snap capture magnetic beads  (New England Biolabs)


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    Name:
    SNAP Capture Magnetic Beads
    Description:
    SNAP Capture Magnetic Beads 2ml
    Catalog Number:
    s9145s
    Price:
    224
    Size:
    2 ml
    Category:
    Protein Purification Kit Components
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    Structured Review

    New England Biolabs snap capture magnetic beads
    SNAP Capture Magnetic Beads
    SNAP Capture Magnetic Beads 2ml
    https://www.bioz.com/result/snap capture magnetic beads/product/New England Biolabs
    Average 95 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    snap capture magnetic beads - by Bioz Stars, 2020-02
    95/100 stars

    Images

    1) Product Images from "Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine"

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.188581

    Expression of recombinant SNAP-fusion galectins. A , constructs for producing SNAP-LEC fusions and their uses in in situ detection of carbohydrates and in pull down of specific glycoproteins. B , expression and purification of SNAP-LEC-6. Lane 1 , molecular weight marker; lane 2 , lysate from E. coli induced for recombinant protein expression; lane 3 , lysate from noninduced cells; lanes 4–7 , consecutive fractions eluted from nickel resin. C , purified recombinant SNAP-LEC-6 labeled with infrared dye.
    Figure Legend Snippet: Expression of recombinant SNAP-fusion galectins. A , constructs for producing SNAP-LEC fusions and their uses in in situ detection of carbohydrates and in pull down of specific glycoproteins. B , expression and purification of SNAP-LEC-6. Lane 1 , molecular weight marker; lane 2 , lysate from E. coli induced for recombinant protein expression; lane 3 , lysate from noninduced cells; lanes 4–7 , consecutive fractions eluted from nickel resin. C , purified recombinant SNAP-LEC-6 labeled with infrared dye.

    Techniques Used: Expressing, Recombinant, Construct, In Situ, Purification, Molecular Weight, Marker, Labeling

    Labeled recombinant SNAP-LECs recognize target molecules located in diverse C. elegans tissues. A , LEC-1. Staining is found in the rectal region ( arrowheads ). B , LEC-6. Staining is most prominent along the intestinal lumen ( arrow ), the grinder of the pharynx ( star ), and the coelomocytes ( arrowhead ). C , LEC-9. Staining is more concentrated along the intestinal lumen ( arrow ) and shows significant but diffuse signal in most tissues. D , LEC-10. Staining is primarily along the lumen in the intestine ( arrow ). E , LEC-11. Staining is localized in the grinder ( arrowhead ) and the buccal cavity of the pharynx ( arrow ), and a diffuse signal is also present in most cells. F , CGL2. Staining is very similar to LEC-9 with concentrated signal localizing along the intestinal lumen with a diffuse signal in most tissues. G , diagram of tissues showing staining with recombinant galectins.
    Figure Legend Snippet: Labeled recombinant SNAP-LECs recognize target molecules located in diverse C. elegans tissues. A , LEC-1. Staining is found in the rectal region ( arrowheads ). B , LEC-6. Staining is most prominent along the intestinal lumen ( arrow ), the grinder of the pharynx ( star ), and the coelomocytes ( arrowhead ). C , LEC-9. Staining is more concentrated along the intestinal lumen ( arrow ) and shows significant but diffuse signal in most tissues. D , LEC-10. Staining is primarily along the lumen in the intestine ( arrow ). E , LEC-11. Staining is localized in the grinder ( arrowhead ) and the buccal cavity of the pharynx ( arrow ), and a diffuse signal is also present in most cells. F , CGL2. Staining is very similar to LEC-9 with concentrated signal localizing along the intestinal lumen with a diffuse signal in most tissues. G , diagram of tissues showing staining with recombinant galectins.

    Techniques Used: Labeling, Recombinant, Staining

    Related Articles

    Centrifugation:

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
    Article Snippet: Pull-down Experiments with SNAP-galectin Fusions 100 μl of SNAP-capture magnetic beads (NEB S9145) (with a coupling capacity of 0.5 mg/ml for SNAP protein) were washed twice in immobilization buffer (50 mm Tris-Cl, pH 7.5, 100 mm NaCl, 1 mm DTT, and 0.1% Tween 20). .. C. elegans total protein lysates were prepared by homogenizing mixed stage worms in RIPA buffer followed by centrifugation to remove insoluble materials.

