m0290  (New England Biolabs)


Bioz Verified Symbol New England Biolabs is a verified supplier
Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    Name:
    Alkaline Phosphatase Calf Intest CIP
    Description:
    Alkaline Phosphatase Calf Intest CIP 5 000 units
    Catalog Number:
    m0290l
    Price:
    342
    Size:
    5 000 units
    Category:
    Alkaline Phosphatases
    Buy from Supplier


    Structured Review

    New England Biolabs m0290
    Alkaline Phosphatase Calf Intest CIP
    Alkaline Phosphatase Calf Intest CIP 5 000 units
    https://www.bioz.com/result/m0290/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    m0290 - by Bioz Stars, 2020-08
    99/100 stars

    Related Products / Commonly Used Together

    calf intestinal -- cip
    alkaline phosphatase
    dephosphorylation

    Images

    Related Articles

    Transfection:

    Article Title: Regulation of Herpes Simplex Virus 2 Protein Kinase UL13 by Phosphorylation and Its Role in Viral Pathogenesis
    Article Snippet: .. Lysates of Vero cells that had been infected with wild-type HSV-2 186 at an MOI of 3 for 24 h and lysates of HEK293T cells that had been transfected with pEGFP-EF-1δ(F) were treated with calf intestinal alkaline phosphatase (CIP) (New England BioLabs) as described previously ( ). .. Vero and U2OS cells were infected with each of the recombinant viruses at an MOI of 0.0001, and plaque sizes were determined as described previously ( ).

    Activation Assay:

    Article Title: Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells
    Article Snippet: .. For studying JNK activation, after the Western transfer, the membrane was further treated with calf intestinal alkaline phosphatase (CIP) (New England Biolabs) for about 2 h at 37 °C. ..

    Infection:

    Article Title: Regulation of Herpes Simplex Virus 2 Protein Kinase UL13 by Phosphorylation and Its Role in Viral Pathogenesis
    Article Snippet: .. Lysates of Vero cells that had been infected with wild-type HSV-2 186 at an MOI of 3 for 24 h and lysates of HEK293T cells that had been transfected with pEGFP-EF-1δ(F) were treated with calf intestinal alkaline phosphatase (CIP) (New England BioLabs) as described previously ( ). .. Vero and U2OS cells were infected with each of the recombinant viruses at an MOI of 0.0001, and plaque sizes were determined as described previously ( ).

    Purification:

    Article Title: “Pocket-sized RNA-Seq”: A Method to Capture New Mature microRNA Produced from a Genomic Region of Interest
    Article Snippet: .. One microgram of bait RNA was therefore dephosphorylated using 1 U CIP (Alkaline Phosphatase, Calf Intestinal, New England Biolabs, Evry, France) at 37 °C for 60 min and RNAs were purified by phenol-chloroform extraction. .. RNA Sample Preparation RNA samples that will be hybridized to the bait were isolated from MCF-7 breast cancer cells or primary myoblasts with TRI reagent (Sigma) as previously described [ , ].

    Concentration Assay:

    Article Title: HIV-1-Tat Protein Inhibits SC35-mediated Tau Exon 10 Inclusion through Up-regulation of DYRK1A Kinase *
    Article Snippet: .. Lysates (30 μg) were incubated with or without calf intestinal alkaline phosphatase at the concentration of 1 unit/μg of protein in CutSmart buffer, both obtained from New England Biolabs (Ipswich, MA). .. The reaction was supplemented with 1 m m protease inhibitor mixture and PMSF and incubated for 30 min at 37 °C.

    Incubation:

    Article Title: HIV-1-Tat Protein Inhibits SC35-mediated Tau Exon 10 Inclusion through Up-regulation of DYRK1A Kinase *
    Article Snippet: .. Lysates (30 μg) were incubated with or without calf intestinal alkaline phosphatase at the concentration of 1 unit/μg of protein in CutSmart buffer, both obtained from New England Biolabs (Ipswich, MA). .. The reaction was supplemented with 1 m m protease inhibitor mixture and PMSF and incubated for 30 min at 37 °C.

