteins; adiponectin, perilipin, HSP70, and laminin ( n = 7 or 8). ( e ) Increased proportion of unsaturated lipid in TAG of gluteal WAT of mice housed at 22°C ( n = 5). Data are presented as mean ± s.d. * p

    Article Snippet: HADHB (MTPβ) (Novus Biologicals NBP1-54750), HSP70 (BD Transduction lab 610607), HSP90 (BD Transduction lab 610418), Laminin (Novus Biologicals, NB300-144), OXPHOS Cocktail (Abcam ab110413), Perilipin (Abcam Ab3526), PMP70 (Thermo Fisher Scientific PA1650), PEX5 (Thermo Fisher Scientific PA558716), PPARg (Millipore MAB3872), SCD1 (Cell Signaling Technology #2438), SREBP1 (ThermoFisher Invitrogen 2A4), Tubulin (Invitrogen MA1-80017), UCP1 (Alpha Diagnostic UCP11-A), VDAC1 (Abcam ab15895).

    Techniques: Expressing, Gas Chromatography, Mouse Assay

    Pharmacologic inhibition of CX 3 CR1 results in formation of leaky microvessels within experimental plaque. A, Drug (F1) study protocol: Carotid artery was ligated in the C57BL6J mice (wt mice) and animals were treated with a selective CX 3 CR1 inhibitor (F1) (from second week post carotid ligation for another two weeks). B, Representative cross sectional images of carotid artery from C57BL6J mice treated with saline or a selective CX 3 CR1 inhibitor (F1) and stained for laminin (B; Basement membrane; Red), or CD42b (D; Platelets; Red), CX 3 CR1 (GFP; Green) and DAPI (Nucleus; Blue). B C, Significantly greater number of CX 3 CR1 positive microvessels were covered by basement membrane laminin in saline treated C57BL6J mice compared to F1 treated mice. D E, Increased platelet CD42b staining was observed in the neointimal interstitial space in the F1 treated mice compared to saline treated mice (Scale bar: 50 µm). In addition the leaky microvessel phenotype in mice treated with F1 was confirmed by presence of intravenously administered (tail vein) 2–2.5 µm diameter microspheres (red spheres) in the neointimal lesion (F G). IgG control staining for isotype-matched antibodies shown. Data is represented as mean ± SEM of 15 plaque sections/mice (n = 4 independently performed experiments); * denotes p

    Journal: PLoS ONE

    Article Title: Role of CX3CR1 Receptor in Monocyte/Macrophage Driven Neovascularization

    doi: 10.1371/journal.pone.0057230

    Figure Lengend Snippet: Pharmacologic inhibition of CX 3 CR1 results in formation of leaky microvessels within experimental plaque. A, Drug (F1) study protocol: Carotid artery was ligated in the C57BL6J mice (wt mice) and animals were treated with a selective CX 3 CR1 inhibitor (F1) (from second week post carotid ligation for another two weeks). B, Representative cross sectional images of carotid artery from C57BL6J mice treated with saline or a selective CX 3 CR1 inhibitor (F1) and stained for laminin (B; Basement membrane; Red), or CD42b (D; Platelets; Red), CX 3 CR1 (GFP; Green) and DAPI (Nucleus; Blue). B C, Significantly greater number of CX 3 CR1 positive microvessels were covered by basement membrane laminin in saline treated C57BL6J mice compared to F1 treated mice. D E, Increased platelet CD42b staining was observed in the neointimal interstitial space in the F1 treated mice compared to saline treated mice (Scale bar: 50 µm). In addition the leaky microvessel phenotype in mice treated with F1 was confirmed by presence of intravenously administered (tail vein) 2–2.5 µm diameter microspheres (red spheres) in the neointimal lesion (F G). IgG control staining for isotype-matched antibodies shown. Data is represented as mean ± SEM of 15 plaque sections/mice (n = 4 independently performed experiments); * denotes p

    Article Snippet: For immunofluorescence detection of smooth muscle specific protein and GFP expression carotid artery/Matrigel sections were stained for calponin (rabbit anti calponin: 1∶200; Epitomics, CA, USA), CX3 CR1 (rabbit anti CX3 CR1:1∶50; ProSci Incorporated, CA, USA), F4/80 (Rat anti mouse F4/80: 1∶100; eBioscience; Hatfield, UK), Laminin (mouse anti laminin: 1∶500; Novus Biologicals, Cambridge, UK) and/or CD42b (rat anti CD42b: 1∶200; emfret Analytics GmbH & co.KG, Eibelstadt, Germany).

    Techniques: Inhibition, Mouse Assay, Ligation, Staining

    Functional deficiency of CX 3 CR1 results in leaky microvessel phenotype in experimental plaque. Representative cross sectional images of carotid artery plaques from CX 3 CR1 +/gfp and CX 3 CR1 gfp/gfp mice stained with CD42b (Platelets; Red) (A) or laminin (Basement membrane; Red) (C) and DAPI (Nucleus; Blue). B, Significantly increased staining for platelet CD42b was observed in the neointimal interstitial space in CX 3 CR1 gfp/gfp mice compared to competent CX 3 CR1 +/gfp mice (Scale bar: 50 µm). D, A significantly greater number of CX 3 CR1 positive microvessels were covered by basement membrane laminin in CX 3 CR1 +/gfp mice compared to CX 3 CR1 gfp/gfp mice (insets in panel C show GFP and laminin co-staining present in CX 3 CR1 +/gfp but not CX 3 CR1 gfp/gfp mice). Data is represented as mean ± SEM of 15 plaque sections/mice (n = 4 independently performed experiments); * denotes p

