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P6611

Millipore

HIS-Select® Nickel Affinity Gel

HIS-Select® Nickel Affinity Gel
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(1:1 suspension in a 20% ethanol solution)

Sinonimo/i:

Ni-NTA resin, nickel charged agarose

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5 ML
146,00 €
25 ML
473,00 €
100 ML
1.460,00 €
500 ML
6.570,00 €

146,00 €


Per informazioni sulla disponibilità, contatta il Servizio Clienti.


Scegli un formato

Cambia visualizzazione
5 ML
146,00 €
25 ML
473,00 €
100 ML
1.460,00 €
500 ML
6.570,00 €

About This Item

Codice UNSPSC:
12352200
NACRES:
NA.56

146,00 €


Per informazioni sulla disponibilità, contatta il Servizio Clienti.

Coniugato

magnetic beads

Livello qualitativo

Stato

(1:1 suspension in a 20% ethanol solution)

Caratteristiche

hydrophilic

Confezionamento

pkg of 1 mL
pkg of 100 mL
pkg of 25 mL
pkg of 5 mL
pkg of 500 mL

Concentrazione

1.5-2.4 mL/mL (suspension in packed gel)

tecniche

protein purification: suitable

Colore

faint blue to very dark blue

Matrice

6% Beaded Agarose

Capacità

>15 mg/mL, gel binding capacity (protein)(with an approx. 30 kDa protein)

Temp. transizione

flash point 32 °C (closed cup)

Temperatura di conservazione

2-8°C

Descrizione generale

HIS-Select® Nickel Affinity Gel is an immobilized metal ion affinity chromatography (IMAC) product, used for the purification of His-tagged proteins. While the unique, non-charged, hydrophilic linkage of the proprietary quadridentate NTA chelate group to the beaded agarose charged with nickel ensures high selectivity for small to medium scale His-tag protein purification, it also results in reduced non-specific binding of other proteins. HIS-Select Nickel Affinity Gel is selective for recombinant proteins with His-tags and exhibits low non-specific binding of other proteins. The selectivity can be modulated with the inclusion of imidazole during chromatography.
HIS-Select® Nickel Affinity Gel is durable and can capture the recombinant proteins with histidine tags at a high flow rate. Recombinant proteins with histidine tags are bound using either native or denaturing conditions.

Applicazioni

HIS-Select® Nickel Affinity Gel has been used in the purification of recombinant proteins like EF-hand calcium-binding protein (S100A14),[1] LIM homeobox transcription factor 1 alpha protein,[2] sigma-1 receptor[3] as well as harpin,[4] stable protein 1 (SP1),[5][6] and BCR-ABL fusion protein.[7]

Caratteristiche e vantaggi

  • High selectivity for higher purity.
  • Unique non-charged hydrophilic linkage reduces non-specific binding.
  • Binding capacity for histidine-tagged protein is greater than 15 mg/mL.
  • Binding under denaturing or non-denaturing conditions.
  • One-step purification.
  • Minimizes unwanted ionic interactions.
  • Minimal nickel leaching.
  • Bead size: 45-165 μm.

Linkage

It is also available with the EZview™ technology (Product Code E3528).

Stato fisico

1:1 suspension in a 20% ethanol solution

Stoccaggio e stabilità

HIS-Select Nickel Affinity Gel is stable for at least one year when stored properly. The HIS-Select Nickel Affinity Gel should be cleaned after each use and an antimicrobial agent such as 20% ethanol should be added to the storage buffer.

