Pierce™ IP Lysis Buffer
Thermo Scientific™

Pierce™ IP Lysis Buffer

Maximize cell lysate yield, purity and compatibility with this immunoprecipitation-optimized protein extraction reagent.
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Catalog NumberQuantity
87787100 mL
87788250 mL
Catalog number 87787
Price (MXN)
-
Quantity:
100 mL
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Thermo Scientific Pierce IP Lysis Buffer is optimized for cell lysate yield, purity and compatibility with immunoprecipitation (IP and Co-IP) as the downstream application for the cell lysate.

Features of IP Lysis Buffer:

  • Optimized for compatibility with immunoprecipitation and pull-down assays
  • Compatible with protein assays, reporter assays and immunoassay procedures
  • Ready-made formula is effective for extracting cytoplasmic, membrane and nuclear proteins
  • Gentle formulation helps maintain protein complexes for co-immunoprecipitation
  • Does not liberate genomic DNA which can cause high sample viscosity

IP Lysis Buffer is a mammalian whole cell lysis reagent based on a modified RIPA buffer formulation without SDS. This moderate-strength lysis buffer effectively solubilizes cellular proteins but does not liberate genomic DNA or disrupt protein complexes like ordinary RIPA buffer. Pierce IP Lysis Buffer is specially formulated for pull-down and immunoprecipitation assays.

Pierce IP Lysis Buffer is effective for lysing cultured mammalian cells from both plated cells and cells pelleted from suspension cultures. Optimized for pull-down and immunoprecipitation assays, this lysis buffer is also compatible with many other applications, including the Thermo Scientific Pierce BCA and 660 nm Protein Assays, protein purification and immunoassays (e.g., ELISA, Western blot).

Pierce IP Lysis Buffer is composed of 25 mM Tris-HCl pH 7.4, 150 mM NaCl, 1 mM EDTA, 1% NP-40 and 5% glycerol. The buffer does not contain protease or phosphatase inhibitors; however, if desired, inhibitors, such as Thermo Scientific Halt Protease Inhibitor Cocktail or Phosphatase Inhibitor Cocktail can be added just before use to prevent proteolysis and maintain phosphorylation of proteins.

Related Products

  • M-PER™ Mammalian Protein Extraction Reagent (Cat. No. 78501)
  • RIPA Lysis and Extraction Buffer (Cat. No. 89900)
For Research Use Only. Not for use in diagnostic procedures.

The Pierce IP Lysis Buffer is effective for lysing cultured mammalian cells from both plated cells and cells pelleted from suspension cultures. Optimized for pull-down and immunoprecipitation assays, this lysis buffer is also compatible with many other applications, including the Thermo Scientific Pierce BCA and 660 nm Protein Assays, protein purification and immunoassays (e.g., ELISA, Western blot).

The Pierce IP Lysis Buffer is composed of 25 mM Tris-HCl pH 7.4, 150 mM NaCl, 1 mM EDTA, 1% NP-40 and 5% glycerol. The buffer does not contain protease or phosphatase inhibitors; however, if desired, inhibitors, such as Thermo Scientific Halt Protease Inhibitor Cocktail or Phosphatase Inhibitor Cocktail can be added just before use to prevent proteolysis and maintain phosphorylation of proteins.

Specifications
FormatLiquid
Quantity100 mL
Volume (Metric)100 mL
Product LinePierce
Product TypeIP Lysis Buffer
Unit SizeEach
Contents & Storage
Upon receipt store at 4°C.

Citations & References (3)

Citations & References
Abstract
Rac1 augments Wnt signaling by stimulating ß-catenin-lymphoid enhancer factor-1 complex assembly independent of ß-catenin nuclear import.
Authors:Jamieson C, Lui C, Brocardo MG, Martino-Echarri E, Henderson BR
Journal:
PubMed ID:26403202
ß-Catenin transduces the Wnt signaling pathway and its nuclear accumulation leads to gene transactivation and cancer. Rac1 GTPase is known to stimulate ß-catenin-dependent transcription of Wnt target genes and we confirmed this activity. Here we tested the recent hypothesis that Rac1 augments Wnt signaling by enhancing ß-catenin nuclear import; however, ... More
Characterization of extracellular circulating microRNA.
Authors:Turchinovich A, Weiz L, Langheinz A, Burwinkel B
Journal:Nucleic Acids Res
PubMed ID:21609964
MicroRNAs (miRNAs), a class of post-transcriptional gene expression regulators, have recently been detected in human body fluids, including peripheral blood plasma as extracellular nuclease resistant entities. However, the origin and function of extracellular circulating miRNA remain essentially unknown. Here, we confirmed that circulating mature miRNA in contrast to mRNA or ... More
Increasing the Receptor Tyrosine Kinase EphB2 Prevents Amyloid-ß-induced Depletion of Cell Surface Glutamate Receptors by a Mechanism That Requires the PDZ-binding Motif of EphB2 and Neuronal Activity.
Authors:Miyamoto T, Kim D, Knox JA, Johnson E, Mucke L
Journal:J Biol Chem
PubMed ID:26589795
'Diverse lines of evidence suggest that amyloid-ß (Aß) peptides causally contribute to the pathogenesis of Alzheimer disease (AD), the most frequent neurodegenerative disorder. However, the mechanisms by which Aß impairs neuronal functions remain to be fully elucidated. Previous studies showed that soluble Aß oligomers interfere with synaptic functions by depleting ... More