    Construct:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. The successful pull-down of SH3Hck was assessed by antibody labeling of the N-terminal CLIP tag of the construct.

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: The cell lysate was diluted in the immobilization buffer (50 mM Tris–HCl, 100 mM NaCl, 1 mM DTT, 0.1% Tween, pH = 7.5), tested for protein expression by anti-SNAP western-blot analysis , then incubated with SNAP capture magnetic beads (New England Biolabs™) for one hour at room temperature. .. The SNAP-ELMO1–727 constructs retained by beads due to a covalent binding were eluted after protease (TEV) cleavage of the SNAP tag overnight at 4 °C.

    Microarray:

    Article Title: Unraveling the Role of KIAA1199, a Novel Endoplasmic Reticulum Protein, in Cancer Cell Migration
    Article Snippet: SNAP-capture beads and rabbit anti-SNAP polyclonal antibody were purchased from New England Biolabs (Ipswich, MA). .. The human breast cancer tissue microarray samples (BR804, BC08013a, and BR10010a) were purchased from US Biomax Inc (Rockville, MD).

    Incubation:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. The cell lysate was diluted in the immobilization buffer (50 mM Tris–HCl, 100 mM NaCl, 1 mM DTT, 0.1% Tween, pH = 7.5), tested for protein expression by anti-SNAP western-blot analysis , then incubated with SNAP capture magnetic beads (New England Biolabs™) for one hour at room temperature. .. The SNAP-ELMO1–727 constructs retained by beads due to a covalent binding were eluted after protease (TEV) cleavage of the SNAP tag overnight at 4 °C.

    Article Title: The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length
    Article Snippet: SNAP magnetic beads (Cat. No. S9145S; New England Biolabs) were prepared as follows: for each strain, 40 μl of the SNAP magnetic beads were spun down at room temperature using a bench-top minicentrifuge at top speed (14,000 × g ) for 1 min. .. The clarified supernatant was removed and the beads were incubated overnight in an end-over-end rocker at 4°C in a buffer containing 3% BSA, 10 mM HEPES, 5 mM MgSO4 , 1 mM DTT, 25 mM NaCl, and protease inhibitors at pH 7.4.

    Article Title: Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space
    Article Snippet: .. Cleared cell lysates were incubated for different time with 100 μl Snap capture beads (NEB) to pull down MreB interacting proteins. .. The specific interaction between MreB and EF-Tu was then verified by western blotting using an EF-Tu antibody (Hucult Biotech).

    Article Title: The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length
    Article Snippet: SNAP magnetic beads (Cat. No. S9145S; New England Biolabs) were prepared as follows: for each strain, 40 μl of the SNAP magnetic beads were spun down at room temperature using a bench-top minicentrifuge at top speed (14,000 × g ) for 1 min. .. The clarified supernatant was removed and the beads were incubated overnight in an end-over-end rocker at 4°C in a buffer containing 3% BSA, 10 mM HEPES, 5 mM MgSO4 , 1 mM DTT, 25 mM NaCl, and protease inhibitors at pH 7.4.

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
    Article Snippet: Pull-down Experiments with SNAP-galectin Fusions 100 μl of SNAP-capture magnetic beads (NEB S9145) (with a coupling capacity of 0.5 mg/ml for SNAP protein) were washed twice in immobilization buffer (50 mm Tris-Cl, pH 7.5, 100 mm NaCl, 1 mm DTT, and 0.1% Tween 20). .. The equilibrated beads were then added to 200 μl of immobilization buffer containing 200 μg of active SNAP-tagged galectin supplemented with an additional 1 mm of DTT and incubated for an hour at room temperature with rotation.

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
    Article Snippet: The SNAP-capture magnetic beads with the immobilized SNAP-tagged lectin were then incubated with C. elegans lysates containing ∼250 μg of protein for 3 h rotating at room temperature either with or without 50 mm lactose. .. While washing, the SNAP-Capture Magnetic Beads were separated from solution using a magnetic separation rack (NEB, S1506S).

