ProBond™ Nickel-Chelating Resin
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Invitrogen™

ProBond™ Nickel-Chelating Resin

ProBond™ Nickel-Chelating Resin is a nickel-charged affinity resin used to purify recombinant proteins containing a polyhistidine (6xHis) sequence. Proteins boundRead more
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Catalog NumberQuantity
R80115150 mL
R8010150 mL
Catalog number R80115
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2,181.65
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2,490.00
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Estimated availability date 12-Jul-2025
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Price (USD)
2,181.65
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2,490.00
Save 308.35 (12%)
Each
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ProBond™ Nickel-Chelating Resin is a nickel-charged affinity resin used to purify recombinant proteins containing a polyhistidine (6xHis) sequence. Proteins bound to the resin may be eluted with either low pH buffer or by competition with imidazole or histidine. One-step purification can be performed under both native and denaturing conditions. ProBond™ Resin uses the chelating ligand iminodiacetic acid (IDA) coupled to a highly cross-linked 6% agarose resin that is suitable for use in FPLC, batch, and gravity flow applications.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Quantity150 mL
Stationary PhaseNickel-Chelating
Column TypeAffinity Column
FormSuspension
Product LineProBond™
TypeResin
Unit SizeEach
Contents & Storage
The ProBond™ resin is pre-charged and able to bind 1-5 mg of recombinant protein per 1 ml of resin. It is provided as a 50% slurry in 20% ethanol. The resin will appear blue in color when charged with Ni2+ . Store at +4°C. ProBond™ resin is guaranteed stable for 6 months when properly stored.

Frequently asked questions (FAQs)

How do you typically detect expression of a recombinant fusion protein?

Western blot analysis is typically used to detect the expressed protein. We sell several antibodies against various epitopes, such as Xpress, HisG, V5, or C-terminal 6xHis. Additionally, His-tagged proteins can be purified using our ProBond Purification System via affinity purification.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

What expression levels can be expected with the pTrcHis/CAT construct?

In one experiment, 35 µg CAT/mg total protein or 68.2 mg CAT/liter of culture was obtained. 50 ml of cell extract was loaded onto a ProBond column and 2 mg of CAT was recovered. The eluted protein appeared reasonably pure on a gel.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

I purified my protein from a ProBond column using denaturing conditions. After elution, I tried digesting off my N- terminal tag with EKMax Enterokinase, but see no EK cleavage. What can you suggest I try?

The enzyme could be denatured. Try buffer exchange or dialysis before digestion with EKMax Enterokinase.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

Can ProBond or Ni-NTA beads be used for large-scale preparations?

ProBond and Ni-NTA beads can be used in FPLC columns. However, the beads can only withstand low pressure (~43.5 psi max).

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

The pH of my ProBond buffers is off. Instead of pH 4-7, it is close to pH 9. What should I do?

pH drift is typical with these buffers. Adjust with concentrated HCl if the pH is too high or with 10 N NaOH if the pH is low.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

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