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his60 ni superflow resin  (TaKaRa)


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    Structured Review

    TaKaRa his60 ni superflow resin
    Sortase‐mediated site‐specific labeling of anti‐HS scFvs. ( A ) Schematic of site‐specific sortase A–mediated fluorophore conjugation of an anti‐HS scFv. ( B , C ) Conjugation of HS011D with fluorophore GGK‐TAMRA by SDS‐PAGE. The gel was visualized on a FluorChem instrument with white light/Coomassie staining (B) and with a green filter (537/35 nm) (C). Sortagging efficiency was calculated to be >95% (based on near absence of scFv in the <t>His60</t> elute fraction). Degree of labeling was calculated to be >90% (based on absorbance values).
    His60 Ni Superflow Resin, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 229 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ni+superflow+resin/His60+Ni+Superflow+Resin/pmc13170773-182-1-5
    Average 99 stars, based on 229 article reviews
    his60 ni superflow resin - by Bioz Stars, 2026-10
    99/100 stars

    Images

    1) Product Images from "Engineering, Expression, Purification, and Application of Glycosaminoglycan‐Specific Antibodies"

    Article Title: Engineering, Expression, Purification, and Application of Glycosaminoglycan‐Specific Antibodies

    Journal: Current Protocols

    doi: 10.1002/cpz1.70358

    Sortase‐mediated site‐specific labeling of anti‐HS scFvs. ( A ) Schematic of site‐specific sortase A–mediated fluorophore conjugation of an anti‐HS scFv. ( B , C ) Conjugation of HS011D with fluorophore GGK‐TAMRA by SDS‐PAGE. The gel was visualized on a FluorChem instrument with white light/Coomassie staining (B) and with a green filter (537/35 nm) (C). Sortagging efficiency was calculated to be >95% (based on near absence of scFv in the His60 elute fraction). Degree of labeling was calculated to be >90% (based on absorbance values).
    Figure Legend Snippet: Sortase‐mediated site‐specific labeling of anti‐HS scFvs. ( A ) Schematic of site‐specific sortase A–mediated fluorophore conjugation of an anti‐HS scFv. ( B , C ) Conjugation of HS011D with fluorophore GGK‐TAMRA by SDS‐PAGE. The gel was visualized on a FluorChem instrument with white light/Coomassie staining (B) and with a green filter (537/35 nm) (C). Sortagging efficiency was calculated to be >95% (based on near absence of scFv in the His60 elute fraction). Degree of labeling was calculated to be >90% (based on absorbance values).

    Techniques Used: Labeling, Conjugation Assay, SDS Page, Staining

    Related Articles

    Purification:

    Article Title: A Simplified Method for Evaluating Chitin-Binding Activity Applied to YKL-40 (HC-gp39, CHI3L1) and Chitotriosidase.
    Article Snippet: .. The preparation of protein A-CHIT1-V5-His and protein A-YKL-40-V5-His from the E. coli was performed and purified by Ni Superflow Resin (Takara Bio, Shiga, Japan), as described previously [37]. .. The protein fractions were analyzed using standard SDS-polyacrylamide gel electrophoresis (PAGE), followed by Western blot, using an anti-V5-HRP monoclonal antibody (Thermo Fisher Scientific, Waltham, MA, USA) [37].

    Article Title: A Simplified Method for Evaluating Chitin-Binding Activity Applied to YKL-40 (HC-gp39, CHI3L1) and Chitotriosidase
    Article Snippet: .. The preparation of protein A-CHIT1-V5-His and protein A-YKL-40-V5-His from the E. coli was performed and purified by Ni Superflow Resin (Takara Bio, Shiga, Japan), as described previously [ ]. .. The protein fractions were analyzed using standard SDS-polyacrylamide gel electrophoresis (PAGE), followed by Western blot, using an anti-V5-HRP monoclonal antibody (Thermo Fisher Scientific, Waltham, MA, USA) [ ].

    Article Title: Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes.
    Article Snippet: Cell culture expressing EPHA2-CRD or antigen-B was supplemented with 5 mM Kifunensine (MedChemExpress) to inhibit mannosidase I activity. .. EPHA2-FN2, EPHA2-CRD, and antigen-A were purified using His 60 Ni Superflow resin (Takara), while antigen-B was purified with rProteinA Sepharose (GE Healthcare). .. Affinity tags were cleaved by incubation with either thrombin (Merck) or papain (Thermo Scientific).

    Article Title: Idiotopes of antibodies against HIV-1 CD4-induced epitope shared with those against microorganisms.
    Article Snippet: Funding information Japan Agency for Medical Research and Development, Grant/Award Numbers: JP20fk0410025h0002, JP21fk0410025h0003, JP22fk0410054h0001, JP23fk0410054h0002; JSPS KAKENHI, Grant/Award Numbers: 18H0285400, 21H02970 Abstract Induction of antibodies (Abs) against the conformational CD4-induced (CD4i) epitope is frequent in HIV-1 infection.. However, the mechanism of development of anti-CD4i Abs is unclear.. We used anti-idiotypic (aID) monoclonal Abs (mAbs) of anti-CD4i mAbs to isolate anti-CD4i mAbs from infected subjects and track the causative antigens.