    Article Title: Lis1 has two opposing modes of regulating cytoplasmic dynein
    Article Snippet: .. Sixteen µL of magnetic SNAP-Capture beads (NEB) were incubated with increasing concentrations of SNAP-Lis1 (0–600 nM) in modified TEV buffer for 1 hour at room temperature with agitation. .. The supernatant was removed, the beads were washed with 1 ml of modified TEV buffer followed by 1 ml of TEV buffer supplemented with 1 mM DTT, 0.1% NP40, 2 mM MgCl2 , 1 mM ATP, and 1 mM NaVO4 .

    Expressing:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. The successful pull-down of SH3Hck was assessed by antibody labeling of the N-terminal CLIP tag of the construct.

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. The cell lysate was diluted in the immobilization buffer (50 mM Tris–HCl, 100 mM NaCl, 1 mM DTT, 0.1% Tween, pH = 7.5), tested for protein expression by anti-SNAP western-blot analysis , then incubated with SNAP capture magnetic beads (New England Biolabs™) for one hour at room temperature. .. The SNAP-ELMO1–727 constructs retained by beads due to a covalent binding were eluted after protease (TEV) cleavage of the SNAP tag overnight at 4 °C.

    Modification:

    Article Title: The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length
    Article Snippet: For affinity purification, we used a modified protocol from Zlatic et al. ( ). .. SNAP magnetic beads (Cat. No. S9145S; New England Biolabs) were prepared as follows: for each strain, 40 μl of the SNAP magnetic beads were spun down at room temperature using a bench-top minicentrifuge at top speed (14,000 × g ) for 1 min.

    Article Title: The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length
    Article Snippet: For affinity purification, we used a modified protocol from Zlatic et al. ( ). .. SNAP magnetic beads (Cat. No. S9145S; New England Biolabs) were prepared as follows: for each strain, 40 μl of the SNAP magnetic beads were spun down at room temperature using a bench-top minicentrifuge at top speed (14,000 × g ) for 1 min.

    Article Title: Lis1 has two opposing modes of regulating cytoplasmic dynein
    Article Snippet: .. Sixteen µL of magnetic SNAP-Capture beads (NEB) were incubated with increasing concentrations of SNAP-Lis1 (0–600 nM) in modified TEV buffer for 1 hour at room temperature with agitation. .. The supernatant was removed, the beads were washed with 1 ml of modified TEV buffer followed by 1 ml of TEV buffer supplemented with 1 mM DTT, 0.1% NP40, 2 mM MgCl2 , 1 mM ATP, and 1 mM NaVO4 .

    Western Blot:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. The successful pull-down of SH3Hck was assessed by antibody labeling of the N-terminal CLIP tag of the construct.

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. The cell lysate was diluted in the immobilization buffer (50 mM Tris–HCl, 100 mM NaCl, 1 mM DTT, 0.1% Tween, pH = 7.5), tested for protein expression by anti-SNAP western-blot analysis , then incubated with SNAP capture magnetic beads (New England Biolabs™) for one hour at room temperature. .. The SNAP-ELMO1–727 constructs retained by beads due to a covalent binding were eluted after protease (TEV) cleavage of the SNAP tag overnight at 4 °C.

    Article Title: Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space
    Article Snippet: Cleared cell lysates were incubated for different time with 100 μl Snap capture beads (NEB) to pull down MreB interacting proteins. .. The specific interaction between MreB and EF-Tu was then verified by western blotting using an EF-Tu antibody (Hucult Biotech).

    Transfection:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. The successful pull-down of SH3Hck was assessed by antibody labeling of the N-terminal CLIP tag of the construct.

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: 2.5 Pull Down of CLIP-SH3Hck by ELMO1 from cellular extracts HEK293T cells were transiently transfected with SNAP-ELMO1 domains and CLIP-SH3Hck or with only CLIP-SH3Hck for the control well. .. The cell lysate was diluted in the immobilization buffer (50 mM Tris–HCl, 100 mM NaCl, 1 mM DTT, 0.1% Tween, pH = 7.5), tested for protein expression by anti-SNAP western-blot analysis , then incubated with SNAP capture magnetic beads (New England Biolabs™) for one hour at room temperature.

