ProBond™ Nickel-Chelating Resin
Product Image
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 bound深入閱讀
Have Questions?
變更視圖buttonViewtableView
產品號碼Quantity
R80115150 mL
R8010150 mL
R80115TS
亦稱為 R80115
產品號碼 R80115
價格 (TWD)
91,350.00
Online offer
Ends: 31-Dec-2025
101,500.00
您節省 10,150.00 (10%)
Each
新增至購物車
Quantity:
150 mL
Request bulk or custom format
價格 (TWD)
91,350.00
Online offer
Ends: 31-Dec-2025
101,500.00
您節省 10,150.00 (10%)
Each
新增至購物車
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.
規格
Quantity150 mL
Stationary PhaseNickel-Chelating
Column TypeAffinity Column
FormSuspension
Product LineProBond
TypeResin
Unit SizeEach
內容物與存放
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.

常見問答集 (常見問題)

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.

引用資料與參考文獻 (5)

引用資料與參考文獻
Abstract
Total synthesis of cyclic ADP-carbocyclic-ribose, a stable mimic of Ca2+-mobilizing second messenger cyclic ADP-ribose.
Authors: Shuto S; Fukuoka M; Manikowsky A; Ueno Y; Nakano T; Kuroda R; Kuroda H; Matsuda A;
Journal:J Am Chem Soc
PubMed ID:11535079
'The synthesis of cyclic ADP-carbocyclic-ribose (cADPcR, 4) designed as a stable mimic of cyclic ADP-ribose (cADPR, 1), a Ca2+-mobilizing second messenger, was achieved using as the key step a condensation reaction with the phenylthiophosphate-type substrate 14 to form an intramolecular pyrophosphate linkage. The N-1-carbocyclic-ribosyladenosine derivative 16 was prepared via the ... More
Interaction between the insulin receptor and its downstream effectors. Use of individually expressed receptor domains for structure/function analysis.
Authors:Paz K, Voliovitch H, Hadari YR, Roberts CT Jr, LeRoith D, Zick Y
Journal:J Biol Chem
PubMed ID:8636129
'A structural analysis has been carried out to determine which part of the intracellular domain of the insulin receptor (IR) beta subunit is involved in direct interaction with the receptor substrates IRS-1 and Shc. Toward this end, the juxtamembrane (JM) domain (amino acids 943- 984) and the carboxyl-terminal (CT) region ... More
A Calcium-Responsive Transcription Factor, CaRF, that Regulates Neuronal Activity-Dependent Expression of BDNF.
Authors: Tao Xu; West Anne E; Chen Wen G; Corfas Gabriel; Greenberg Michael E;
Journal:Neuron
PubMed ID:11832226
'Transcription of the brain-derived neurotrophic factor (BDNF) gene is regulated in a calcium- and neuron-selective manner; however, the mechanisms that underlie this selectivity are not known. We have characterized a new calcium-response element, CaRE1, that is required for activity-dependent transcription of BDNF exon III and have cloned a transcription factor, ... More
Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase.
Authors:Zhou T, Rosen BP
Journal:J Biol Chem
PubMed ID:9242630
The ars operon of plasmid R773 encodes an ATP-dependent extrusion pump for arsenite and antimonite in Escherichia coli. The ArsA ATPase is the catalytic subunit of the pump protein, with two nucleotide binding consensus sequences, one in the NH2-terminal half and one in the COOH- terminal half of the protein. ... More
Structure and ligand of a histone acetyltransferase bromodomain.
Authors:Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM
Journal:Nature
PubMed ID:10365964
Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure ... More