ProBond™ Nickel-Chelating Resin
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Citas y referencias (5)
Invitrogen™

ProBond™ Nickel-Chelating Resin

La resina quelante de níquel ProBond™ es una resina de afinidad cargada de níquel que se utiliza para purificar proteínasMás información
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Número de catálogoCantidad
R80115150 ml
R8010150 mL
R80115TS
también denominado R80115
Número de catálogo R80115
Precio (MXN)
-
Cantidad:
150 ml
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La resina quelante de níquel ProBond™ es una resina de afinidad cargada de níquel que se utiliza para purificar proteínas recombinantes que contienen una secuencia de polihistidina (6xHis). Las proteínas ligadas a la resina pueden eluirse con tampón de pH bajo o por competencia con imidazol o histidina. La purificación en un solo paso se puede realizar tanto en condiciones nativas como desnaturalizantes. La resina ProBond™ utiliza el ácido inodiacético (IDA) del ligando quelante unido a una resina de agarosa al 6 % altamente entrecruzada que es adecuada para su uso en aplicaciones de flujo por gravedad, lotes y FPLC.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Cantidad150 ml
Fase estacionariaQuelante de níquel
Tipo de columnaColumna de afinidad
FormularioSuspensión
Línea de productosProBond
TipoResina
Unit SizeEach
Contenido y almacenamiento
La resina ProBond™ está precargada y es capaz de unir de 1 a 5 mg de proteína recombinante por cada 1 ml de resina. Se proporciona como una pulpa al 50 % en etanol al 20%. La resina aparecerá de color azul cuando se cargue con Ni2+. Almacenar a +4 °C. Se garantiza la estabilidad de la resina ProBond™ durante seis meses si se almacenan correctamente.

Preguntas frecuentes

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.

View all ProBond™ Nickel-Chelating Resin, 150 mL FAQs

Citations & References (5)

Citations & References
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