    Förster Resonance Energy Transfer:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: Paragraph title: In cellulo pull-down and Förster resonance energy transfer (FRET) analysis of ELMO1 and SH3Hck interactions ... Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf.

    Generated:

    Article Title: Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space
    Article Snippet: Verification of MreB and EF-Tu interaction in E. coli Snap-tagged MreB strain was generated by lambda red recombination. .. Cleared cell lysates were incubated for different time with 100 μl Snap capture beads (NEB) to pull down MreB interacting proteins.

    Affinity Purification:

    Article Title: The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length
    Article Snippet: Paragraph title: SNAP affinity purification ... SNAP magnetic beads (Cat. No. S9145S; New England Biolabs) were prepared as follows: for each strain, 40 μl of the SNAP magnetic beads were spun down at room temperature using a bench-top minicentrifuge at top speed (14,000 × g ) for 1 min.

    Binding Assay:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. The successful pull-down of SH3Hck was assessed by antibody labeling of the N-terminal CLIP tag of the construct.

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: The cell lysate was diluted in the immobilization buffer (50 mM Tris–HCl, 100 mM NaCl, 1 mM DTT, 0.1% Tween, pH = 7.5), tested for protein expression by anti-SNAP western-blot analysis , then incubated with SNAP capture magnetic beads (New England Biolabs™) for one hour at room temperature. .. The SNAP-ELMO1–727 constructs retained by beads due to a covalent binding were eluted after protease (TEV) cleavage of the SNAP tag overnight at 4 °C.

    Article Title: Lis1 has two opposing modes of regulating cytoplasmic dynein
    Article Snippet: Paragraph title: Lis1 affinity capture to determine Lis1-dynein binding affinities ... Sixteen µL of magnetic SNAP-Capture beads (NEB) were incubated with increasing concentrations of SNAP-Lis1 (0–600 nM) in modified TEV buffer for 1 hour at room temperature with agitation.

    Magnetic Beads:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. The successful pull-down of SH3Hck was assessed by antibody labeling of the N-terminal CLIP tag of the construct.

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: .. The cell lysate was diluted in the immobilization buffer (50 mM Tris–HCl, 100 mM NaCl, 1 mM DTT, 0.1% Tween, pH = 7.5), tested for protein expression by anti-SNAP western-blot analysis , then incubated with SNAP capture magnetic beads (New England Biolabs™) for one hour at room temperature. .. The SNAP-ELMO1–727 constructs retained by beads due to a covalent binding were eluted after protease (TEV) cleavage of the SNAP tag overnight at 4 °C.

    Article Title: A Structured Workflow for Mapping Human Sin3 Histone Deacetylase Complex Interactions Using Halo-MudPIT Affinity-Purification Mass Spectrometry
    Article Snippet: .. SNAP-Capture magnetic beads (S9145S) were from NEB (Ipswich, MA). .. Salt Active Nuclease (SAN) was from ArcticZymes (Tromso, Norway).

    Article Title: Dynein Engages and Disassembles Cytosol-Localized Simian Virus 40 To Promote Infection
    Article Snippet: .. Nocodazole, Triton X-100, dithiothreitol (DTT), and phenylmethanesulfonyl fluoride (PMSF) were purchased from Sigma; SNAP capture magnetic beads, from New England BioLabs (Ipswich, MA); protein G-conjugated magnetic beads and dithiobis(succinimidyl propionate) (DSP), from Thermo Fisher (Rockford, IL); ciliobrevin D and digitonin, from EMD Millipore (San Diego, CA). .. SV40 was purified as described previously ( ).

    Article Title: The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length
    Article Snippet: .. SNAP magnetic beads (Cat. No. S9145S; New England Biolabs) were prepared as follows: for each strain, 40 μl of the SNAP magnetic beads were spun down at room temperature using a bench-top minicentrifuge at top speed (14,000 × g ) for 1 min. .. The clarified supernatant was removed and the beads were incubated overnight in an end-over-end rocker at 4°C in a buffer containing 3% BSA, 10 mM HEPES, 5 mM MgSO4 , 1 mM DTT, 25 mM NaCl, and protease inhibitors at pH 7.4.

