Skip to Content
Merck
All Photos(1)

Key Documents

View All Documentation

70666

Millipore

Ni-NTA His•Bind® Resin

Synonym(s):

nickel affinity gel, nickel charged agarose

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

UNSPSC Code:
41106500
NACRES:
NA.56

form

slurry

Quality Level

400

manufacturer/tradename

Novagen®

storage condition

do not freeze

application(s)

life science and biopharma

shipped in

ambient

storage temp.

2-8°C

General description

Ni-NTA His•Bind Resin is a high-performance Ni2+-charged agarose used for rapid one-step purification of proteins containing a His•Tag sequence by metal chelation chromatography. NTA chemistry minimizes metal leaching during purification and is compatible with up to 10 mM β-mercaptoethanol or 1 mM Tris(hydroxypropyl)phosphine (THP) for reduction of disulfide bonds. Ni-NTA His•Bind Resin has a binding capacity of 5–10 mg His•Tag fusion protein per ml resin.

Supplied as a 50% slurry; the quantity/pack is based on the amount of the settled resin.

Warning

Toxicity: Flammable (J)

Other Notes

Due to the nature of the Hazardous Materials in this shipment, additional shipping charges may be applied to your order. Certain sizes may be exempt from the additional hazardous materials shipping charges. Please contact your local sales office for more information regarding these charges.

Legal Information

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

Pictograms

Flame
GHS02

Signal Word

Danger

Hazard Statements

H225

Hazard Classifications

Flam. Liq. 2

Storage Class Code

3 - Flammable liquids

WGK

WGK 1

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Hadas Bar-Joseph et al.
Reproductive biomedicine online, 41(2), 335-342 (2020-06-14)
Does recombinant pigment epithelium derived factor (PEDF) have potential in treating uterine fibroids? In-vitro models that used human leiomyoma and Eker rat uterine leiomyoma (ELT-3) cell lines. The ELT-3 cell line was used to examine cellular targets after adding recombinant
Bao-Rui Zhao et al.
Journal of immunology (Baltimore, Md. : 1950), 204(3), 487-497 (2019-12-20)
Rapid synthesis and release of active antimicrobial peptides (AMPs) is an important strategy in innate immune. Processing of the precursor into the active form is a common posttranslational modification of AMPs in mammals. However, in invertebrates, the mechanism of AMP
Yu-Xi Luo et al.
The EMBO journal, 39(7), e102008-e102008 (2020-03-03)
Deposition of H2A.Z in chromatin is known to be mediated by a conserved SWR1 chromatin-remodeling complex in eukaryotes. However, little is known about whether and how the SWR1 complex cooperates with other chromatin regulators. Using immunoprecipitation followed by mass spectrometry

Articles

YeastBuster™ Protein Extraction Reagent for Fast, Efficient Extraction of Proteins from Yeast

YeastBuster™ Protein Extraction Reagent for Fast, Efficient Extraction of Proteins from Yeast

BugBuster® and Benzonase® Reagents are the Clear Solutions to Simple, Efficient Extraction of E. coli Proteins

This article shows the use of BugBuster® and Benzonase® as protein purification tools to extract recombinant proteins from E. coli and to reduce the viscosity of the extract.

BugBuster® and Benzonase® Reagents are the Clear Solutions to Simple, Efficient Extraction of E. coli Proteins

This article shows the use of BugBuster® and Benzonase® as protein purification tools to extract recombinant proteins from E. coli and to reduce the viscosity of the extract.

BugBuster® and Benzonase® Reagents are the Clear Solutions to Simple, Efficient Extraction of E. coli Proteins

This article shows the use of BugBuster® and Benzonase® as protein purification tools to extract recombinant proteins from E. coli and to reduce the viscosity of the extract.

See All

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service