    De-Phosphorylation Assay:

    Article Title: Regulation and Substrate Specificity of the SR Protein Kinase Clk/Sty
    Article Snippet: .. Tyr-dephosphorylated Clk/Sty (PTP-Clk/Sty) and unphosphorylated Clk/Sty (CIP-Clk/Sty) were prepared by adding 200 U of protein tyrosine phosphatase (PTP) (Boehringer Mannheim) and 40 U of calf intestinal alkaline phosphatase (CIP) (New England Biolabs), respectively, to 400 μg of P-Clk/Sty bound to glutathione beads, and dephosphorylation was carried out according to the manufacturers' instructions. ..

    Article Title: Biochemical and Genetic Requirements for Function of the Immune Response Regulator BOTRYTIS-INDUCED KINASE1 in Plant Growth, Ethylene Signaling, and PAMP-Triggered Immunity in Arabidopsis [C] [C] [W]
    Article Snippet: .. Protein dephosphorylation was performed using calf intestinal alkaline phosphatase (CIP) according to the manufacturer’s protocol (New England Biolabs) with ~1 to 2.5 units of CIP (as indicated)/μg protein. .. Total RNA was isolated with Trizol reagent according to the manufacturer’s instructions (Invitrogen).

    Western Blot:

    Article Title: Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells
    Article Snippet: .. For studying JNK activation, after the Western transfer, the membrane was further treated with calf intestinal alkaline phosphatase (CIP) (New England Biolabs) for about 2 h at 37 °C. ..

    Gel Extraction:

    Article Title: Deletion of znuA Virulence Factor Attenuates Brucella abortus and Confers Protection against Wild-Type Challenge
    Article Snippet: .. Restriction endonucleases, T4 DNA ligase, calf intestinal alkaline phosphatase, the plasmid Miniprep kit, and the DNA fragment gel extraction kit were purchased from New England Biolabs and used according to the manufacturer's specifications. .. B. abortus strain 2308 and the vaccine strain RB51 were obtained from the National Veterinary Services Laboratory, USDA (Ames, IA).

    Plasmid Preparation:

    Article Title: Deletion of znuA Virulence Factor Attenuates Brucella abortus and Confers Protection against Wild-Type Challenge
    Article Snippet: .. Restriction endonucleases, T4 DNA ligase, calf intestinal alkaline phosphatase, the plasmid Miniprep kit, and the DNA fragment gel extraction kit were purchased from New England Biolabs and used according to the manufacturer's specifications. .. B. abortus strain 2308 and the vaccine strain RB51 were obtained from the National Veterinary Services Laboratory, USDA (Ames, IA).

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    New England Biolabs calf intestinal alkaline phosphatase cip
    Ser/Thr and Tyr autophosphorylation independently influence substrate specificity. Increasing amounts (8, 20, and 50 ng) of P-Clk/Sty (lanes 2 to 4), <t>PTP-Clk/Sty</t> (lanes 5 to 7), and <t>CIP-Clk/Sty</t> (lanes 8 to 10) were added to splicing reactions performed with S100 extracts in the presence of phosphatase inhibitors and ASF/SF2 (A) or SC35 (B). Reaction mixtures were deproteinized after 80 min, and RNAs were precipitated with ethanol. RNAs were fractionated by 5% denaturing PAGE and visualized by autoradiography.
    Calf Intestinal Alkaline Phosphatase Cip, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/calf intestinal alkaline phosphatase cip/product/New England Biolabs
    Average 99 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    calf intestinal alkaline phosphatase cip - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    Image Search Results


    Ser/Thr and Tyr autophosphorylation independently influence substrate specificity. Increasing amounts (8, 20, and 50 ng) of P-Clk/Sty (lanes 2 to 4), PTP-Clk/Sty (lanes 5 to 7), and CIP-Clk/Sty (lanes 8 to 10) were added to splicing reactions performed with S100 extracts in the presence of phosphatase inhibitors and ASF/SF2 (A) or SC35 (B). Reaction mixtures were deproteinized after 80 min, and RNAs were precipitated with ethanol. RNAs were fractionated by 5% denaturing PAGE and visualized by autoradiography.

