rabbit anti parvalbumin  (Novus Biologicals)

 
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    Name:
    Parvalbumin Antibody
    Description:
    The Parvalbumin Antibody from Novus Biologicals is a rabbit polyclonal antibody to Parvalbumin This antibody reacts with human mouse rat The Parvalbumin Antibody has been validated for the following applications Western Blot ELISA Immunohistochemistry Immunocytochemistry Immunofluorescence Immunoprecipitation Immunohistochemistry Paraffin Immunohistochemistry Frozen
    Catalog Number:
    nb120-11427
    Price:
    349
    Host:
    Rabbit
    Purity:
    Immunogen affinity purified
    Conjugate:
    Unconjugated
    Immunogen:
    Purified parvalbumin from rat skeletal muscle.
    Size:
    100 ug
    Category:
    Primary Antibodies
    Isotype:
    IgG
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    Structured Review

    Novus Biologicals rabbit anti parvalbumin
    Incorporation of collagen networks in 3D hydrogel scaffolds supports cell alignment and differentiation. ( a ) Dry fabrics can be readily incorporated into commonly-used non-cell-adherent hydrogels such as agarose. ( b ) Low magnification epifluorescence images of actin-phalloidin and Hoechst nuclear staining demonstrate that collagen-doped fabrics promote large-scale alignment of agarose-encapsulated C2C12 cells. Cell alignment and growth is not observed for control fabrics that do not contain collagen. Arrows indicate direction of fabric alignment. ( c ) High-resolution confocal maximum intensity projections show details of aligned fascicle-like structures. Positioning of cell nuclei and interconnected cytoskeleton structures are indicative of myotube formation. Myotubes and fascicle-like structures are not observed for cells cultured with control fabrics. C2C12 cells growing along collagen networks within the hydrogels display immunofluorescence for skeletal muscle cell differentiation markers including myosin heavy chain, <t>parvalbumin</t> and NOS-I. All scale bars, 50 µm. ( d ) Representative Western blots for myosin heavy chain, parvalbumin and GAPDH for cells grown in 2D on tissue culture plastic, within agarose containing 3D control fabrics (3D (−)) and within agarose containing 3D collagen fabrics (3D (+)). Images are cropped from the original full blots with adjustment of brightness and contrast to ensure that faint bands are visible. Unprocessed Western blot images are available in Supplementary Figure 7 . Levels of myosin heavy chain ( e ) and parvalbumin ( f ) relative to GAPDH (AU; Arbitrary Units) were compared across culture conditions. Significant differences of p
    The Parvalbumin Antibody from Novus Biologicals is a rabbit polyclonal antibody to Parvalbumin This antibody reacts with human mouse rat The Parvalbumin Antibody has been validated for the following applications Western Blot ELISA Immunohistochemistry Immunocytochemistry Immunofluorescence Immunoprecipitation Immunohistochemistry Paraffin Immunohistochemistry Frozen
    https://www.bioz.com/result/rabbit anti parvalbumin/product/Novus Biologicals
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti parvalbumin - by Bioz Stars, 2020-09
    92/100 stars

    Images

    1) Product Images from "Templated Assembly of Collagen Fibers Directs Cell Growth in 2D and 3D"

    Article Title: Templated Assembly of Collagen Fibers Directs Cell Growth in 2D and 3D

