proteinase k agarose beads  (Millipore)


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    Structured Review

    Millipore proteinase k agarose beads
    LplA1, but not LplA2, restores growth to lipoic acid auxotrophs in the presence of lipoyl peptides ( A–F ) Growth (OD 550 ) of the indicated lipoic acid auxotrophs in RPMI supplemented with ( A ) 2.5 mg ml −1 undigested pyruvate dehydrogenase (PDH), ( B ) 2.5 mg ml −1 <t>proteinase</t> K digested PDH, ( C ) 100 μM DKA tripeptide, ( D ) 100 μM DK L A tripeptide, ( E ) 100 μM DKT tripeptide, and ( F ) 100 μM DK L T tripeptide. Strain designations are as follows: Wildtype (WT), Δ lipA Δ lplA1 (Δ A Δ A1 ) , Δ lipA Δ lplA2 (Δ A Δ A2 ), Δ lipA Δ lplA1 Δ lplA2 (Δ A Δ A1 Δ A2 ), Δ lipA Δ lplA1 Δ lplA2 + lplA1 (Δ A Δ A1 Δ A2 + A1 ), and Δ lipA Δ lplA1 Δ lplA2 + lplA2 (Δ A Δ A1 Δ A2 + A2 ).
    Proteinase K Agarose Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proteinase k agarose beads/product/Millipore
    Average 93 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    proteinase k agarose beads - by Bioz Stars, 2020-04
    93/100 stars

    Images

    1) Product Images from "Increased flexibility in the use of exogenous lipoic acid by Staphylococcus aureus"

    Article Title: Increased flexibility in the use of exogenous lipoic acid by Staphylococcus aureus

    Journal: Molecular microbiology

    doi: 10.1111/mmi.13970

    LplA1, but not LplA2, restores growth to lipoic acid auxotrophs in the presence of lipoyl peptides ( A–F ) Growth (OD 550 ) of the indicated lipoic acid auxotrophs in RPMI supplemented with ( A ) 2.5 mg ml −1 undigested pyruvate dehydrogenase (PDH), ( B ) 2.5 mg ml −1 proteinase K digested PDH, ( C ) 100 μM DKA tripeptide, ( D ) 100 μM DK L A tripeptide, ( E ) 100 μM DKT tripeptide, and ( F ) 100 μM DK L T tripeptide. Strain designations are as follows: Wildtype (WT), Δ lipA Δ lplA1 (Δ A Δ A1 ) , Δ lipA Δ lplA2 (Δ A Δ A2 ), Δ lipA Δ lplA1 Δ lplA2 (Δ A Δ A1 Δ A2 ), Δ lipA Δ lplA1 Δ lplA2 + lplA1 (Δ A Δ A1 Δ A2 + A1 ), and Δ lipA Δ lplA1 Δ lplA2 + lplA2 (Δ A Δ A1 Δ A2 + A2 ).
    Figure Legend Snippet: LplA1, but not LplA2, restores growth to lipoic acid auxotrophs in the presence of lipoyl peptides ( A–F ) Growth (OD 550 ) of the indicated lipoic acid auxotrophs in RPMI supplemented with ( A ) 2.5 mg ml −1 undigested pyruvate dehydrogenase (PDH), ( B ) 2.5 mg ml −1 proteinase K digested PDH, ( C ) 100 μM DKA tripeptide, ( D ) 100 μM DK L A tripeptide, ( E ) 100 μM DKT tripeptide, and ( F ) 100 μM DK L T tripeptide. Strain designations are as follows: Wildtype (WT), Δ lipA Δ lplA1 (Δ A Δ A1 ) , Δ lipA Δ lplA2 (Δ A Δ A2 ), Δ lipA Δ lplA1 Δ lplA2 (Δ A Δ A1 Δ A2 ), Δ lipA Δ lplA1 Δ lplA2 + lplA1 (Δ A Δ A1 Δ A2 + A1 ), and Δ lipA Δ lplA1 Δ lplA2 + lplA2 (Δ A Δ A1 Δ A2 + A2 ).