    Article Title: A ligand-based system for receptor-specific delivery of proteins
    Article Snippet: .. SNAP-capture magnetic beads (NEB #S9145S) were used to remove excess of free-ligand when this was present at the end of the process. .. In-vitro primary keratinocyte treatment with CLIP-Cre S-CROSS Cross-linked complexes or CLIP-Cre alone were diluted in-vitro in keratinocytes serum free media to the desired concentration (2 μM) in a final volume of 100 μl.

    Article Title: The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length
    Article Snippet: .. SNAP magnetic beads (Cat. No. S9145S; New England Biolabs) were prepared as follows: for each strain, 40 μl of the SNAP magnetic beads were spun down at room temperature using a bench-top minicentrifuge at top speed (14,000 × g ) for 1 min. .. The clarified supernatant was removed and the beads were incubated overnight in an end-over-end rocker at 4°C in a buffer containing 3% BSA, 10 mM HEPES, 5 mM MgSO4 , 1 mM DTT, 25 mM NaCl, and protease inhibitors at pH 7.4.

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
    Article Snippet: .. Pull-down Experiments with SNAP-galectin Fusions 100 μl of SNAP-capture magnetic beads (NEB S9145) (with a coupling capacity of 0.5 mg/ml for SNAP protein) were washed twice in immobilization buffer (50 mm Tris-Cl, pH 7.5, 100 mm NaCl, 1 mm DTT, and 0.1% Tween 20). .. The equilibrated beads were then added to 200 μl of immobilization buffer containing 200 μg of active SNAP-tagged galectin supplemented with an additional 1 mm of DTT and incubated for an hour at room temperature with rotation.

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
    Article Snippet: .. While washing, the SNAP-Capture Magnetic Beads were separated from solution using a magnetic separation rack (NEB, S1506S). .. Proteins captured with the magnetic beads were eluted by boiling with 20 μl of SDS-loading buffer and separated by SDS-PAGE.

    Mutagenesis:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. As expected, when CLIP-SH3Hck is co-expressed with the ELMO1 C-terminal domain lacking its polyproline motif (ELMO532–707 ), only a residual signal similar to the one observed in the negative control (cells transfected with CLIP-SH3Hck alone) is apparent, despite the correct expression of CLIP-SH3Hck and ELMO532–707 deletion mutant ( ).

    Antibody Labeling:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. The successful pull-down of SH3Hck was assessed by antibody labeling of the N-terminal CLIP tag of the construct.

    Labeling:

    Article Title: A Structured Workflow for Mapping Human Sin3 Histone Deacetylase Complex Interactions Using Halo-MudPIT Affinity-Purification Mass Spectrometry
    Article Snippet: IRDye® 800CW labeled goat anti-Rabbit (926–3211) and IRDye® 680LT labeled goat anti-Mouse (926–68020) secondary antibodies were from LI-COR Biosciences (Lincoln, NE). .. SNAP-Capture magnetic beads (S9145S) were from NEB (Ipswich, MA).

    Cotransfection:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: 3.2 In cellulo pull-down and Förster resonance energy transfer (FRET) analysis of ELMO1 and SH3Hck interactions We next examined if this interaction could occur in the cell context after co-transfection of HEK293T cells. .. Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf.

    SDS Page:

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
    Article Snippet: While washing, the SNAP-Capture Magnetic Beads were separated from solution using a magnetic separation rack (NEB, S1506S). .. Proteins captured with the magnetic beads were eluted by boiling with 20 μl of SDS-loading buffer and separated by SDS-PAGE.

    Plasmid Preparation:

    Article Title: Unraveling the Role of KIAA1199, a Novel Endoplasmic Reticulum Protein, in Cancer Cell Migration
    Article Snippet: SNAP-capture beads and rabbit anti-SNAP polyclonal antibody were purchased from New England Biolabs (Ipswich, MA). .. PKCγK380R cDNA (Addgene plasmid 21239) and PKCβI cDNA (Addgene plasmid 16378) ( ) were purchased from Addgene (Cambridge, MA).