    Journal: Molecular and Cellular Biology

    Article Title: Regulation and Substrate Specificity of the SR Protein Kinase Clk/Sty

    doi: 10.1128/MCB.23.12.4139-4149.2003

    Figure Lengend Snippet: Ser/Thr and Tyr autophosphorylation independently influence substrate specificity. Increasing amounts (8, 20, and 50 ng) of P-Clk/Sty (lanes 2 to 4), PTP-Clk/Sty (lanes 5 to 7), and CIP-Clk/Sty (lanes 8 to 10) were added to splicing reactions performed with S100 extracts in the presence of phosphatase inhibitors and ASF/SF2 (A) or SC35 (B). Reaction mixtures were deproteinized after 80 min, and RNAs were precipitated with ethanol. RNAs were fractionated by 5% denaturing PAGE and visualized by autoradiography.

    Article Snippet: Tyr-dephosphorylated Clk/Sty (PTP-Clk/Sty) and unphosphorylated Clk/Sty (CIP-Clk/Sty) were prepared by adding 200 U of protein tyrosine phosphatase (PTP) (Boehringer Mannheim) and 40 U of calf intestinal alkaline phosphatase (CIP) (New England Biolabs), respectively, to 400 μg of P-Clk/Sty bound to glutathione beads, and dephosphorylation was carried out according to the manufacturers' instructions.

    Techniques: Polyacrylamide Gel Electrophoresis, Autoradiography

    Autophosphorylation of Clk/Sty modulates kinase activity towards ASF/SF2 but not SRp40. (A) Increasing amounts of P-Clk/Sty (1, 5, and 20 ng) and equivalent amounts of PTP- and CIP-Clk/Sty were incubated with 1 μg of MBP under kinase conditions. Reactions were stopped by adding 1/2 volume of 3× SDS sample buffer, and proteins were fractionated by 10% SDS-PAGE and detected by autoradiography. (B and C) Increasing amounts of P-Clk/Sty (5, 20, and 100 ng) or equivalent amounts of PTP- and CIP-Clk/Sty were added to 1 μg of ASF/SF2 (B) or SRp40 (C) purified from E. coli and incubated for 30 min at 37°C. Reactions were processed as described for panel A except that proteins were transferred to nitrocellulose following PAGE. The extent of γ- 32 P incorporation was visualized by autoradiography (lanes 1 to 10). Subsequently, blots were incubated with the monoclonal antibody mAb104 (lanes 11 to 20) and reactivity was detected by chemiluminescence.

    Journal: Molecular and Cellular Biology

    Article Title: Regulation and Substrate Specificity of the SR Protein Kinase Clk/Sty

    doi: 10.1128/MCB.23.12.4139-4149.2003

    Figure Lengend Snippet: Autophosphorylation of Clk/Sty modulates kinase activity towards ASF/SF2 but not SRp40. (A) Increasing amounts of P-Clk/Sty (1, 5, and 20 ng) and equivalent amounts of PTP- and CIP-Clk/Sty were incubated with 1 μg of MBP under kinase conditions. Reactions were stopped by adding 1/2 volume of 3× SDS sample buffer, and proteins were fractionated by 10% SDS-PAGE and detected by autoradiography. (B and C) Increasing amounts of P-Clk/Sty (5, 20, and 100 ng) or equivalent amounts of PTP- and CIP-Clk/Sty were added to 1 μg of ASF/SF2 (B) or SRp40 (C) purified from E. coli and incubated for 30 min at 37°C. Reactions were processed as described for panel A except that proteins were transferred to nitrocellulose following PAGE. The extent of γ- 32 P incorporation was visualized by autoradiography (lanes 1 to 10). Subsequently, blots were incubated with the monoclonal antibody mAb104 (lanes 11 to 20) and reactivity was detected by chemiluminescence.