    Techniques Used:

    2) Product Images from "Gangliosides are receptors for murine polyoma virus and SV40"

    Article Title: Gangliosides are receptors for murine polyoma virus and SV40

    Journal: The EMBO Journal

    doi: 10.1093/emboj/cdg439

    Fig. 1.  Py binds to a protease-resistant receptor at the plasma membrane. ( A ) Purified Py (strain RA) was incubated in the absence of membranes or with plasma membranes pre-treated with or without proteinase K. The samples were floated in a discontinuous sucrose gradient. Fractions were collected from the top of the gradient and analyzed by SDS–PAGE and immunoblotting with a Py VP1 antibody (left panels). The proteins in the non-proteolyzed and proteolyzed plasma membranes were analyzed by SDS–PAGE followed by staining with Coomassie blue (right panel). ( B ) Purified Py (strain RA) was incubated in the absence of membranes or with plasma membranes pre-treated with or without α2,3-neuraminidase (NA). The analysis was performed as in (A). ( C ) Purified Py was incubated alone, or with yeast or bacterial membranes. The analysis was performed as in (A).
    Figure Legend Snippet: Fig. 1. Py binds to a protease-resistant receptor at the plasma membrane. ( A ) Purified Py (strain RA) was incubated in the absence of membranes or with plasma membranes pre-treated with or without proteinase K. The samples were floated in a discontinuous sucrose gradient. Fractions were collected from the top of the gradient and analyzed by SDS–PAGE and immunoblotting with a Py VP1 antibody (left panels). The proteins in the non-proteolyzed and proteolyzed plasma membranes were analyzed by SDS–PAGE followed by staining with Coomassie blue (right panel). ( B ) Purified Py (strain RA) was incubated in the absence of membranes or with plasma membranes pre-treated with or without α2,3-neuraminidase (NA). The analysis was performed as in (A). ( C ) Purified Py was incubated alone, or with yeast or bacterial membranes. The analysis was performed as in (A).

    Techniques Used: Purification, Incubation, SDS Page, Staining

    3) Product Images from "Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids"

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids

    Journal: Journal of Virology

    doi: 10.1128/JVI.01218-12

    Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with proteinase K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.
    Figure Legend Snippet: Detection of CDK2 in HBV capsids purified from HepG2 cells by Western blotting. HBV capsids (0.5 μg) were digested with proteinase K (PK) agarose beads as described in Materials and Methods. Proteinase K was then inactivated by the addition of the proteinase K inhibitor, and the sample was resolved by SDS-PAGE (lanes 8 and 10), along with the same amount of undigested capsids from the same fractions (lanes 7 and 9). Purified GST-CDK2 standards (lanes 1 to 3) and total lysate from HepG2 cells (lane 4) were loaded as controls for CDK2 detection. A sucrose fraction that did not contain HBV capsids was also treated with the proteinase K agarose beads to ensure that contaminating proteins were removed by the digestion (lane 6) or mock treated (lane 5). The capsids loaded in lanes 9 and 10 were from a capsid-positive sucrose fraction of higher purity than those loaded in lanes 7 and 8. CDK2 was detected by Western blotting using the anti-CDK2 antibody (top panel). HBc was visualized by Sypro ruby staining (bottom panel). C, core protein.

