edta free buffer  (Millipore)


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    Structured Review

    Millipore edta free buffer
    Edta Free Buffer, supplied by Millipore, 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/edta free buffer/product/Millipore
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    edta free buffer - by Bioz Stars, 2020-04
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    Cell Isolation:

    Article Title: TREM-1 promotes intestinal tumorigenesis
    Article Snippet: Paragraph title: Cell isolation from murine colons and tumors ... After washing of tissue pieces with EDTA-free buffer, lamina propria (LP) cells were obtained by digestion with 100 U/ml Collagenase (Type IV, Sigma) and 50 U/ml DNase (Type I, grade II, Roche) in Ca2+ and Mg2+ -supplemented HBSS/HEPES 5% FCS for 20–30 min at 37 °C.

    Isolation:

    Article Title: TREM-1 promotes intestinal tumorigenesis
    Article Snippet: After washing of tissue pieces with EDTA-free buffer, lamina propria (LP) cells were obtained by digestion with 100 U/ml Collagenase (Type IV, Sigma) and 50 U/ml DNase (Type I, grade II, Roche) in Ca2+ and Mg2+ -supplemented HBSS/HEPES 5% FCS for 20–30 min at 37 °C. .. For isolation of cells from tumors, tumors were carefully excised from the tumor-free mucosa and transferred into 15 ml U-bottom tubes with small magnetic stirrers (larger tumors were additionally minced with a scalpel).

    Cytometry:

    Article Title: TREM-1 promotes intestinal tumorigenesis
    Article Snippet: After washing of tissue pieces with EDTA-free buffer, lamina propria (LP) cells were obtained by digestion with 100 U/ml Collagenase (Type IV, Sigma) and 50 U/ml DNase (Type I, grade II, Roche) in Ca2+ and Mg2+ -supplemented HBSS/HEPES 5% FCS for 20–30 min at 37 °C. .. Cell suspensions from tumors and tumor-free colons were passed through a 70 μM cell strainer and further characterized by flow cytometry.

    Incubation:

    Article Title: TREM-1 promotes intestinal tumorigenesis
    Article Snippet: Epithelial cells were removed by incubation of tissue pieces in HBSS/HEPES containing 5% FCS, 2 mM EDTA for 2 × 15 min at 37 °C under magnetic stirring. .. After washing of tissue pieces with EDTA-free buffer, lamina propria (LP) cells were obtained by digestion with 100 U/ml Collagenase (Type IV, Sigma) and 50 U/ml DNase (Type I, grade II, Roche) in Ca2+ and Mg2+ -supplemented HBSS/HEPES 5% FCS for 20–30 min at 37 °C.

    Flow Cytometry:

    Article Title: TREM-1 promotes intestinal tumorigenesis
    Article Snippet: After washing of tissue pieces with EDTA-free buffer, lamina propria (LP) cells were obtained by digestion with 100 U/ml Collagenase (Type IV, Sigma) and 50 U/ml DNase (Type I, grade II, Roche) in Ca2+ and Mg2+ -supplemented HBSS/HEPES 5% FCS for 20–30 min at 37 °C. .. Cell suspensions from tumors and tumor-free colons were passed through a 70 μM cell strainer and further characterized by flow cytometry.

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    Millipore v ethylenediaminetetraacetic acid free
    V Ethylenediaminetetraacetic Acid Free, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Millipore ccp1 buffer
    Substrate specificity profile derived from putative <t>CCP1</t> substrates. ) was used to show the enriched residues present at the different identified CCP1 putative substrate positions as compared with the reference set ( i.e. C termini of human proteins in the Swiss-Prot database). For the iceLogo preparation we took into consideration that MCPs sequentially release amino acids. As a result, when a few amino acids are released to get to the final identified product, intermediate products of digestion act as new substrate and are further digested by CCP1. Consequently, intermediate products of digestion were considered as different individual substrates when preparing the iceLogo and, as a result, 35 CCP1 substrates were considered. Only those substrates identified by proteomics were considered here. In the representation the substrate residues are depicted according to Schechter Berger nomenclature. The frequency of the amino acid occurrence at each position in the sequence set was compared with the occurrence in the reference set. Only statistically significant residues with a p value ≤ 0.05 are plotted. Amino acids height shows the degree of difference in the positional amino acid frequencies in the experimental set as compared with the reference set. Residues that are statistically over- or underrepresented in the experimental set are shown in the upper or lower part of the iceLogo respectively.
    Ccp1 Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 87/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore buffer
    Substrate specificity profile derived from putative <t>CCP1</t> substrates. ) was used to show the enriched residues present at the different identified CCP1 putative substrate positions as compared with the reference set ( i.e. C termini of human proteins in the Swiss-Prot database). For the iceLogo preparation we took into consideration that MCPs sequentially release amino acids. As a result, when a few amino acids are released to get to the final identified product, intermediate products of digestion act as new substrate and are further digested by CCP1. Consequently, intermediate products of digestion were considered as different individual substrates when preparing the iceLogo and, as a result, 35 CCP1 substrates were considered. Only those substrates identified by proteomics were considered here. In the representation the substrate residues are depicted according to Schechter Berger nomenclature. The frequency of the amino acid occurrence at each position in the sequence set was compared with the occurrence in the reference set. Only statistically significant residues with a p value ≤ 0.05 are plotted. Amino acids height shows the degree of difference in the positional amino acid frequencies in the experimental set as compared with the reference set. Residues that are statistically over- or underrepresented in the experimental set are shown in the upper or lower part of the iceLogo respectively.
    Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 256 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 256 article reviews
    Price from $9.99 to $1999.99
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    Substrate specificity profile derived from putative CCP1 substrates. ) was used to show the enriched residues present at the different identified CCP1 putative substrate positions as compared with the reference set ( i.e. C termini of human proteins in the Swiss-Prot database). For the iceLogo preparation we took into consideration that MCPs sequentially release amino acids. As a result, when a few amino acids are released to get to the final identified product, intermediate products of digestion act as new substrate and are further digested by CCP1. Consequently, intermediate products of digestion were considered as different individual substrates when preparing the iceLogo and, as a result, 35 CCP1 substrates were considered. Only those substrates identified by proteomics were considered here. In the representation the substrate residues are depicted according to Schechter Berger nomenclature. The frequency of the amino acid occurrence at each position in the sequence set was compared with the occurrence in the reference set. Only statistically significant residues with a p value ≤ 0.05 are plotted. Amino acids height shows the degree of difference in the positional amino acid frequencies in the experimental set as compared with the reference set. Residues that are statistically over- or underrepresented in the experimental set are shown in the upper or lower part of the iceLogo respectively.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: C-terminomics Screen for Natural Substrates of Cytosolic Carboxypeptidase 1 Reveals Processing of Acidic Protein C termini *