    Article Title: Anti-PSMA antibodies and uses thereof
    Article Snippet: .. For the purification of all recombinant PSMA proteins, cells were removed via centrifugation and His-tagged PSMA proteins were purified from the supernatant via immobilized metal affinity chromatography using His 60 Ni Superflow Resin (Clonetech, Cat #635662) followed by Superdex 200 preparative size exclusion chromatography (SEC) (GE Healthcare) and formulated into 1×DPBS, pH 7.2 containing 1 mM CaCl2, 0.5 mM MgCl2, and 0.5 mM ZnCl2. ..

    other:

    Article Title: A recombinant chimeric spider pyriform-aciniform silk with highly tunable mechanical performance
    Article Snippet: The cell lysate was centrifuged at 12000 rcf for 30 min at 4 °C and the resulting pellets were resuspended in denaturing buffer (100 mM NaH 2 PO 4 , 10 mM Tris-base, 8 M urea, pH 8), and the supernatant was passed through a nickel affinity column (Ni SuperFlow Resin, Takara Bio, San Jose, CA).

    Incubation:

    Article Title: Small molecule substrates for the rapid quantification of acyl transfer activity of nylon hydrolase NylC A .
    Article Snippet: The widespread use of polyamides such as nylons has led to the accumulation of nylon waste, which is particularly resistant to decomposition due to the intrinsic stability of the amide bond.. New methods are required for the true recycling of these waste materials by depolymerization.. Enzymes that are capable of hydrolyzing polyamides have been proposed as biocatalysts that may be suitable for this application.

    Size-exclusion Chromatography:

    Article Title: Integrating Segmental Deuteration iCM-SANS with SAXS and MD for Dynamical Analysis of Multi-domain Proteins
    Article Snippet: In the C-side a’ domains, the His x6-smt3 tag was cleaved by treatment with SUMO protease (LifeSensors, USA) at 4°C overnight. .. The cleaved tag was removed from the samples by applying them to His60 Ni Superflow Resin (TaKaRa BIO Inc.), followed by size exclusion chromatography (SEC) on Superdex 200 Increase 10/300GL (GE Healthcare) with 20 mM Tris-HCl buffer (pH 8.0) containing 150 mM NaCl. ..

    Article Title: Anti-PSMA antibodies and uses thereof
    Article Snippet: .. For the purification of all recombinant PSMA proteins, cells were removed via centrifugation and His-tagged PSMA proteins were purified from the supernatant via immobilized metal affinity chromatography using His 60 Ni Superflow Resin (Clonetech, Cat #635662) followed by Superdex 200 preparative size exclusion chromatography (SEC) (GE Healthcare) and formulated into 1×DPBS, pH 7.2 containing 1 mM CaCl2, 0.5 mM MgCl2, and 0.5 mM ZnCl2. ..

    Binding Assay:

    Article Title: Idiotopes of antibodies against HIV-1 CD4-induced epitope shared with those against microorganisms.
    Article Snippet: Funding information Japan Agency for Medical Research and Development, Grant/Award Numbers: JP20fk0410025h0002, JP21fk0410025h0003, JP22fk0410054h0001, JP23fk0410054h0002; JSPS KAKENHI, Grant/Award Numbers: 18H0285400, 21H02970 Abstract Induction of antibodies (Abs) against the conformational CD4-induced (CD4i) epitope is frequent in HIV-1 infection.. However, the mechanism of development of anti-CD4i Abs is unclear.. We used anti-idiotypic (aID) monoclonal Abs (mAbs) of anti-CD4i mAbs to isolate anti-CD4i mAbs from infected subjects and track the causative antigens.

    Expressing:

    Article Title: Idiotopes of antibodies against HIV-1 CD4-induced epitope shared with those against microorganisms.
    Article Snippet: Funding information Japan Agency for Medical Research and Development, Grant/Award Numbers: JP20fk0410025h0002, JP21fk0410025h0003, JP22fk0410054h0001, JP23fk0410054h0002; JSPS KAKENHI, Grant/Award Numbers: 18H0285400, 21H02970 Abstract Induction of antibodies (Abs) against the conformational CD4-induced (CD4i) epitope is frequent in HIV-1 infection.. However, the mechanism of development of anti-CD4i Abs is unclear.. We used anti-idiotypic (aID) monoclonal Abs (mAbs) of anti-CD4i mAbs to isolate anti-CD4i mAbs from infected subjects and track the causative antigens.

    Plasmid Preparation:

    Article Title: Idiotopes of antibodies against HIV-1 CD4-induced epitope shared with those against microorganisms.
    Article Snippet: Funding information Japan Agency for Medical Research and Development, Grant/Award Numbers: JP20fk0410025h0002, JP21fk0410025h0003, JP22fk0410054h0001, JP23fk0410054h0002; JSPS KAKENHI, Grant/Award Numbers: 18H0285400, 21H02970 Abstract Induction of antibodies (Abs) against the conformational CD4-induced (CD4i) epitope is frequent in HIV-1 infection.. However, the mechanism of development of anti-CD4i Abs is unclear.. We used anti-idiotypic (aID) monoclonal Abs (mAbs) of anti-CD4i mAbs to isolate anti-CD4i mAbs from infected subjects and track the causative antigens.