    Techniques Used: Purification, Western Blot, SDS Page, Staining

    Endogenous kinase reactions with virion-derived HBV capsids. HBV capsids were released from virions purified from the medium of HBV-transfected HepG2 cells by NP-40 treatment. One control aliquot was removed, and the remaining virion-derived capsids were digested by proteinase K. The untreated (lane 1) or proteinase K-treated (lanes 2 to 5), virion-derived capsids (ca. 6 ng per reaction) were phosphorylated by the encapsidated kinase in endogenous kinase reactions in the presence of the indicated kinase inhibitors (lanes 3 to 5) or DMSO control (lane 2). Kinase inhibitors used included CDK2 inhibitor III (lane 3, 250 μM, 500× IC 50 for CDK2), roscovitine (lane 4, 250 μM, 350× IC 50 for CDK2), and Bisindo (lane 3, 5 μM, 500× IC 50 for PKC). An equal amount of proteinase K alone was also loaded as an additional control (lane 6). In parallel, 6 ng (lane 7) or 12 ng (lane 8) of cytoplasmic HBV capsids from HepG2 cells (also treated with proteinase K; see Materials and Methods) were subjected to the endogenous kinase reaction. Half of each reaction product was resolved by agarose gel electrophoresis to visualize capsid particles (top), and proteinase K inhibitor was added to the other half to terminate the digestion before boiling in SDS sample buffer and resolving by SDS-PAGE to visualize the total core protein (bottom). The gels were dried, and labeled capsids or core proteins were detected by autoradiography. *, unknown labeled species. CA, capsids; C, core protein; PK, proteinase K; IC, intracellular.
    Figure Legend Snippet: Endogenous kinase reactions with virion-derived HBV capsids. HBV capsids were released from virions purified from the medium of HBV-transfected HepG2 cells by NP-40 treatment. One control aliquot was removed, and the remaining virion-derived capsids were digested by proteinase K. The untreated (lane 1) or proteinase K-treated (lanes 2 to 5), virion-derived capsids (ca. 6 ng per reaction) were phosphorylated by the encapsidated kinase in endogenous kinase reactions in the presence of the indicated kinase inhibitors (lanes 3 to 5) or DMSO control (lane 2). Kinase inhibitors used included CDK2 inhibitor III (lane 3, 250 μM, 500× IC 50 for CDK2), roscovitine (lane 4, 250 μM, 350× IC 50 for CDK2), and Bisindo (lane 3, 5 μM, 500× IC 50 for PKC). An equal amount of proteinase K alone was also loaded as an additional control (lane 6). In parallel, 6 ng (lane 7) or 12 ng (lane 8) of cytoplasmic HBV capsids from HepG2 cells (also treated with proteinase K; see Materials and Methods) were subjected to the endogenous kinase reaction. Half of each reaction product was resolved by agarose gel electrophoresis to visualize capsid particles (top), and proteinase K inhibitor was added to the other half to terminate the digestion before boiling in SDS sample buffer and resolving by SDS-PAGE to visualize the total core protein (bottom). The gels were dried, and labeled capsids or core proteins were detected by autoradiography. *, unknown labeled species. CA, capsids; C, core protein; PK, proteinase K; IC, intracellular.

    Techniques Used: Derivative Assay, Purification, Transfection, Agarose Gel Electrophoresis, SDS Page, Labeling, Autoradiography

    Related Articles

    Nucleic Acid Electrophoresis:

    Article Title: Mitochondrial translocation of ?-synuclein is promoted by intracellular acidification
    Article Snippet: SDS-PAGE buffer was added and solutions were incubated at 30°C for 15 minutes before gel electrophoresis and immunoblotting. .. 20 mg (20 U/ml) washed Proteinase K-Agarose beads (Sigma) were added and rocked for 30 minutes at 4°C.

    Centrifugation:

    Article Title: Increased flexibility in the use of exogenous lipoic acid by Staphylococcus aureus
    Article Snippet: Proteinase K agarose beads and porcine pyruvate dehydrogenase (PDH) were purchased from Sigma. .. Before protein digestion, the beads were washed three times by centrifugation for 3 min at 400 x g followed by resuspension in 800 μl activation buffer.

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids
    Article Snippet: HepG2 HBV capsids in sucrose fractions were digested for 1.5 h with proteinase K-agarose beads (Sigma) at 37°C with gentle agitation. .. Following the digestion, the proteinase K resin was removed by centrifugation.