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-10182-8

    Incorporation of collagen networks in 3D hydrogel scaffolds supports cell alignment and differentiation. ( a ) Dry fabrics can be readily incorporated into commonly-used non-cell-adherent hydrogels such as agarose. ( b ) Low magnification epifluorescence images of actin-phalloidin and Hoechst nuclear staining demonstrate that collagen-doped fabrics promote large-scale alignment of agarose-encapsulated C2C12 cells. Cell alignment and growth is not observed for control fabrics that do not contain collagen. Arrows indicate direction of fabric alignment. ( c ) High-resolution confocal maximum intensity projections show details of aligned fascicle-like structures. Positioning of cell nuclei and interconnected cytoskeleton structures are indicative of myotube formation. Myotubes and fascicle-like structures are not observed for cells cultured with control fabrics. C2C12 cells growing along collagen networks within the hydrogels display immunofluorescence for skeletal muscle cell differentiation markers including myosin heavy chain, parvalbumin and NOS-I. All scale bars, 50 µm. ( d ) Representative Western blots for myosin heavy chain, parvalbumin and GAPDH for cells grown in 2D on tissue culture plastic, within agarose containing 3D control fabrics (3D (−)) and within agarose containing 3D collagen fabrics (3D (+)). Images are cropped from the original full blots with adjustment of brightness and contrast to ensure that faint bands are visible. Unprocessed Western blot images are available in Supplementary Figure 7 . Levels of myosin heavy chain ( e ) and parvalbumin ( f ) relative to GAPDH (AU; Arbitrary Units) were compared across culture conditions. Significant differences of p
    Figure Legend Snippet: Incorporation of collagen networks in 3D hydrogel scaffolds supports cell alignment and differentiation. ( a ) Dry fabrics can be readily incorporated into commonly-used non-cell-adherent hydrogels such as agarose. ( b ) Low magnification epifluorescence images of actin-phalloidin and Hoechst nuclear staining demonstrate that collagen-doped fabrics promote large-scale alignment of agarose-encapsulated C2C12 cells. Cell alignment and growth is not observed for control fabrics that do not contain collagen. Arrows indicate direction of fabric alignment. ( c ) High-resolution confocal maximum intensity projections show details of aligned fascicle-like structures. Positioning of cell nuclei and interconnected cytoskeleton structures are indicative of myotube formation. Myotubes and fascicle-like structures are not observed for cells cultured with control fabrics. C2C12 cells growing along collagen networks within the hydrogels display immunofluorescence for skeletal muscle cell differentiation markers including myosin heavy chain, parvalbumin and NOS-I. All scale bars, 50 µm. ( d ) Representative Western blots for myosin heavy chain, parvalbumin and GAPDH for cells grown in 2D on tissue culture plastic, within agarose containing 3D control fabrics (3D (−)) and within agarose containing 3D collagen fabrics (3D (+)). Images are cropped from the original full blots with adjustment of brightness and contrast to ensure that faint bands are visible. Unprocessed Western blot images are available in Supplementary Figure 7 . Levels of myosin heavy chain ( e ) and parvalbumin ( f ) relative to GAPDH (AU; Arbitrary Units) were compared across culture conditions. Significant differences of p

    Techniques Used: Staining, Cell Culture, Immunofluorescence, Cell Differentiation, Western Blot

    2) Product Images from "Paradoxical proepileptic response to NMDA receptor blockade linked to cortical interneuron defect in stargazer mice"

    Article Title: Paradoxical proepileptic response to NMDA receptor blockade linked to cortical interneuron defect in stargazer mice

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2013.00156

    Stargazin expression is restricted to PV + interneurons in WT mouse somatosensory cortex (upper row). Somatodendritic stargazin immunoreactivity is lost in PV + interneurons in stargazer mouse (lower row). Co-labeling of stargazin and parvalbumin antibodies shown in layer 2/3 at 63× magnification (scale = 10 μm).
    Figure Legend Snippet: Stargazin expression is restricted to PV + interneurons in WT mouse somatosensory cortex (upper row). Somatodendritic stargazin immunoreactivity is lost in PV + interneurons in stargazer mouse (lower row). Co-labeling of stargazin and parvalbumin antibodies shown in layer 2/3 at 63× magnification (scale = 10 μm).

    Techniques Used: Expressing, Labeling

    3) Product Images from "Templated Assembly of Collagen Fibers Directs Cell Growth in 2D and 3D"

    Article Title: Templated Assembly of Collagen Fibers Directs Cell Growth in 2D and 3D

