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Merck

P6611

HIS-Select® Nickel Affinity Gel

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

동의어(들):

Ni-NTA resin, nickel charged agarose

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제품정보 (DICE 배송 시 비용 별도)

NACRES:
NA.56
UNSPSC Code:
12352200
기술 서비스
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도움 문의

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.

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.

Physical form

1:1 suspension in a 20% ethanol solution

Preparation Note

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.

Other Notes

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

Legal Information

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

pictograms

Flame

signalword

Warning

hcodes

Hazard Classifications

Flam. Liq. 3

저장 등급

3 - Flammable liquids

wgk

WGK 3

flash_point_f

89.6 °F - closed cup

flash_point_c

32 °C - closed cup


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시험 성적서(COA)

Lot/Batch Number

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

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
Michael B Battles et al.
Nature communications, 8(1), 1528-1528 (2017-11-17)
Human metapneumovirus (hMPV) is a frequent cause of bronchiolitis in young children. Its F glycoprotein mediates virus-cell membrane fusion and is the primary target of neutralizing antibodies. The inability to produce recombinant hMPV F glycoprotein in the metastable pre-fusion conformation
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)

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