    Article Title: A Protein in Crude Cytosol Regulates Glucose-6-phosphatase Activity in Crude Microsomes to Regulate Group Size in Dictyostelium
    Article Snippet: In addition, the S > 10K was treated with DNase I (Sigma) at 0.5 μ g/ μ l, RNase A (Sigma) at 15 ng/ μ l, or proteinase K agarose beads (Sigma) at 0.1 mg/ μ l for 30 min at 37 °C. .. The proteinase K-agarose beads were removed by centrifugation at 19,000 × g for 5 min, twice.

    Article Title: Cell Vacuolation Caused by Vibrio cholerae Hemolysin
    Article Snippet: Proteinase K-agarose beads (Sigma) were suspended at 1 mg/ml in distilled water and washed three times with ice-cold Tris HCl at pH 7.2, and the pellet from 1 ml of this washed suspension (1 U) was mixed with 500 μl of V. cholerae culture supernatant. .. The proteinase beads were removed by centrifugation for 1 min at 13,000 rpm (in an Eppendorf microfuge), and bead-free supernatants were then tested for vacuolating cytotoxic activity on Vero cells as described above.

    Agarose Gel Electrophoresis:

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids
    Article Snippet: HepG2 HBV capsids in sucrose fractions were digested for 1.5 h with proteinase K-agarose beads (Sigma) at 37°C with gentle agitation. .. For capsid particle analysis, proteinase K-treated capsids were loaded onto a 1% agarose gel.

    Activation Assay:

    Article Title: Increased flexibility in the use of exogenous lipoic acid by Staphylococcus aureus
    Article Snippet: Proteinase K agarose beads and porcine pyruvate dehydrogenase (PDH) were purchased from Sigma. .. The Proteinase K beads were activated by suspending 40 mg beads in 1 ml activation buffer (20 mM Tris-HCl, 1 mM CaCl2, pH 7.4) and incubated for 2 hours at room temperature.

    Size-exclusion Chromatography:

    Article Title: Mitochondrial translocation of ?-synuclein is promoted by intracellular acidification
    Article Snippet: 20 mg (20 U/ml) washed Proteinase K-Agarose beads (Sigma) were added and rocked for 30 minutes at 4°C. .. Pellets were resuspended in 0.1 ml MB buffer plus 2 mM PMSF and sonicated for 5 sec before use.

    Purification:

    Article Title: Gangliosides are receptors for murine polyoma virus and SV40
    Article Snippet: .. Purified gangliosides were purchased from Matreya, purified phosphatidyl-choline,-ethanolamine, -serine and -inositol from Avanti, proteinase K–agarose beads and 4′,6′-diamidino-2-phenylindole (DAPI) from Sigma, α2,3-neuraminidase, puromycin, antibodies against BiP and SV40 large T antigen from Calbiochem, C6 glioma cell line from ATCC, Oregon Green anti-rabbit antibodies from Molecular Probes, and rhodamine-labeled goat anti-rat antibodies from Jackson Laboratories. .. Antibodies against the Py VP1 protein, VP1, -2 and -3 proteins and Py large T antigen were generated in the Benjamin laboratory.

    Concentration Assay:

    Article Title: The Antistaphylococcal Lysin, CF-301, Activates Key Host Factors in Human Blood To Potentiate Methicillin-Resistant Staphylococcus aureus Bacteriolysis
    Article Snippet: For the supplementation of delipidated serum with fatty acids, 50-mg/ml stock solutions of either oleate in H2 O or palmitate in 100% ethanol were prepared and added to the serum to achieve a final concentration of 0.625 mg/ml; the supplemented serum was then incubated at 37°C for 1 h prior to use to promote fatty acid binding to HSA. .. The analysis of CF-301 activity in human serum pretreated for 3 h with proteinase K-agarose beads (Sigma-Aldrich) was performed according to the manufacturer’s protocol.