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-10182-8

    Incorporation of collagen networks in 3D hydrogel scaffolds supports cell alignment and differentiation. ( a ) Dry fabrics can be readily incorporated into commonly-used non-cell-adherent hydrogels such as agarose. ( b ) Low magnification epifluorescence images of actin-phalloidin and Hoechst nuclear staining demonstrate that collagen-doped fabrics promote large-scale alignment of agarose-encapsulated C2C12 cells. Cell alignment and growth is not observed for control fabrics that do not contain collagen. Arrows indicate direction of fabric alignment. ( c ) High-resolution confocal maximum intensity projections show details of aligned fascicle-like structures. Positioning of cell nuclei and interconnected cytoskeleton structures are indicative of myotube formation. Myotubes and fascicle-like structures are not observed for cells cultured with control fabrics. C2C12 cells growing along collagen networks within the hydrogels display immunofluorescence for skeletal muscle cell differentiation markers including myosin heavy chain, parvalbumin and NOS-I. All scale bars, 50 µm. ( d ) Representative Western blots for myosin heavy chain, parvalbumin and GAPDH for cells grown in 2D on tissue culture plastic, within agarose containing 3D control fabrics (3D (−)) and within agarose containing 3D collagen fabrics (3D (+)). Images are cropped from the original full blots with adjustment of brightness and contrast to ensure that faint bands are visible. Unprocessed Western blot images are available in Supplementary Figure 7 . Levels of myosin heavy chain ( e ) and parvalbumin ( f ) relative to GAPDH (AU; Arbitrary Units) were compared across culture conditions. Significant differences of p
    Figure Legend Snippet: Incorporation of collagen networks in 3D hydrogel scaffolds supports cell alignment and differentiation. ( a ) Dry fabrics can be readily incorporated into commonly-used non-cell-adherent hydrogels such as agarose. ( b ) Low magnification epifluorescence images of actin-phalloidin and Hoechst nuclear staining demonstrate that collagen-doped fabrics promote large-scale alignment of agarose-encapsulated C2C12 cells. Cell alignment and growth is not observed for control fabrics that do not contain collagen. Arrows indicate direction of fabric alignment. ( c ) High-resolution confocal maximum intensity projections show details of aligned fascicle-like structures. Positioning of cell nuclei and interconnected cytoskeleton structures are indicative of myotube formation. Myotubes and fascicle-like structures are not observed for cells cultured with control fabrics. C2C12 cells growing along collagen networks within the hydrogels display immunofluorescence for skeletal muscle cell differentiation markers including myosin heavy chain, parvalbumin and NOS-I. All scale bars, 50 µm. ( d ) Representative Western blots for myosin heavy chain, parvalbumin and GAPDH for cells grown in 2D on tissue culture plastic, within agarose containing 3D control fabrics (3D (−)) and within agarose containing 3D collagen fabrics (3D (+)). Images are cropped from the original full blots with adjustment of brightness and contrast to ensure that faint bands are visible. Unprocessed Western blot images are available in Supplementary Figure 7 . Levels of myosin heavy chain ( e ) and parvalbumin ( f ) relative to GAPDH (AU; Arbitrary Units) were compared across culture conditions. Significant differences of p

    Techniques Used: Staining, Cell Culture, Immunofluorescence, Cell Differentiation, Western Blot

    Related Articles

    Immunohistochemistry:

    Article Title: Paradoxical proepileptic response to NMDA receptor blockade linked to cortical interneuron defect in stargazer mice
    Article Snippet: .. Primary antibodies used for immunohistochemistry included: mouse anti-parvalbumin (Sigma, 1:1000 dilution) for co-labeling with rabbit anti-GluA4 (Millipore, 3 mg/ml); mouse anti-stargazin (Neuromab, 1:10 dilution) for co-labeling with rabbit anti-parvalbumin (Novus Biologicals), and rabbit anti-GluA4 as above. .. Secondary antibodies for immunofluorescence included: Alexa Fluor 488 F(ab′)2 fragment of goat anti-mouse IgG (H+L) 2 mg/ml and Alexa Fluor 555 F(ab′)2 fragment of goat anti-rabbit IgG (H+L) 2 mg/ml; both at 1:1000 dilution.

    Immunofluorescence:

    Article Title: Templated Assembly of Collagen Fibers Directs Cell Growth in 2D and 3D
    Article Snippet: .. The following primary antibodies were used to assess C2C12 differentiation in 3D culture conditions by immunofluorescence: mouse-anti-myosin-hc (1:100; Novus Biologicals), mouse-anti-parvalbumin (1:200; Chemicon), rabbit-anti-parvalbumin (1:100; Novus Biologicals), rabbit-anti-NOS-I (1:200; Chemicon) and goat-anti-nNOS (NOS-I) (1:100; Novus Biologicals). .. Two different antibodies were used to confirm appropriate staining for parvalbumin and NOS-I in C2C12 cells due to the diffuse expression of these markers in the cytoplasm.

