calf liver rna  (Millipore)


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  • 99
    Name:
    Ribonucleic acid from calf liver
    Description:

    Catalog Number:
    r7250
    Price:
    None
    Applications:
    Ribonucleic acid (RNA) from calf liver may be used as a substrate for studying ribonuclease activities of enzymes such as RNAase(s). RNA from calf liver may also be used as a substrate to study the effects of various reactive nitrogen species on nucleotides.
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    Structured Review

    Millipore calf liver rna
    Subtraction of <t>DNA,</t> <t>RNA</t> and protein spectra from the spect1 for positions 1 and 2. DNA, RNA and protein stack-files were subtracted sequentially from spect1 resulting in spect2D, spect2R and spect3, respectively. C, N, and O are photon energy regions of the K absorption edges for carbon, nitrogen and oxygen. Location of the positions 1 (green) and 2 (blue) were shown in the lower figure. Spect2D in the position 1 was not appeared in the figure.

    https://www.bioz.com/result/calf liver rna/product/Millipore
    Average 99 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    calf liver rna - by Bioz Stars, 2020-04
    99/100 stars

    Related Products / Commonly Used Together

    bovine serum albumin bsa
    calf thymus dna

    Images

    1) Product Images from "Discrimination of DNA and RNA distribution in a mammalian cell by scanning transmission soft X-ray microscopy"

    Article Title: Discrimination of DNA and RNA distribution in a mammalian cell by scanning transmission soft X-ray microscopy

    Journal: Journal of X-Ray Science and Technology

    doi: 10.3233/XST-180392

    Subtraction of DNA, RNA and protein spectra from the spect1 for positions 1 and 2. DNA, RNA and protein stack-files were subtracted sequentially from spect1 resulting in spect2D, spect2R and spect3, respectively. C, N, and O are photon energy regions of the K absorption edges for carbon, nitrogen and oxygen. Location of the positions 1 (green) and 2 (blue) were shown in the lower figure. Spect2D in the position 1 was not appeared in the figure.
    Figure Legend Snippet: Subtraction of DNA, RNA and protein spectra from the spect1 for positions 1 and 2. DNA, RNA and protein stack-files were subtracted sequentially from spect1 resulting in spect2D, spect2R and spect3, respectively. C, N, and O are photon energy regions of the K absorption edges for carbon, nitrogen and oxygen. Location of the positions 1 (green) and 2 (blue) were shown in the lower figure. Spect2D in the position 1 was not appeared in the figure.

    Techniques Used:

    Soft X-ray absorption spectra of DNA, RNA and BSA at the photon energy regions of carbon, nitrogen and oxygen K absorption edge. Each spectrum was adjusted to be the same level at the left end of the photon energy.
    Figure Legend Snippet: Soft X-ray absorption spectra of DNA, RNA and BSA at the photon energy regions of carbon, nitrogen and oxygen K absorption edge. Each spectrum was adjusted to be the same level at the left end of the photon energy.

    Techniques Used:

    RGB expression and optical density expression at the photon energy of 398 eV with gray scale of the CHO image. For RGB expression (a), DNA, RNA and protein are displayed as red, green and blue, respectively. Original (spect1) absorption image (b), DNA image (c), RNA image (d), protein image (e) and residual (spect3) image (f) at the photon energy of 398 eV are displayed with the gray scale of optical density.
    Figure Legend Snippet: RGB expression and optical density expression at the photon energy of 398 eV with gray scale of the CHO image. For RGB expression (a), DNA, RNA and protein are displayed as red, green and blue, respectively. Original (spect1) absorption image (b), DNA image (c), RNA image (d), protein image (e) and residual (spect3) image (f) at the photon energy of 398 eV are displayed with the gray scale of optical density.

    Techniques Used: Expressing

    DNA (a) and RNA (b) images obtained by the SVD method in aXis2000 program. The scale bar is 5 μ m.
    Figure Legend Snippet: DNA (a) and RNA (b) images obtained by the SVD method in aXis2000 program. The scale bar is 5 μ m.