    Incubation:

    Article Title: Increased flexibility in the use of exogenous lipoic acid by Staphylococcus aureus
    Article Snippet: Proteinase K agarose beads and porcine pyruvate dehydrogenase (PDH) were purchased from Sigma. .. The Proteinase K beads were activated by suspending 40 mg beads in 1 ml activation buffer (20 mM Tris-HCl, 1 mM CaCl2, pH 7.4) and incubated for 2 hours at room temperature.

    Article Title: Mitochondrial translocation of ?-synuclein is promoted by intracellular acidification
    Article Snippet: SDS-PAGE buffer was added and solutions were incubated at 30°C for 15 minutes before gel electrophoresis and immunoblotting. .. 20 mg (20 U/ml) washed Proteinase K-Agarose beads (Sigma) were added and rocked for 30 minutes at 4°C.

    Article Title: The Antistaphylococcal Lysin, CF-301, Activates Key Host Factors in Human Blood To Potentiate Methicillin-Resistant Staphylococcus aureus Bacteriolysis
    Article Snippet: For the supplementation of delipidated serum with fatty acids, 50-mg/ml stock solutions of either oleate in H2 O or palmitate in 100% ethanol were prepared and added to the serum to achieve a final concentration of 0.625 mg/ml; the supplemented serum was then incubated at 37°C for 1 h prior to use to promote fatty acid binding to HSA. .. The analysis of CF-301 activity in human serum pretreated for 3 h with proteinase K-agarose beads (Sigma-Aldrich) was performed according to the manufacturer’s protocol.

    Article Title: Cell Vacuolation Caused by Vibrio cholerae Hemolysin
    Article Snippet: Proteinase K-agarose beads (Sigma) were suspended at 1 mg/ml in distilled water and washed three times with ice-cold Tris HCl at pH 7.2, and the pellet from 1 ml of this washed suspension (1 U) was mixed with 500 μl of V. cholerae culture supernatant. .. The mixture was incubated for 10 min at 4 or 25°C with 1 mM CaCl2 , or without CaCl2 as a negative control (proteinase K activity depends on Ca2+ ions).

    Activity Assay:

    Article Title: The Antistaphylococcal Lysin, CF-301, Activates Key Host Factors in Human Blood To Potentiate Methicillin-Resistant Staphylococcus aureus Bacteriolysis
    Article Snippet: .. The analysis of CF-301 activity in human serum pretreated for 3 h with proteinase K-agarose beads (Sigma-Aldrich) was performed according to the manufacturer’s protocol. ..

    Article Title: A Protein in Crude Cytosol Regulates Glucose-6-phosphatase Activity in Crude Microsomes to Regulate Group Size in Dictyostelium
    Article Snippet: To determine the nature of the glucose-6-phosphatase-inhibiting activity of wild-type S > 10K and the stimulating activity of countin − S > 10K, we subjected wild-type or countin − S > 10K to various treatments. .. In addition, the S > 10K was treated with DNase I (Sigma) at 0.5 μ g/ μ l, RNase A (Sigma) at 15 ng/ μ l, or proteinase K agarose beads (Sigma) at 0.1 mg/ μ l for 30 min at 37 °C.

    Article Title: Cell Vacuolation Caused by Vibrio cholerae Hemolysin
    Article Snippet: Proteinase K-agarose beads (Sigma) were suspended at 1 mg/ml in distilled water and washed three times with ice-cold Tris HCl at pH 7.2, and the pellet from 1 ml of this washed suspension (1 U) was mixed with 500 μl of V. cholerae culture supernatant. .. The mixture was incubated for 10 min at 4 or 25°C with 1 mM CaCl2 , or without CaCl2 as a negative control (proteinase K activity depends on Ca2+ ions).

    Negative Control:

    Article Title: Cell Vacuolation Caused by Vibrio cholerae Hemolysin
    Article Snippet: Proteinase K-agarose beads (Sigma) were suspended at 1 mg/ml in distilled water and washed three times with ice-cold Tris HCl at pH 7.2, and the pellet from 1 ml of this washed suspension (1 U) was mixed with 500 μl of V. cholerae culture supernatant. .. The mixture was incubated for 10 min at 4 or 25°C with 1 mM CaCl2 , or without CaCl2 as a negative control (proteinase K activity depends on Ca2+ ions).