    Article Snippet: Tyr-dephosphorylated Clk/Sty (PTP-Clk/Sty) and unphosphorylated Clk/Sty (CIP-Clk/Sty) were prepared by adding 200 U of protein tyrosine phosphatase (PTP) (Boehringer Mannheim) and 40 U of calf intestinal alkaline phosphatase (CIP) (New England Biolabs), respectively, to 400 μg of P-Clk/Sty bound to glutathione beads, and dephosphorylation was carried out according to the manufacturers' instructions.

    Techniques: Activity Assay, Incubation, SDS Page, Autoradiography, Purification, Polyacrylamide Gel Electrophoresis

    Clk/Sty is autophosphorylated on Ser/Thr and Thr. (A) A total of 1 μg each of GST-Clk/Sty (lane 1) and a kinase-inactive mutant (GST-ClkR/Sty; lane 2) was fractionated by 10% SDS-PAGE and stained with Coomassie blue. The species indicated by the asterisk reflects an N-terminal truncation consisting of GST plus an approximately 10-kDa segment of Clk/Sty, which became phosphorylated in the wild-type but not the mutant sample. (B) A total of 0.5 μg of P-, PTP-, and CIP-Clk/Sty (lanes 1 to 3, respectively), was fractionated by 10% SDS-PAGE and stained with Coomassie blue. (C) A total of 20 to 50 ng of P-Clk/Sty (lane 1), PTP-Clk/Sty (lane 2), and CIP-Clk/Sty (lane 3) was fractionated by 10% SDS-PAGE and transferred to nitrocellulose. The blot was probed with antiphosphotyrosine antibody, and proteins were detected by chemiluminescence.

    Journal: Molecular and Cellular Biology

    Article Title: Regulation and Substrate Specificity of the SR Protein Kinase Clk/Sty

    doi: 10.1128/MCB.23.12.4139-4149.2003

    Figure Lengend Snippet: Clk/Sty is autophosphorylated on Ser/Thr and Thr. (A) A total of 1 μg each of GST-Clk/Sty (lane 1) and a kinase-inactive mutant (GST-ClkR/Sty; lane 2) was fractionated by 10% SDS-PAGE and stained with Coomassie blue. The species indicated by the asterisk reflects an N-terminal truncation consisting of GST plus an approximately 10-kDa segment of Clk/Sty, which became phosphorylated in the wild-type but not the mutant sample. (B) A total of 0.5 μg of P-, PTP-, and CIP-Clk/Sty (lanes 1 to 3, respectively), was fractionated by 10% SDS-PAGE and stained with Coomassie blue. (C) A total of 20 to 50 ng of P-Clk/Sty (lane 1), PTP-Clk/Sty (lane 2), and CIP-Clk/Sty (lane 3) was fractionated by 10% SDS-PAGE and transferred to nitrocellulose. The blot was probed with antiphosphotyrosine antibody, and proteins were detected by chemiluminescence.

    Article Snippet: Tyr-dephosphorylated Clk/Sty (PTP-Clk/Sty) and unphosphorylated Clk/Sty (CIP-Clk/Sty) were prepared by adding 200 U of protein tyrosine phosphatase (PTP) (Boehringer Mannheim) and 40 U of calf intestinal alkaline phosphatase (CIP) (New England Biolabs), respectively, to 400 μg of P-Clk/Sty bound to glutathione beads, and dephosphorylation was carried out according to the manufacturers' instructions.