    Techniques Used:

    2) Product Images from "Discrimination of DNA and RNA distribution in a mammalian cell by scanning transmission soft X-ray microscopy"

    Article Title: Discrimination of DNA and RNA distribution in a mammalian cell by scanning transmission soft X-ray microscopy

    Journal: Journal of X-Ray Science and Technology

    doi: 10.3233/XST-180392

    Subtraction of DNA, RNA and protein spectra from the spect1 for positions 1 and 2. DNA, RNA and protein stack-files were subtracted sequentially from spect1 resulting in spect2D, spect2R and spect3, respectively. C, N, and O are photon energy regions of the K absorption edges for carbon, nitrogen and oxygen. Location of the positions 1 (green) and 2 (blue) were shown in the lower figure. Spect2D in the position 1 was not appeared in the figure.
    Figure Legend Snippet: Subtraction of DNA, RNA and protein spectra from the spect1 for positions 1 and 2. DNA, RNA and protein stack-files were subtracted sequentially from spect1 resulting in spect2D, spect2R and spect3, respectively. C, N, and O are photon energy regions of the K absorption edges for carbon, nitrogen and oxygen. Location of the positions 1 (green) and 2 (blue) were shown in the lower figure. Spect2D in the position 1 was not appeared in the figure.

    Techniques Used:

    Soft X-ray absorption spectra of DNA, RNA and BSA at the photon energy regions of carbon, nitrogen and oxygen K absorption edge. Each spectrum was adjusted to be the same level at the left end of the photon energy.
    Figure Legend Snippet: Soft X-ray absorption spectra of DNA, RNA and BSA at the photon energy regions of carbon, nitrogen and oxygen K absorption edge. Each spectrum was adjusted to be the same level at the left end of the photon energy.

    Techniques Used:

    RGB expression and optical density expression at the photon energy of 398 eV with gray scale of the CHO image. For RGB expression (a), DNA, RNA and protein are displayed as red, green and blue, respectively. Original (spect1) absorption image (b), DNA image (c), RNA image (d), protein image (e) and residual (spect3) image (f) at the photon energy of 398 eV are displayed with the gray scale of optical density.
    Figure Legend Snippet: RGB expression and optical density expression at the photon energy of 398 eV with gray scale of the CHO image. For RGB expression (a), DNA, RNA and protein are displayed as red, green and blue, respectively. Original (spect1) absorption image (b), DNA image (c), RNA image (d), protein image (e) and residual (spect3) image (f) at the photon energy of 398 eV are displayed with the gray scale of optical density.

    Techniques Used: Expressing

    DNA (a) and RNA (b) images obtained by the SVD method in aXis2000 program. The scale bar is 5 μ m.
    Figure Legend Snippet: DNA (a) and RNA (b) images obtained by the SVD method in aXis2000 program. The scale bar is 5 μ m.

    Techniques Used:

    Related Articles

    SYBR Green Assay:

    Article Title: Muscle characteristics in chicks challenged with Salmonella Enteritidis and the effect of preventive application of the probiotic Enterococcus faecium
    Article Snippet: .. The RNA content of muscle homogenates (diluted 1:80) was quantified fluorometrically with SYBR Green II against a calf liver RNA standard (Sigma-Aldrich GmbH, Steinheim, Germany) as published by Oksbjerg et al. ( ). .. DNA and RNA assays were performed in 96-well quartz microwell plates by using a Flx-800-I microplate fluorescence reader (Bio-Tek Instruments Inc., Bad Friedrichshall, Germany).

    Concentration Assay:

    Article Title: Discrimination of DNA and RNA distribution in a mammalian cell by scanning transmission soft X-ray microscopy
    Article Snippet: .. Calf thymus DNA, calf liver RNA and bovine serum albumin (BSA) were purchased from Sigma-Aldrich Co., dissolved in water at the concentration of 2 mg/ml, dropped on a silicon nitride membrane and dried. ..

    Fluorescence:

    Article Title: Muscle characteristics in chicks challenged with Salmonella Enteritidis and the effect of preventive application of the probiotic Enterococcus faecium
    Article Snippet: The RNA content of muscle homogenates (diluted 1:80) was quantified fluorometrically with SYBR Green II against a calf liver RNA standard (Sigma-Aldrich GmbH, Steinheim, Germany) as published by Oksbjerg et al. ( ). .. DNA and RNA assays were performed in 96-well quartz microwell plates by using a Flx-800-I microplate fluorescence reader (Bio-Tek Instruments Inc., Bad Friedrichshall, Germany).