    doi: 10.1074/mcp.M114.040360

    Figure Lengend Snippet: Substrate specificity profile derived from putative CCP1 substrates. ) was used to show the enriched residues present at the different identified CCP1 putative substrate positions as compared with the reference set ( i.e. C termini of human proteins in the Swiss-Prot database). For the iceLogo preparation we took into consideration that MCPs sequentially release amino acids. As a result, when a few amino acids are released to get to the final identified product, intermediate products of digestion act as new substrate and are further digested by CCP1. Consequently, intermediate products of digestion were considered as different individual substrates when preparing the iceLogo and, as a result, 35 CCP1 substrates were considered. Only those substrates identified by proteomics were considered here. In the representation the substrate residues are depicted according to Schechter Berger nomenclature. The frequency of the amino acid occurrence at each position in the sequence set was compared with the occurrence in the reference set. Only statistically significant residues with a p value ≤ 0.05 are plotted. Amino acids height shows the degree of difference in the positional amino acid frequencies in the experimental set as compared with the reference set. Residues that are statistically over- or underrepresented in the experimental set are shown in the upper or lower part of the iceLogo respectively.

    Article Snippet: Affinity purified CCP1 was incubated at 5 ng/μl for 2 h or 16 h at 37 °C with affinity purified TRAD1 or HMGB3 at 25 ng/μl in CCP1 buffer (80 m m PIPES, pH 6.8, 1 m m MgCl2 , complemented with EDTA-free protease inhibitor mixture Set III (EMD Millipore)).

    Techniques: Derivative Assay, Activated Clotting Time Assay, Sequencing

    CCP1 overexpression increases the levels of Δ2-tubulin. A ). B , Detection of tubulin PTMs. Extracts from control cells or CCP1 expressing cells were analyzed by Western blot using anti-Δ2-tubulin and anti-Tyr-tubulin antibodies. The Western blot probing anti-β-actin served as loading control.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: C-terminomics Screen for Natural Substrates of Cytosolic Carboxypeptidase 1 Reveals Processing of Acidic Protein C termini *

    doi: 10.1074/mcp.M114.040360

    Figure Lengend Snippet: CCP1 overexpression increases the levels of Δ2-tubulin. A ). B , Detection of tubulin PTMs. Extracts from control cells or CCP1 expressing cells were analyzed by Western blot using anti-Δ2-tubulin and anti-Tyr-tubulin antibodies. The Western blot probing anti-β-actin served as loading control.

    Article Snippet: Affinity purified CCP1 was incubated at 5 ng/μl for 2 h or 16 h at 37 °C with affinity purified TRAD1 or HMGB3 at 25 ng/μl in CCP1 buffer (80 m m PIPES, pH 6.8, 1 m m MgCl2 , complemented with EDTA-free protease inhibitor mixture Set III (EMD Millipore)).

    Techniques: Over Expression, Expressing, Western Blot

    HMGB2 and HMGB1 are processed by CCP1. CCP1 is able to cleave the C terminus of A , HMGB1 and B , HMGB2. N-terminally Myc-tagged HMGB1 or HMGB2 were cotransfected with active or inactive CCP1. Equal amounts of each cell extract were analyzed by Western blot using a HA-tag antibody, to show equal expression levels of both CCP1 variants. Western blotting using an anti-Myc antibody shows the appearance of C-terminal processed forms of the HMGB proteins when co-expressed with active CCP1.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: C-terminomics Screen for Natural Substrates of Cytosolic Carboxypeptidase 1 Reveals Processing of Acidic Protein C termini *

    doi: 10.1074/mcp.M114.040360

    Figure Lengend Snippet: HMGB2 and HMGB1 are processed by CCP1. CCP1 is able to cleave the C terminus of A , HMGB1 and B , HMGB2. N-terminally Myc-tagged HMGB1 or HMGB2 were cotransfected with active or inactive CCP1. Equal amounts of each cell extract were analyzed by Western blot using a HA-tag antibody, to show equal expression levels of both CCP1 variants. Western blotting using an anti-Myc antibody shows the appearance of C-terminal processed forms of the HMGB proteins when co-expressed with active CCP1.

    Article Snippet: Affinity purified CCP1 was incubated at 5 ng/μl for 2 h or 16 h at 37 °C with affinity purified TRAD1 or HMGB3 at 25 ng/μl in CCP1 buffer (80 m m PIPES, pH 6.8, 1 m m MgCl2 , complemented with EDTA-free protease inhibitor mixture Set III (EMD Millipore)).

    Techniques: Western Blot, Expressing