    Journal: PLoS ONE

    Article Title: Role of CX3CR1 Receptor in Monocyte/Macrophage Driven Neovascularization

    doi: 10.1371/journal.pone.0057230

    Figure Lengend Snippet: Functional deficiency of CX 3 CR1 results in leaky microvessel phenotype in experimental plaque. Representative cross sectional images of carotid artery plaques from CX 3 CR1 +/gfp and CX 3 CR1 gfp/gfp mice stained with CD42b (Platelets; Red) (A) or laminin (Basement membrane; Red) (C) and DAPI (Nucleus; Blue). B, Significantly increased staining for platelet CD42b was observed in the neointimal interstitial space in CX 3 CR1 gfp/gfp mice compared to competent CX 3 CR1 +/gfp mice (Scale bar: 50 µm). D, A significantly greater number of CX 3 CR1 positive microvessels were covered by basement membrane laminin in CX 3 CR1 +/gfp mice compared to CX 3 CR1 gfp/gfp mice (insets in panel C show GFP and laminin co-staining present in CX 3 CR1 +/gfp but not CX 3 CR1 gfp/gfp mice). Data is represented as mean ± SEM of 15 plaque sections/mice (n = 4 independently performed experiments); * denotes p

    Article Snippet: For immunofluorescence detection of smooth muscle specific protein and GFP expression carotid artery/Matrigel sections were stained for calponin (rabbit anti calponin: 1∶200; Epitomics, CA, USA), CX3 CR1 (rabbit anti CX3 CR1:1∶50; ProSci Incorporated, CA, USA), F4/80 (Rat anti mouse F4/80: 1∶100; eBioscience; Hatfield, UK), Laminin (mouse anti laminin: 1∶500; Novus Biologicals, Cambridge, UK) and/or CD42b (rat anti CD42b: 1∶200; emfret Analytics GmbH & co.KG, Eibelstadt, Germany).

    Techniques: Functional Assay, Mouse Assay, Staining

    CX 3 CR1 deficient cells lack in vitro tunnelling capacity in solid matrix and form incomplete 3D tube-like structures compared to CX 3 CR1 competent cells. CX 3 CR1 cells isolated from bone marrow of CX 3 CR1 +/gfp or CX 3 CR1 gfp/gfp mice were sandwiched between two DQ-red fortified (20 µg/ml; substrate for proteases) Matrigel layers with or without 10 ng/ml CX 3 CL1 gradient and were cultured for 5 days. A B, CX 3 CR1 cells remodelled into tube-like structures (tubulation) especially under CX 3 CL1 gradient (Scale bar: 10 µm). However these tubular structures were incompletely formed by CX 3 CR1 deficient cells. Furthermore, the CX 3 CR1 deficient cells lacked tunneling capacity (dotted lines-protease activation red) in the Matrigel (C D) and produced significantly less laminin following CX 3 CL1 stimulation (E F). Data is represented as mean ± SEM of 4 independently performed experiments;* denotes p

    Journal: PLoS ONE

    Article Title: Role of CX3CR1 Receptor in Monocyte/Macrophage Driven Neovascularization

    doi: 10.1371/journal.pone.0057230

    Figure Lengend Snippet: CX 3 CR1 deficient cells lack in vitro tunnelling capacity in solid matrix and form incomplete 3D tube-like structures compared to CX 3 CR1 competent cells. CX 3 CR1 cells isolated from bone marrow of CX 3 CR1 +/gfp or CX 3 CR1 gfp/gfp mice were sandwiched between two DQ-red fortified (20 µg/ml; substrate for proteases) Matrigel layers with or without 10 ng/ml CX 3 CL1 gradient and were cultured for 5 days. A B, CX 3 CR1 cells remodelled into tube-like structures (tubulation) especially under CX 3 CL1 gradient (Scale bar: 10 µm). However these tubular structures were incompletely formed by CX 3 CR1 deficient cells. Furthermore, the CX 3 CR1 deficient cells lacked tunneling capacity (dotted lines-protease activation red) in the Matrigel (C D) and produced significantly less laminin following CX 3 CL1 stimulation (E F). Data is represented as mean ± SEM of 4 independently performed experiments;* denotes p

    Article Snippet: For immunofluorescence detection of smooth muscle specific protein and GFP expression carotid artery/Matrigel sections were stained for calponin (rabbit anti calponin: 1∶200; Epitomics, CA, USA), CX3 CR1 (rabbit anti CX3 CR1:1∶50; ProSci Incorporated, CA, USA), F4/80 (Rat anti mouse F4/80: 1∶100; eBioscience; Hatfield, UK), Laminin (mouse anti laminin: 1∶500; Novus Biologicals, Cambridge, UK) and/or CD42b (rat anti CD42b: 1∶200; emfret Analytics GmbH & co.KG, Eibelstadt, Germany).

    Techniques: In Vitro, Isolation, Mouse Assay, Cell Culture, Activation Assay, Produced

    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: Sections were fixed in cold acetone for 10 minutes, blocked and stained with directly conjugated anti-pan-laminin (Novus Biologicals), MCAM-Fc, anti-CD31 (BD Pharmingen) or anti-laminin α4 (R & D Systems).

    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: Sections were fixed in cold acetone for 10 minutes, blocked and stained with directly conjugated anti-pan-laminin (Novus Biologicals), MCAM-Fc, anti-CD31 (BD Pharmingen) or anti-laminin α4 (R & D Systems).

    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: Sections were fixed in cold acetone for 10 minutes, blocked and stained with directly conjugated anti-pan-laminin (Novus Biologicals), MCAM-Fc, anti-CD31 (BD Pharmingen) or anti-laminin α4 (R & D Systems).

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