    Cell Culture:

    Article Title: Discrimination of DNA and RNA distribution in a mammalian cell by scanning transmission soft X-ray microscopy
    Article Snippet: 2 Materials and methods Cultured CHO cells derived from Chinese hamster ovary were plated on a silicon nitride membrane (thickness, 100 nm; purchased from Silson Ltd, England) and grown in HAM F12 medium (purchased from Sigma-Aldrich Co.) supplemented with 10% fetal bovine serum and antibiotics at 37°C in a humidified 5% CO2 atmosphere. .. Calf thymus DNA, calf liver RNA and bovine serum albumin (BSA) were purchased from Sigma-Aldrich Co., dissolved in water at the concentration of 2 mg/ml, dropped on a silicon nitride membrane and dried.

    Derivative Assay:

    Article Title: Discrimination of DNA and RNA distribution in a mammalian cell by scanning transmission soft X-ray microscopy
    Article Snippet: 2 Materials and methods Cultured CHO cells derived from Chinese hamster ovary were plated on a silicon nitride membrane (thickness, 100 nm; purchased from Silson Ltd, England) and grown in HAM F12 medium (purchased from Sigma-Aldrich Co.) supplemented with 10% fetal bovine serum and antibiotics at 37°C in a humidified 5% CO2 atmosphere. .. Calf thymus DNA, calf liver RNA and bovine serum albumin (BSA) were purchased from Sigma-Aldrich Co., dissolved in water at the concentration of 2 mg/ml, dropped on a silicon nitride membrane and dried.

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  • 86
    Millipore e cadherin ntf
    Hp HtrA cleaves <t>E-cadherin</t> on the cell surface. ( A ) Recombinant E-cadherin was incubated with decreasing amounts of purified Hp HtrA wt or inactive Hp HtrA SA . E-Cad rec., <t>NTF</t> and Hp HtrA were detected. ( B ) E-Cad rec. was incubated with increasing amounts of hHtrA1. E-Cad rec., NTF and HtrA were detected by western blots. Putative NTF fragments are indicated by asterisks ( * ). ( C ) Detached MKN-28 cells were incubated in culture medium for 3 h for re-expression of E-Cad-FL, followed by treatment with HtrA wt or HtrA SA for 16 h. Formation of NTF, loss of E-Cad-FL, Hp HtrA and equal GAPDH expression were detected. ( D ) MKN-28 cells were treated with control or hHtrA1-specific siRNA for 48 h. Downregulation of hHtrA1 was demonstrated by western blot using an hHtrA1-specific antibody. β-Actin is shown as a control (left panel). Transfected cells were then infected with H. pylori for 16 h. NTF was detected in the supernatants of cells; loss of E-Cad-FL and GAPDH are shown in the lysates of transfected cells (right panel). E-Cad rec., recombinant E-cadherin containing the extracellular domain; E-Cad-FL, full-length 125-kDa E-cadherin; Hp , Helicobacter pylori ; HtrA, high-temperature requirement A; siRNA, short interfering RNA.
    E Cadherin Ntf, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e cadherin ntf/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    e cadherin ntf - by Bioz Stars, 2020-04
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    Image Search Results


    Hp HtrA cleaves E-cadherin on the cell surface. ( A ) Recombinant E-cadherin was incubated with decreasing amounts of purified Hp HtrA wt or inactive Hp HtrA SA . E-Cad rec., NTF and Hp HtrA were detected. ( B ) E-Cad rec. was incubated with increasing amounts of hHtrA1. E-Cad rec., NTF and HtrA were detected by western blots. Putative NTF fragments are indicated by asterisks ( * ). ( C ) Detached MKN-28 cells were incubated in culture medium for 3 h for re-expression of E-Cad-FL, followed by treatment with HtrA wt or HtrA SA for 16 h. Formation of NTF, loss of E-Cad-FL, Hp HtrA and equal GAPDH expression were detected. ( D ) MKN-28 cells were treated with control or hHtrA1-specific siRNA for 48 h. Downregulation of hHtrA1 was demonstrated by western blot using an hHtrA1-specific antibody. β-Actin is shown as a control (left panel). Transfected cells were then infected with H. pylori for 16 h. NTF was detected in the supernatants of cells; loss of E-Cad-FL and GAPDH are shown in the lysates of transfected cells (right panel). E-Cad rec., recombinant E-cadherin containing the extracellular domain; E-Cad-FL, full-length 125-kDa E-cadherin; Hp , Helicobacter pylori ; HtrA, high-temperature requirement A; siRNA, short interfering RNA.