    Generated:

    Article Title: Na+ channel-dependent recruitment of Nav?4 to axon initial segments and nodes of Ranvier
    Article Snippet: .. The following primary antibodies were used: mouse anti(α)–Nav β4 (NeuroMab, N168/6 generated against a fusion protein including amino acids 184-228), rabbit α-Nav β4 F3888 (generated against a peptide, CKKLITFILKKTREK), rat α-GFP (Nacalai Tesque Inc., 04404-84), rabbit α-V5 (Sigma, V8137), mouse α-V5 (AbD Serotec, SV5-Pk1), rabbit α-Nav 1.6 , rabbit α-βIV spectrin , mouse α-Kv 1.2 (NeuroMab, K14/16), chicken α-MAP2 (EnCor Biotechnology Inc.), mouse α-ankyrin G (NeuroMab, N106/36), mouse α-pan Nav α(Sigma, K58/35), rabbit α-parvalbumin (Novus Biologicals, NB120-11427), rabbit α-calbindin (Sigma, C2724), mouse α-calbindin (abcam, AF2E5), rabbit α-Kv 1.2 , rat α-MBP (Millipore, MAB386), rabbit α-GFP (Invitrogen, ), mouse α-GFP (Invitrogen, 11E5), mouse α-His tag (Upstate Biotechnology, 05-531), rabbit α-GAPDH (Sigma, G9545), and mouse α-actin (Millipore, MAB1501). .. The following secondary antibodies were used: goat α-rat 488 (Invitrogen, ), goat α-mouse XA 594 (Invitrogen, A11032), goat α-mouse IgG1 488 (Jackson ImmunoResearch 115-515-205), goat α-mouse IgG2a 594 (Jackson ImmunoResearch, 115-515-206), goat α-mouse IgG2b 594 (Jackson ImmunoResearch, 115-515-207), goat α-rabbit 594 (Invitrogen, ), goat α-rabbit 488 (Invitrogen, ), goat α-mouse XA 350 (Invitrogen, ), and goat α-chicken AMCA (Jackson ImmunoResearch, 103-155-155), goat α-mouse HRP (Invitrogen, ), goat α-rabbit HRP (Invitrogen, ), at 1:1000.

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  • 92
    Novus Biologicals rabbit anti parvalbumin
    Incorporation of collagen networks in 3D hydrogel scaffolds supports cell alignment and differentiation. ( a ) Dry fabrics can be readily incorporated into commonly-used non-cell-adherent hydrogels such as agarose. ( b ) Low magnification epifluorescence images of actin-phalloidin and Hoechst nuclear staining demonstrate that collagen-doped fabrics promote large-scale alignment of agarose-encapsulated C2C12 cells. Cell alignment and growth is not observed for control fabrics that do not contain collagen. Arrows indicate direction of fabric alignment. ( c ) High-resolution confocal maximum intensity projections show details of aligned fascicle-like structures. Positioning of cell nuclei and interconnected cytoskeleton structures are indicative of myotube formation. Myotubes and fascicle-like structures are not observed for cells cultured with control fabrics. C2C12 cells growing along collagen networks within the hydrogels display immunofluorescence for skeletal muscle cell differentiation markers including myosin heavy chain, <t>parvalbumin</t> and NOS-I. All scale bars, 50 µm. ( d ) Representative Western blots for myosin heavy chain, parvalbumin and GAPDH for cells grown in 2D on tissue culture plastic, within agarose containing 3D control fabrics (3D (−)) and within agarose containing 3D collagen fabrics (3D (+)). Images are cropped from the original full blots with adjustment of brightness and contrast to ensure that faint bands are visible. Unprocessed Western blot images are available in Supplementary Figure 7 . Levels of myosin heavy chain ( e ) and parvalbumin ( f ) relative to GAPDH (AU; Arbitrary Units) were compared across culture conditions. Significant differences of p
    Rabbit Anti Parvalbumin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti parvalbumin/product/Novus Biologicals
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    rabbit anti parvalbumin - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    Image Search Results


    Incorporation of collagen networks in 3D hydrogel scaffolds supports cell alignment and differentiation. ( a ) Dry fabrics can be readily incorporated into commonly-used non-cell-adherent hydrogels such as agarose. ( b ) Low magnification epifluorescence images of actin-phalloidin and Hoechst nuclear staining demonstrate that collagen-doped fabrics promote large-scale alignment of agarose-encapsulated C2C12 cells. Cell alignment and growth is not observed for control fabrics that do not contain collagen. Arrows indicate direction of fabric alignment. ( c ) High-resolution confocal maximum intensity projections show details of aligned fascicle-like structures. Positioning of cell nuclei and interconnected cytoskeleton structures are indicative of myotube formation. Myotubes and fascicle-like structures are not observed for cells cultured with control fabrics. C2C12 cells growing along collagen networks within the hydrogels display immunofluorescence for skeletal muscle cell differentiation markers including myosin heavy chain, parvalbumin and NOS-I. All scale bars, 50 µm. ( d ) Representative Western blots for myosin heavy chain, parvalbumin and GAPDH for cells grown in 2D on tissue culture plastic, within agarose containing 3D control fabrics (3D (−)) and within agarose containing 3D collagen fabrics (3D (+)). Images are cropped from the original full blots with adjustment of brightness and contrast to ensure that faint bands are visible. Unprocessed Western blot images are available in Supplementary Figure 7 . Levels of myosin heavy chain ( e ) and parvalbumin ( f ) relative to GAPDH (AU; Arbitrary Units) were compared across culture conditions. Significant differences of p