    Polyacrylamide Gel Electrophoresis:

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids
    Article Snippet: HepG2 HBV capsids in sucrose fractions were digested for 1.5 h with proteinase K-agarose beads (Sigma) at 37°C with gentle agitation. .. The supernatant was collected and used for endogenous kinase reactions or sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis.

    Sonication:

    Article Title: Mitochondrial translocation of ?-synuclein is promoted by intracellular acidification
    Article Snippet: The pellet was rinsed with 0.1 M pH buffer, resuspended in an equal volume of PBS and briefly sonicated. .. 20 mg (20 U/ml) washed Proteinase K-Agarose beads (Sigma) were added and rocked for 30 minutes at 4°C.

    Western Blot:

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids
    Article Snippet: HepG2 HBV capsids in sucrose fractions were digested for 1.5 h with proteinase K-agarose beads (Sigma) at 37°C with gentle agitation. .. The supernatant was collected and used for endogenous kinase reactions or sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis.

    Binding Assay:

    Article Title: Mitochondrial translocation of ?-synuclein is promoted by intracellular acidification
    Article Snippet: 20 mg (20 U/ml) washed Proteinase K-Agarose beads (Sigma) were added and rocked for 30 minutes at 4°C. .. The same total amount of input mitochondria was used in control and carbonate/Proteinase K-treated binding reactions.

    Article Title: The Antistaphylococcal Lysin, CF-301, Activates Key Host Factors in Human Blood To Potentiate Methicillin-Resistant Staphylococcus aureus Bacteriolysis
    Article Snippet: For the supplementation of delipidated serum with fatty acids, 50-mg/ml stock solutions of either oleate in H2 O or palmitate in 100% ethanol were prepared and added to the serum to achieve a final concentration of 0.625 mg/ml; the supplemented serum was then incubated at 37°C for 1 h prior to use to promote fatty acid binding to HSA. .. The analysis of CF-301 activity in human serum pretreated for 3 h with proteinase K-agarose beads (Sigma-Aldrich) was performed according to the manufacturer’s protocol.

    SDS Page:

    Article Title: Mitochondrial translocation of ?-synuclein is promoted by intracellular acidification
    Article Snippet: SDS-PAGE buffer was added and solutions were incubated at 30°C for 15 minutes before gel electrophoresis and immunoblotting. .. 20 mg (20 U/ml) washed Proteinase K-Agarose beads (Sigma) were added and rocked for 30 minutes at 4°C.

    Article Title: Cyclin-Dependent Kinase 2 Phosphorylates S/T-P Sites in the Hepadnavirus Core Protein C-Terminal Domain and Is Incorporated into Viral Capsids
    Article Snippet: HepG2 HBV capsids in sucrose fractions were digested for 1.5 h with proteinase K-agarose beads (Sigma) at 37°C with gentle agitation. .. The supernatant was collected and used for endogenous kinase reactions or sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis.

    Generated:

    Article Title: Gangliosides are receptors for murine polyoma virus and SV40
    Article Snippet: Purified gangliosides were purchased from Matreya, purified phosphatidyl-choline,-ethanolamine, -serine and -inositol from Avanti, proteinase K–agarose beads and 4′,6′-diamidino-2-phenylindole (DAPI) from Sigma, α2,3-neuraminidase, puromycin, antibodies against BiP and SV40 large T antigen from Calbiochem, C6 glioma cell line from ATCC, Oregon Green anti-rabbit antibodies from Molecular Probes, and rhodamine-labeled goat anti-rat antibodies from Jackson Laboratories. .. Antibodies against the Py VP1 protein, VP1, -2 and -3 proteins and Py large T antigen were generated in the Benjamin laboratory.

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    Millipore proteinase a agarose beads
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    https://www.bioz.com/result/proteinase a agarose beads/product/Millipore
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