    Journal: EMBO Reports

    Article Title: Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion

    doi: 10.1038/embor.2010.114

    Figure Lengend Snippet: Hp HtrA cleaves E-cadherin on the cell surface. ( A ) Recombinant E-cadherin was incubated with decreasing amounts of purified Hp HtrA wt or inactive Hp HtrA SA . E-Cad rec., NTF and Hp HtrA were detected. ( B ) E-Cad rec. was incubated with increasing amounts of hHtrA1. E-Cad rec., NTF and HtrA were detected by western blots. Putative NTF fragments are indicated by asterisks ( * ). ( C ) Detached MKN-28 cells were incubated in culture medium for 3 h for re-expression of E-Cad-FL, followed by treatment with HtrA wt or HtrA SA for 16 h. Formation of NTF, loss of E-Cad-FL, Hp HtrA and equal GAPDH expression were detected. ( D ) MKN-28 cells were treated with control or hHtrA1-specific siRNA for 48 h. Downregulation of hHtrA1 was demonstrated by western blot using an hHtrA1-specific antibody. β-Actin is shown as a control (left panel). Transfected cells were then infected with H. pylori for 16 h. NTF was detected in the supernatants of cells; loss of E-Cad-FL and GAPDH are shown in the lysates of transfected cells (right panel). E-Cad rec., recombinant E-cadherin containing the extracellular domain; E-Cad-FL, full-length 125-kDa E-cadherin; Hp , Helicobacter pylori ; HtrA, high-temperature requirement A; siRNA, short interfering RNA.

    Article Snippet: Monoclonal antibodies HecD1 and H-108 against the extracellular domain of E-cadherin (NTF) were obtained from Calbiochem and Santa Cruz, respectively.

    Techniques: Recombinant, Incubation, Purification, Western Blot, Expressing, Transfection, Infection, Small Interfering RNA

    Helicobacter pylori induces ectodomain E-cadherin shedding independently of host proteases. ( A ) E-cadherin has five extracellular domains (EC1–EC5), a transmembrane domain and an intracellular domain. Cleavage by host proteases generates an extracellular N-terminal fragment (NTF) and two C-terminal fragments (CTF1 and CTF2). ( B ) MKN-28 cells were infected with H. pylori as indicated and the soluble 85-kDa E-cadherin fragment (NTF) was detected in the supernatant of host cells by using western blots with the E-cadherin ectodomain antibody. Loss of E-Cad-FL in whole-cell lysates was confirmed using an antibody detecting intracellular CTF1 and CTF2. GAPDH is shown as a control. ( C ) MKN-28 cells were preincubated with 150 nM MMP inhibitor II (MMP-Inh.; 5 × IC 50 ) or treated with ADAM10 siRNA followed by infection with H. pylori . Soluble NTF in supernatants and E-Cad-FL in whole-cell lysates were detected. Mature ADAM10 (60 kDa) and GAPDH are shown as controls. ADAM10, a disintegrin and metallopeptidase 10; E-Cad-FL, full-length 125-kDa E-cadherin; MMP, matrix metalloprotease; siRNA, short interfering RNA.

    Journal: EMBO Reports

    Article Title: Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion

    doi: 10.1038/embor.2010.114

    Figure Lengend Snippet: Helicobacter pylori induces ectodomain E-cadherin shedding independently of host proteases. ( A ) E-cadherin has five extracellular domains (EC1–EC5), a transmembrane domain and an intracellular domain. Cleavage by host proteases generates an extracellular N-terminal fragment (NTF) and two C-terminal fragments (CTF1 and CTF2). ( B ) MKN-28 cells were infected with H. pylori as indicated and the soluble 85-kDa E-cadherin fragment (NTF) was detected in the supernatant of host cells by using western blots with the E-cadherin ectodomain antibody. Loss of E-Cad-FL in whole-cell lysates was confirmed using an antibody detecting intracellular CTF1 and CTF2. GAPDH is shown as a control. ( C ) MKN-28 cells were preincubated with 150 nM MMP inhibitor II (MMP-Inh.; 5 × IC 50 ) or treated with ADAM10 siRNA followed by infection with H. pylori . Soluble NTF in supernatants and E-Cad-FL in whole-cell lysates were detected. Mature ADAM10 (60 kDa) and GAPDH are shown as controls. ADAM10, a disintegrin and metallopeptidase 10; E-Cad-FL, full-length 125-kDa E-cadherin; MMP, matrix metalloprotease; siRNA, short interfering RNA.

    Article Snippet: Monoclonal antibodies HecD1 and H-108 against the extracellular domain of E-cadherin (NTF) were obtained from Calbiochem and Santa Cruz, respectively.

    Techniques: Infection, Western Blot, Small Interfering RNA