    Techniques: Mutagenesis, SDS Page, Staining

    BIK1 Conserved Residues and in Vitro and in Vivo Kinase Assays. (A) Structure of the BIK1 protein and comparison of residues in the ADs of BIK1 and related kinases. Gray region denotes the KD and black the AD. Residues noted in the BIK1 protein indicate those substituted for in planta assays. (B) Kinase activity of recombinant BIK1 and Ala substitution mutants produced in E. coli detected by autoradiogram. CCB, Coomassie blue staining. (C) and (D) BIK1 substitution mutants in vivo detected by a mobility shift on an HA-immunoblot or by phosphoserine/Thr-specific antibody. (E) BIK1 and MBP phosphorylation is abrogated by phosphatase treatment. Protein dephosphorylation was performed according to the manufacturer’s protocol (New England Biolabs) with ~1 to 2.5 units CIP/μg protein (left) or (~2.5 μ/μg) (right). −, Buffer; +, CIP. In (C) and (D) , plants were treated with ACC (Ac) or flg22 (Fl) for 3 h and assayed for changes in BIK1 and MBP phosphorylation activity. In (C) to (E) , in vivo BIK1 phosphorylation was detected by ACC or flagellin-induced mobility shifts observable by HA-immunoblot. The top band corresponds to phosphorylated BIK1, which is migrating slower than the unphosphorylated form. MBP phosphorylation by BIK1 was detected by immunoblots with a phosphoserine/Thr-specific antibody.

    Journal: The Plant Cell

    Article Title: Biochemical and Genetic Requirements for Function of the Immune Response Regulator BOTRYTIS-INDUCED KINASE1 in Plant Growth, Ethylene Signaling, and PAMP-Triggered Immunity in Arabidopsis [C] [C] [W]

    doi: 10.1105/tpc.111.087122

    Figure Lengend Snippet: BIK1 Conserved Residues and in Vitro and in Vivo Kinase Assays. (A) Structure of the BIK1 protein and comparison of residues in the ADs of BIK1 and related kinases. Gray region denotes the KD and black the AD. Residues noted in the BIK1 protein indicate those substituted for in planta assays. (B) Kinase activity of recombinant BIK1 and Ala substitution mutants produced in E. coli detected by autoradiogram. CCB, Coomassie blue staining. (C) and (D) BIK1 substitution mutants in vivo detected by a mobility shift on an HA-immunoblot or by phosphoserine/Thr-specific antibody. (E) BIK1 and MBP phosphorylation is abrogated by phosphatase treatment. Protein dephosphorylation was performed according to the manufacturer’s protocol (New England Biolabs) with ~1 to 2.5 units CIP/μg protein (left) or (~2.5 μ/μg) (right). −, Buffer; +, CIP. In (C) and (D) , plants were treated with ACC (Ac) or flg22 (Fl) for 3 h and assayed for changes in BIK1 and MBP phosphorylation activity. In (C) to (E) , in vivo BIK1 phosphorylation was detected by ACC or flagellin-induced mobility shifts observable by HA-immunoblot. The top band corresponds to phosphorylated BIK1, which is migrating slower than the unphosphorylated form. MBP phosphorylation by BIK1 was detected by immunoblots with a phosphoserine/Thr-specific antibody.

    Article Snippet: Protein dephosphorylation was performed using calf intestinal alkaline phosphatase (CIP) according to the manufacturer’s protocol (New England Biolabs) with ~1 to 2.5 units of CIP (as indicated)/μg protein.

    Techniques: In Vitro, In Vivo, Activity Assay, Recombinant, Produced, Staining, Mobility Shift, De-Phosphorylation Assay, Western Blot

    Activation of JNK pathway. (A) Mock-treated or Tula virus-infected cell lysates were resolved in SDS–PAGE and transferred onto nitrocellulose, the membranes were then treated (on the right) or untreated with CIP. (B) TULV-infected or mock Vero E6 cell lysates were collected at the indicated day p.i. and analyzed with antibodies against c-jun (rabbit monoclonal and rabbit polyclonal). Infection was monitored with antibody against nucleocapsid protein. β-actin was used as a loading control. (C) JNK inhibitor II SP600126 (50 μM, added every other day) blocked the cleavage of PARP in Vero E6 cells on the fifth day post-Tula virus infection.