Note legali

HIS-Select is a registered trademark of Merck KGaA, Darmstadt, Germany

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Indicazioni di pericolo

Classi di pericolo

Flam. Liq. 3

Codice della classe di stoccaggio

3 - Flammable liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

89.6 °F - closed cup

Punto d’infiammabilità (°C)

32 °C - closed cup


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I clienti hanno visto anche

Slide 1 of 4

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Purification and characterization of the guinea pig sigma-1 receptor functionally expressed in Escherichia coli
Ramachandran S, et al.
Protein Expression and Purification, 51(2), 283-292 (2007)
S100A14, a member of the EF-hand calcium-binding proteins, is overexpressed in breast cancer and acts as a modulator of HER2 signaling
Xu C, et al.
The Journal of Biological Chemistry, 289(2), 827-837 (2014)
F Weerkamp et al.
Leukemia, 23(6), 1106-1117 (2009-04-24)
BCR-ABL fusion proteins show increased signaling through their ABL tyrosine kinase domain, which can be blocked by specific inhibitors, thereby providing effective treatment. This makes detection of BCR-ABL aberrations of utmost importance for diagnosis, classification and treatment of leukemia patients.
Leucine zipper-like motifs of HrpZPss are not essential to induce hypersensitive response in tobacco
Anil K, et al.
Journal of Plant Physiology, 96(1), 57-62 (2014)
Zhijin Zhang et al.
Plant physiology, 150(1), 365-377 (2009-03-06)
Fine-tuning of ethylene production plays an important role in developmental processes and in plant responses to stress, but very little is known about the regulation of ethylene response factor (ERF) proteins in ethylene biosynthesis genes and ethylene production. Identifying cis-acting

Contenuto correlato

Protein purification techniques, reagents, and protocols for purifying recombinant proteins using methods including, ion-exchange, size-exclusion, and protein affinity chromatography.

Tecniche, reagenti e protocolli per la purificazione di proteine ricombinanti mediante tecniche di cromatografia a scambio ionico, di esclusione dimensionale e di affinità.

Tecnologie per l'espressione di proteine con vari sistemi di espressione, a supporto della ricerca e della produzione di agenti terapeutici e vaccini.

Protein expression technologies for various expression systems supporting research, therapeutics, and vaccine production.

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Domande

1–6 di 6 domande  
  1. Can imidazole be used with HIS-Select® Nickel Affinity Gel, Product P6611?

    1 risposta
    1. For column chromatography, no more than 20 mM is suggested in the extract, equilibration, and wash buffers to prevent non-specific binding of proteins. No more than 250 mM is suggested for the elution buffers.  Many proteins will elute with imidazole levels as low as 100 to 200 mM.  For batch methods the imidazole concentration may have to be reduced or eliminated.When a protein is expressed at low levels, the presence of the imidazole limits the binding of the protein in the batch method but not when  used in a column.

      Utile?

  2. Why won't my recombinant protein with a histidine-containing tag bind to HIS-Select® Nickel Affinity Gel, Product P6611?

    1 risposta
    1. Verify the pH and composition of sample and equilibration buffers.  Make sure there are no chelating or reducing agents present in the extraction buffer. If using the batch mode, remove imidazole.  Run the affinity purification under denaturing conditions.  Run a Western blot of the extract to verify that the recombinant protein is present.

      Utile?

  3. Can I use SDS with HIS-Select® Nickel Affinity Gel, Product P6611?

    1 risposta
    1. 0.1% SDS has been used with some samples, with no adverse effects on the observed protein binding.  However, SDS will effectively coat proteins and may block the binding to the column.  It is probably very  protein-specific and an SDS concentration that works for one protein may not work for another.

      Utile?

  4. What needs to be done if the HIS-Select® Nickel Affinity Gel, Product P6611, resin turns brown on reuse?

    1 risposta
    1. During purification many protein extracts tend to discolor an affinity gel during the loading step. The original color will return after the wash or elution step. If the color is still not changing strip and recharge the affinity gel with nickel.  Wash with EDTA and recharge with Nickel solution.

      Utile?

  5. What is the Department of Transportation shipping information for this product?

    1 risposta
    1. Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.

      Utile?

  6. Can Tris buffers be used instead of phosphate buffer for HIS-Select® Nickel Affinity Gel, Product P6611?

    1 risposta
    1. Yes, Tris buffers should work.

      Utile?

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