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P6611

Millipore

HIS-Select® Nickel Affinity Gel

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

Synonym(s):

Ni-NTA resin, nickel charged agarose

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.56

conjugate

magnetic beads

Quality Level

form

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

feature

hydrophilic

packaging

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

concentration

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

technique(s)

protein purification: suitable

color

faint blue to very dark blue

matrix

6% Beaded Agarose

capacity

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

transition temp

flash point 32 °C (closed cup)

storage temp.

2-8°C

General description

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.

Application

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

Features and Benefits

  • 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).

Physical form

1:1 suspension in a 20% ethanol solution

Storage and Stability

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.

Legal Information

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

related product

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Description
Pricing

Pictograms

Flame

Signal Word

Warning

Hazard Statements

Hazard Classifications

Flam. Liq. 3

Storage Class Code

3 - Flammable liquids

WGK

WGK 3

Flash Point(F)

89.6 °F - closed cup

Flash Point(C)

32 °C - closed cup


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
Lindsay S Garrenton et al.
Molecular and cellular biology, 29(2), 582-601 (2008-11-13)
Saccharomyces cerevisiae cells are capable of responding to mating pheromone only prior to their exit from the G(1) phase of the cell cycle. Ste5 scaffold protein is essential for pheromone response because it couples pheromone receptor stimulation to activation of
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.

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