    Journal: Scientific Reports

    Article Title: Templated Assembly of Collagen Fibers Directs Cell Growth in 2D and 3D

    doi: 10.1038/s41598-017-10182-8

    Figure Lengend Snippet: Incorporation of collagen networks in 3D hydrogel scaffolds supports cell alignment and differentiation. ( a ) Dry fabrics can be readily incorporated into commonly-used non-cell-adherent hydrogels such as agarose. ( b ) Low magnification epifluorescence images of actin-phalloidin and Hoechst nuclear staining demonstrate that collagen-doped fabrics promote large-scale alignment of agarose-encapsulated C2C12 cells. Cell alignment and growth is not observed for control fabrics that do not contain collagen. Arrows indicate direction of fabric alignment. ( c ) High-resolution confocal maximum intensity projections show details of aligned fascicle-like structures. Positioning of cell nuclei and interconnected cytoskeleton structures are indicative of myotube formation. Myotubes and fascicle-like structures are not observed for cells cultured with control fabrics. C2C12 cells growing along collagen networks within the hydrogels display immunofluorescence for skeletal muscle cell differentiation markers including myosin heavy chain, parvalbumin and NOS-I. All scale bars, 50 µm. ( d ) Representative Western blots for myosin heavy chain, parvalbumin and GAPDH for cells grown in 2D on tissue culture plastic, within agarose containing 3D control fabrics (3D (−)) and within agarose containing 3D collagen fabrics (3D (+)). Images are cropped from the original full blots with adjustment of brightness and contrast to ensure that faint bands are visible. Unprocessed Western blot images are available in Supplementary Figure 7 . Levels of myosin heavy chain ( e ) and parvalbumin ( f ) relative to GAPDH (AU; Arbitrary Units) were compared across culture conditions. Significant differences of p

    Article Snippet: The following primary antibodies were used to assess C2C12 differentiation in 3D culture conditions by immunofluorescence: mouse-anti-myosin-hc (1:100; Novus Biologicals), mouse-anti-parvalbumin (1:200; Chemicon), rabbit-anti-parvalbumin (1:100; Novus Biologicals), rabbit-anti-NOS-I (1:200; Chemicon) and goat-anti-nNOS (NOS-I) (1:100; Novus Biologicals).

    Techniques: Staining, Cell Culture, Immunofluorescence, Cell Differentiation, Western Blot

    Stargazin expression is restricted to PV + interneurons in WT mouse somatosensory cortex (upper row). Somatodendritic stargazin immunoreactivity is lost in PV + interneurons in stargazer mouse (lower row). Co-labeling of stargazin and parvalbumin antibodies shown in layer 2/3 at 63× magnification (scale = 10 μm).

    Journal: Frontiers in Cellular Neuroscience

    Article Title: Paradoxical proepileptic response to NMDA receptor blockade linked to cortical interneuron defect in stargazer mice

    doi: 10.3389/fncel.2013.00156

    Figure Lengend Snippet: Stargazin expression is restricted to PV + interneurons in WT mouse somatosensory cortex (upper row). Somatodendritic stargazin immunoreactivity is lost in PV + interneurons in stargazer mouse (lower row). Co-labeling of stargazin and parvalbumin antibodies shown in layer 2/3 at 63× magnification (scale = 10 μm).

    Article Snippet: Primary antibodies used for immunohistochemistry included: mouse anti-parvalbumin (Sigma, 1:1000 dilution) for co-labeling with rabbit anti-GluA4 (Millipore, 3 mg/ml); mouse anti-stargazin (Neuromab, 1:10 dilution) for co-labeling with rabbit anti-parvalbumin (Novus Biologicals), and rabbit anti-GluA4 as above.

    Techniques: Expressing, Labeling