    Negative Control:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf. .. As expected, when CLIP-SH3Hck is co-expressed with the ELMO1 C-terminal domain lacking its polyproline motif (ELMO532–707 ), only a residual signal similar to the one observed in the negative control (cells transfected with CLIP-SH3Hck alone) is apparent, despite the correct expression of CLIP-SH3Hck and ELMO532–707 deletion mutant ( ).

    Recombinant:

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
    Article Snippet: While washing, the SNAP-Capture Magnetic Beads were separated from solution using a magnetic separation rack (NEB, S1506S). .. The same size regions from controls that did not add any recombinant galectin or from samples that had been co-incubated with lactose were also excised.

    Concentration Assay:

    Article Title: A ligand-based system for receptor-specific delivery of proteins
    Article Snippet: Concentration of CLIP protein bound to the cross-linker was assessed using a NANODROP ND-8000 or by quantitative densitometry analysis of SDS-PAGE with ImageJ. .. SNAP-capture magnetic beads (NEB #S9145S) were used to remove excess of free-ligand when this was present at the end of the process.

    Staining:

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine
    Article Snippet: While washing, the SNAP-Capture Magnetic Beads were separated from solution using a magnetic separation rack (NEB, S1506S). .. After staining with Coomassie Blue dye, bands that were only present in the wild type lysate were excised for protein identification.

    Article Title: Lis1 has two opposing modes of regulating cytoplasmic dynein
    Article Snippet: Sixteen µL of magnetic SNAP-Capture beads (NEB) were incubated with increasing concentrations of SNAP-Lis1 (0–600 nM) in modified TEV buffer for 1 hour at room temperature with agitation. .. The supernatant was removed, ran on a 4–12% Bis Tris gel, and stained with Sypro Red (Thermo Fisher) to visualize the fraction of dynein depleted.

    Cross-linking Immunoprecipitation:

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: To efficiently pull-down the SH3 domain of Hck, we expressed SNAP-tag and CLIP-tag N-terminal fusion constructs of ELMO1 and SH3Hck , respectively. .. Lysates of HEK293T cells transiently transfected for the co-expression of the SH3 domain of Hck in the presence of wild type ELMO1–727 or the N-terminal deletion mutants ELMO532–727 and ELMO532–707 , were checked for correct protein expression by western-blot ( ) and subjected to pull-down experiments using ELMO1 as a bait, taking advantage of the specific and covalent binding of SNAP fusion constructs to the SNAP-capture magnetic beads (New England Biolabs, cf.

    Article Title: The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif
    Article Snippet: Paragraph title: Pull Down of CLIP-SH3Hck by ELMO1 from cellular extracts ... The cell lysate was diluted in the immobilization buffer (50 mM Tris–HCl, 100 mM NaCl, 1 mM DTT, 0.1% Tween, pH = 7.5), tested for protein expression by anti-SNAP western-blot analysis , then incubated with SNAP capture magnetic beads (New England Biolabs™) for one hour at room temperature.

    Article Title: A ligand-based system for receptor-specific delivery of proteins
    Article Snippet: The complex was then reacted with SNAP-ligands (IL-31K138A SNAP, NGFR121W SNAP or SNAP) overnight at room temperature in agitation at a 1:0.8 ratio (CLIP-protein-linker:SNAP-ligand) to minimize the presence of free ligand. .. SNAP-capture magnetic beads (NEB #S9145S) were used to remove excess of free-ligand when this was present at the end of the process.

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    New England Biolabs snap capture magnetic beads
    Expression of recombinant <t>SNAP-fusion</t> galectins. A , constructs for producing SNAP-LEC fusions and their uses in in situ detection of carbohydrates and in pull down of specific glycoproteins. B , expression and purification of SNAP-LEC-6. Lane 1 , molecular weight marker; lane 2 , lysate from E. coli induced for recombinant protein expression; lane 3 , lysate from noninduced cells; lanes 4–7 , consecutive fractions eluted from nickel resin. C , purified recombinant SNAP-LEC-6 labeled with infrared dye.
    Snap Capture Magnetic Beads, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Expression of recombinant SNAP-fusion galectins. A , constructs for producing SNAP-LEC fusions and their uses in in situ detection of carbohydrates and in pull down of specific glycoproteins. B , expression and purification of SNAP-LEC-6. Lane 1 , molecular weight marker; lane 2 , lysate from E. coli induced for recombinant protein expression; lane 3 , lysate from noninduced cells; lanes 4–7 , consecutive fractions eluted from nickel resin. C , purified recombinant SNAP-LEC-6 labeled with infrared dye.