    Recombinant:

    Article Title: Anti-PSMA antibodies and uses thereof
    Article Snippet: .. For the purification of all recombinant PSMA proteins, cells were removed via centrifugation and His-tagged PSMA proteins were purified from the supernatant via immobilized metal affinity chromatography using His 60 Ni Superflow Resin (Clonetech, Cat #635662) followed by Superdex 200 preparative size exclusion chromatography (SEC) (GE Healthcare) and formulated into 1×DPBS, pH 7.2 containing 1 mM CaCl2, 0.5 mM MgCl2, and 0.5 mM ZnCl2. ..

    Centrifugation:

    Article Title: Anti-PSMA antibodies and uses thereof
    Article Snippet: .. For the purification of all recombinant PSMA proteins, cells were removed via centrifugation and His-tagged PSMA proteins were purified from the supernatant via immobilized metal affinity chromatography using His 60 Ni Superflow Resin (Clonetech, Cat #635662) followed by Superdex 200 preparative size exclusion chromatography (SEC) (GE Healthcare) and formulated into 1×DPBS, pH 7.2 containing 1 mM CaCl2, 0.5 mM MgCl2, and 0.5 mM ZnCl2. ..

    Affinity Chromatography:

    Article Title: Anti-PSMA antibodies and uses thereof
    Article Snippet: .. For the purification of all recombinant PSMA proteins, cells were removed via centrifugation and His-tagged PSMA proteins were purified from the supernatant via immobilized metal affinity chromatography using His 60 Ni Superflow Resin (Clonetech, Cat #635662) followed by Superdex 200 preparative size exclusion chromatography (SEC) (GE Healthcare) and formulated into 1×DPBS, pH 7.2 containing 1 mM CaCl2, 0.5 mM MgCl2, and 0.5 mM ZnCl2. ..



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    Sortase‐mediated site‐specific labeling of anti‐HS scFvs. ( A ) Schematic of site‐specific sortase A–mediated fluorophore conjugation of an anti‐HS scFv. ( B , C ) Conjugation of HS011D with fluorophore GGK‐TAMRA by SDS‐PAGE. The gel was visualized on a FluorChem instrument with white light/Coomassie staining (B) and with a green filter (537/35 nm) (C). Sortagging efficiency was calculated to be >95% (based on near absence of scFv in the <t>His60</t> elute fraction). Degree of labeling was calculated to be >90% (based on absorbance values).
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    Sortase‐mediated site‐specific labeling of anti‐HS scFvs. ( A ) Schematic of site‐specific sortase A–mediated fluorophore conjugation of an anti‐HS scFv. ( B , C ) Conjugation of HS011D with fluorophore GGK‐TAMRA by SDS‐PAGE. The gel was visualized on a FluorChem instrument with white light/Coomassie staining (B) and with a green filter (537/35 nm) (C). Sortagging efficiency was calculated to be >95% (based on near absence of scFv in the <t>His60</t> elute fraction). Degree of labeling was calculated to be >90% (based on absorbance values).
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    Image Search Results


    Sortase‐mediated site‐specific labeling of anti‐HS scFvs. ( A ) Schematic of site‐specific sortase A–mediated fluorophore conjugation of an anti‐HS scFv. ( B , C ) Conjugation of HS011D with fluorophore GGK‐TAMRA by SDS‐PAGE. The gel was visualized on a FluorChem instrument with white light/Coomassie staining (B) and with a green filter (537/35 nm) (C). Sortagging efficiency was calculated to be >95% (based on near absence of scFv in the His60 elute fraction). Degree of labeling was calculated to be >90% (based on absorbance values).

    Journal: Current Protocols

    Article Title: Engineering, Expression, Purification, and Application of Glycosaminoglycan‐Specific Antibodies

    doi: 10.1002/cpz1.70358

    Figure Lengend Snippet: Sortase‐mediated site‐specific labeling of anti‐HS scFvs. ( A ) Schematic of site‐specific sortase A–mediated fluorophore conjugation of an anti‐HS scFv. ( B , C ) Conjugation of HS011D with fluorophore GGK‐TAMRA by SDS‐PAGE. The gel was visualized on a FluorChem instrument with white light/Coomassie staining (B) and with a green filter (537/35 nm) (C). Sortagging efficiency was calculated to be >95% (based on near absence of scFv in the His60 elute fraction). Degree of labeling was calculated to be >90% (based on absorbance values).

    Article Snippet: Prepare His60 Ni Superflow resin (Clontech, cat. no. 635662) by removing the storage solution, washing in H 2 O, and resuspending in His60 wash buffer (see recipe) to give a 50% (v/v) slurry.

    Techniques: Labeling, Conjugation Assay, SDS Page, Staining