    Journal: Virology

    Article Title: Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells

    doi: 10.1016/j.virol.2005.01.002

    Figure Lengend Snippet: Activation of JNK pathway. (A) Mock-treated or Tula virus-infected cell lysates were resolved in SDS–PAGE and transferred onto nitrocellulose, the membranes were then treated (on the right) or untreated with CIP. (B) TULV-infected or mock Vero E6 cell lysates were collected at the indicated day p.i. and analyzed with antibodies against c-jun (rabbit monoclonal and rabbit polyclonal). Infection was monitored with antibody against nucleocapsid protein. β-actin was used as a loading control. (C) JNK inhibitor II SP600126 (50 μM, added every other day) blocked the cleavage of PARP in Vero E6 cells on the fifth day post-Tula virus infection.

    Article Snippet: For studying JNK activation, after the Western transfer, the membrane was further treated with calf intestinal alkaline phosphatase (CIP) (New England Biolabs) for about 2 h at 37 °C.

    Techniques: Activation Assay, Infection, SDS Page

    Characterization of the anti-EF-1δ-S133 P monoclonal antibody. (A) HEK293T cells were transfected with a plasmid expressing EGFP-EF-1δ(F) (lane 1 and 2) or a plasmid expressing EGFP-EF-1δS133A(F) (lane 3) and harvested at 48 h posttransfection. Cell lysates were mock treated (lanes 1 and 3) or treated with CIP (lane 2) and then analyzed by immunoblotting with anti-Flag monoclonal antibody (top), anti-EF-1δ-S133 P monoclonal antibody (middle), or anti-β-actin monoclonal antibody (bottom). β-Actin was used as a loading control. (B) U2OS cells were mock infected (lane 1) or infected with wild-type HSV-2 186 (lane 2), YK862 (ΔUL13) (lane 3), or YK863 (ΔUL13-repair) (lane 4) at an MOI of 3 and harvested at 24 h postinfection, and lysates were analyzed by immunoblotting with the indicated antibodies. α-Tubulin and UL37 were used as a loading control and an infection indicator, respectively. (C) U2OS cells were mock infected (lanes 1) or infected with wild-type HSV-2 186 (lane 2), YK864 (UL13-K176M) (lane 3), or YK865 (UL13-K176M-repair) (lane 4) and harvested, and lysates were analyzed as described above for panel B. Molecular mass markers are shown on the left.

    Journal: Journal of Virology

    Article Title: Regulation of Herpes Simplex Virus 2 Protein Kinase UL13 by Phosphorylation and Its Role in Viral Pathogenesis

    doi: 10.1128/JVI.00807-18

    Figure Lengend Snippet: Characterization of the anti-EF-1δ-S133 P monoclonal antibody. (A) HEK293T cells were transfected with a plasmid expressing EGFP-EF-1δ(F) (lane 1 and 2) or a plasmid expressing EGFP-EF-1δS133A(F) (lane 3) and harvested at 48 h posttransfection. Cell lysates were mock treated (lanes 1 and 3) or treated with CIP (lane 2) and then analyzed by immunoblotting with anti-Flag monoclonal antibody (top), anti-EF-1δ-S133 P monoclonal antibody (middle), or anti-β-actin monoclonal antibody (bottom). β-Actin was used as a loading control. (B) U2OS cells were mock infected (lane 1) or infected with wild-type HSV-2 186 (lane 2), YK862 (ΔUL13) (lane 3), or YK863 (ΔUL13-repair) (lane 4) at an MOI of 3 and harvested at 24 h postinfection, and lysates were analyzed by immunoblotting with the indicated antibodies. α-Tubulin and UL37 were used as a loading control and an infection indicator, respectively. (C) U2OS cells were mock infected (lanes 1) or infected with wild-type HSV-2 186 (lane 2), YK864 (UL13-K176M) (lane 3), or YK865 (UL13-K176M-repair) (lane 4) and harvested, and lysates were analyzed as described above for panel B. Molecular mass markers are shown on the left.

    Article Snippet: Lysates of Vero cells that had been infected with wild-type HSV-2 186 at an MOI of 3 for 24 h and lysates of HEK293T cells that had been transfected with pEGFP-EF-1δ(F) were treated with calf intestinal alkaline phosphatase (CIP) (New England BioLabs) as described previously ( ).

    Techniques: Transfection, Plasmid Preparation, Expressing, Infection