    Journal: The Journal of Biological Chemistry

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine

    doi: 10.1074/jbc.M110.188581

    Figure Lengend Snippet: Expression of recombinant SNAP-fusion galectins. A , constructs for producing SNAP-LEC fusions and their uses in in situ detection of carbohydrates and in pull down of specific glycoproteins. B , expression and purification of SNAP-LEC-6. Lane 1 , molecular weight marker; lane 2 , lysate from E. coli induced for recombinant protein expression; lane 3 , lysate from noninduced cells; lanes 4–7 , consecutive fractions eluted from nickel resin. C , purified recombinant SNAP-LEC-6 labeled with infrared dye.

    Article Snippet: Pull-down Experiments with SNAP-galectin Fusions 100 μl of SNAP-capture magnetic beads (NEB S9145) (with a coupling capacity of 0.5 mg/ml for SNAP protein) were washed twice in immobilization buffer (50 mm Tris-Cl, pH 7.5, 100 mm NaCl, 1 mm DTT, and 0.1% Tween 20).

    Techniques: Expressing, Recombinant, Construct, In Situ, Purification, Molecular Weight, Marker, Labeling

    Labeled recombinant SNAP-LECs recognize target molecules located in diverse C. elegans tissues. A , LEC-1. Staining is found in the rectal region ( arrowheads ). B , LEC-6. Staining is most prominent along the intestinal lumen ( arrow ), the grinder of the pharynx ( star ), and the coelomocytes ( arrowhead ). C , LEC-9. Staining is more concentrated along the intestinal lumen ( arrow ) and shows significant but diffuse signal in most tissues. D , LEC-10. Staining is primarily along the lumen in the intestine ( arrow ). E , LEC-11. Staining is localized in the grinder ( arrowhead ) and the buccal cavity of the pharynx ( arrow ), and a diffuse signal is also present in most cells. F , CGL2. Staining is very similar to LEC-9 with concentrated signal localizing along the intestinal lumen with a diffuse signal in most tissues. G , diagram of tissues showing staining with recombinant galectins.

    Journal: The Journal of Biological Chemistry

    Article Title: Caenorhabditis elegans Galectins LEC-6 and LEC-10 Interact with Similar Glycoconjugates in the Intestine

    doi: 10.1074/jbc.M110.188581

    Figure Lengend Snippet: Labeled recombinant SNAP-LECs recognize target molecules located in diverse C. elegans tissues. A , LEC-1. Staining is found in the rectal region ( arrowheads ). B , LEC-6. Staining is most prominent along the intestinal lumen ( arrow ), the grinder of the pharynx ( star ), and the coelomocytes ( arrowhead ). C , LEC-9. Staining is more concentrated along the intestinal lumen ( arrow ) and shows significant but diffuse signal in most tissues. D , LEC-10. Staining is primarily along the lumen in the intestine ( arrow ). E , LEC-11. Staining is localized in the grinder ( arrowhead ) and the buccal cavity of the pharynx ( arrow ), and a diffuse signal is also present in most cells. F , CGL2. Staining is very similar to LEC-9 with concentrated signal localizing along the intestinal lumen with a diffuse signal in most tissues. G , diagram of tissues showing staining with recombinant galectins.

    Article Snippet: Pull-down Experiments with SNAP-galectin Fusions 100 μl of SNAP-capture magnetic beads (NEB S9145) (with a coupling capacity of 0.5 mg/ml for SNAP protein) were washed twice in immobilization buffer (50 mm Tris-Cl, pH 7.5, 100 mm NaCl, 1 mm DTT, and 0.1% Tween 20).

    Techniques: Labeling, Recombinant, Staining