RFP-Trap® M (coupled to magnetic beads)

Application: Immunoprecipitation (IP), Mass Spectrometry (MS), Enzyme Activity Assay (EAA)

Catalog no.: ABIN1082218

Additional Information

Description: Red fluorescent proteins (RFP) and variants thereof are widely used to study protein localization and dynamics. For biochemical analyses including mass spectroscopy and enzyme activity measurements these RFP fusion proteins and their interacting factors can be isolated fast and efficiently (one step) via immunoprecipitation using the RFP-Trap®. Since the interaction is mediated by a small RFP binding protein coupled to agarose beads the RFPTrap®_M enables purification of any protein of interest fused to RFP (monomeric derivates of DsRed, including mRFP1, mCherry, mPlum, mOrange).

Characteristics: particle size 0.5 - 1 µm

Specificity: RFP-Trap® efficiently pulls down most common monomeric red fluorescent proteins derived from DsRed, e.g. mRFP1, mCherry, mPlum and RFP fusion proteins. No cross-reaction to GFP derivates can be detected.

Application Details

Principle:  for biochemical analysis of RFP fusion proteins and their interacting partners.

Buffer: PBS

Preservative: 0.05% Sodium azide

Storage: Shipped at ambient temperature. Upon receipt store at 4°C. Stable for 6 months. Do not freeze.

Restrictions: For Research Use only

Images

RFP-Trap® to immunoprecipitate red fluorescent proteins Pulldown of different monomeric red fluorescent proteins mRFP, mCherry and mOrange from cell extracts of human cells. Input (I), non-bound (FT) and bound (B) fractions were separated by SDS-PAGE followed by Coomassie staining and Western Blotting.

Publications

Product: Aboobakar, Wang, Heitman et al.: "The C2 domain protein Cts1 functions in the calcineurin signaling circuit during high-temperature stress responses in Cryptococcus neoformans." in: Eukaryotic cell, Vol. 10, Issue 12, pp. 1714-23, 2011 (PubMed).

Neumüller, Wirtz-Peitz, Lee et al.: "Stringent analysis of gene function and protein-protein interactions using fluorescently tagged genes." in: Genetics, Vol. 190, Issue 3, pp. 931-40, 2012 (PubMed).

Moutin, Raynaud, Fagni et al.: "GKAP-DLC2 interaction organizes the postsynaptic scaffold complex to enhance synaptic NMDA receptor activity." in: Journal of cell science, Vol. 125, Issue Pt 8, pp. 2030-40, 2012 (PubMed).

Lefebvre, Klaus-Heisen, Pietraszewska-Bogiel et al.: "Role of N-glycosylation sites and CXC motifs in trafficking of medicago truncatula Nod factor perception protein to plasma membrane." in: The Journal of biological chemistry, Vol. 287, Issue 14, pp. 10812-23, 2012 (PubMed).

Zanet, Jayo, Plaza et al.: "Fascin promotes filopodia formation independent of its role in actin bundling." in: The Journal of cell biology, Vol. 197, Issue 4, pp. 477-86, 2012 (PubMed).