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H8162

Millipore

HIS-Select® Cobalt Affinity Gel

(1:1 suspension in a 30% ethanol solution)

Synonym(s):

cobalt affinity gel, cobalt charged agarose

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About This Item

UNSPSC Code:
41106500
NACRES:
NA.56

Quality Level

200

form

(1:1 suspension in a 30% ethanol solution)

shelf life

1 yr (when stored properly.)

technique(s)

protein purification: suitable

matrix

6% Beaded Agarose

capacity

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

storage temp.

2-8°C

General description

The HIS-Select Cobalt Affinity Gel is a quadridentate chelate on beaded agarose that is charged with cobalt. The gel is designed to specifically bind histidine-containing proteins / His-tag proteins. It is selective for recombinant proteins with histidine tags and exhibits low non-specific binding of other proteins.
HIS-Select Cobalt Affinity Gel is an immobilized metal-ion affinity chromatography (IMAC) product. The matrix for this affinity gel is 6% beaded agarose. The selectivity can be modulated with the inclusion of imidazole during chromatography. HIS-Select Cobalt Affinity Gel is durable and can capture recombinant proteins with histidine tags at a high flow rate. Recombinant proteins with His tags are bound using native, denaturing, or mild reducing conditions. The capacity of this affinity gel is typically >15 mg/mL of packed gel, determined with a His-tagged protein of molecular mass ~30 kDa.

Application

HIS-Select Cobalt Affinity Gel allows for high purity, low non-specific binding, and high binding capacity of protein. HIS-Select Cobalt Affinity Gel also works well for purification of histidine-tagged proteins / His-tag proteins in native, denaturing, or mild reducing conditions. HIS-Select™ Cobalt Affinity Gel has been used to purify His-tagged proteins.

Physical form

1:1 suspension in a 30% ethanol solution

Legal Information

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

Signal Word

Danger

Hazard Classifications

Aquatic Acute 1 - Aquatic Chronic 1 - Carc. 1B - Eye Irrit. 2 - Flam. Liq. 3 - Muta. 2 - Repr. 1B - Resp. Sens. 1 - Skin Sens. 1

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Kurt C Curtis et al.
Parasitology research, 120(2), 535-545 (2021-01-09)
Paragonimiasis is a foodborne trematode infection that affects 23 million people, mainly in Asia. Lung fluke infections lead frequently to chronic cough with fever and hemoptysis, and are often confused with lung cancer or tuberculosis. Paragonimiasis can be efficiently treated
Shiran Barber-Zucker et al.
Scientific reports, 6, 31933-31933 (2016-08-24)
Cation diffusion facilitators (CDF) are highly conserved, metal ion efflux transporters that maintain divalent transition metal cation homeostasis. Most CDF proteins contain two domains, the cation transporting transmembrane domain and the regulatory cytoplasmic C-terminal domain (CTD). MamM is a magnetosome-associated
Michael Riis Hansen et al.
Biomolecular NMR assignments, 8(1), 103-108 (2013-01-15)
The type I phosphoribosyltransferase OMP synthase (EC 2.4.2.10) is involved in de novo synthesis of pyrimidine nucleotides forming the UMP precursor orotidine 5'-monophosphate (OMP). The homodimeric enzyme has a Rossman α/β core topped by a base-enclosing "hood" domain and a
Katie L Whalen et al.
Journal of chemical information and modeling, 53(9), 2349-2359 (2013-10-12)
Glutamate racemase (GR) is a cofactor independent amino acid racemase that has recently garnered increasing attention as an antimicrobial drug target. There are numerous high resolution crystal structures of GR, yet these are invariably bound to either D-glutamate or very
Adam S B Jalal et al.
Cell reports, 32(3), 107928-107928 (2020-07-23)
Specific interactions between proteins and DNA are essential to many biological processes. Yet, it remains unclear how the diversification in DNA-binding specificity was brought about, and the mutational paths that led to changes in specificity are unknown. Using a pair
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