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Citations & References (3)
Y-PER™ Yeast Protein Extraction Reagent
Release functionally active solubilized proteins with the first commercially available yeast lysis reagent to use a mild detergent lysis procedure.
| Catalog Number | Quantity |
|---|---|
| 78990 | 500 mL |
Catalog number 78990
Price (INR)
143,454.00
Each
Quantity:
500 mL
Price (INR)
143,454.00
Each
Thermo Scientific™ Y-PER Yeast Protein Extraction Reagent is the first commercially available yeast lysis reagent to use a mild detergent lysis procedure to efficiently release functionally active solubilized proteins.
This detergent-based cell lysis buffer eliminates the need to use glass beads or mechanical disruption to break through the thick proteinaceous cell envelope to extract protein Y-PER Reagent is effective for S. cerevisiae and other popular species, making it applicable for use in fusion-tagged protein purification and reporter enzyme assays with these model organisms. The lysis reagent also can be used for genomic and plasmid DNA extraction from yeast. The standard protocol for protein extraction is easy: simply add an appropriate volume of Y-PER Reagent to pelleted yeast cells, incubate at room temperature for approximately 20 minutes and spin down the debris. The resulting supernatant is a concentrated protein solution, surpassing typical yields obtained with traditional glass bead disruption.
Highlights:
More protein – extracts more than twice as much protein as glass bead methods
Less hassle – eliminates the difficulties associated with traditional glass bead lysis (e.g., clinging static-charged beads, protein/bead clumps and runaway beads)
Optmized for yeast – validated for use with Saccharomyces cerevisiae, Schizosaccharomyces pombe and Pichia pastoris
Versatile – effective for many different organisms, including Bacillus subtilus and both Gram-positive and Gram-negative bacteria; suitable for use in a diverse range of situations
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Quantity500 mL
FormatLiquid
Product TypeYeast Protein Extraction Reagent
Volume (Metric)500 mL
Product LineY-PER
Unit SizeEach
Contents & Storage
Store product at room temperature.
Frequently asked questions (FAQs)
Can you provide the shelf-life for the Y-PER Yeast Protein Extraction Reagent?
Does Y-PER Yeast Protein Extraction Reagent (Cat. No. 78990) yield samples that are compatible with the Pierce BCA Protein Assay Kit (Cat. No. 23225)?
Citations & References (3)
Citations & References
Abstract
The hCds1 (Chk2)-FHA domain is essential for a chain of phosphorylation events on hCds1 that is induced by ionizing radiation.
Journal:J Biol Chem
PubMed ID:11390408
'hCds1 (Chk2) is an evolutionarily conserved kinase that functions in DNA damage response and cell cycle checkpoint. The Cds1 family of kinases are activated by a family of large phosphatidylinositol 3-kinase-like kinases. In humans, ataxia telangiectasia-mutated (ATM) and ataxia-telangiectasia and Rad3-related kinases activate hCds1 by phosphorylating Thr(68) . hCds1 and
Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling.
Journal:Mol Cell Biol
PubMed ID:17938211
Hormone-dependent transactivation by several of the steroid hormone receptors is potentiated by the Hsp90-associated cochaperone FKBP52, although not by the closely related FKBP51. Here we analyze the mechanisms of potentiation and the functional differences between FKBP51 and FKBP52. While both have peptidyl-prolyl isomerase activity, this is not required for potentiation,
WOX1 is essential for tumor necrosis factor-, UV light-, staurosporine-, and p53-mediated cell death, and its tyrosine 33-phosphorylated form binds and stabilizes serine 46-phosphorylated p53.
Journal:J Biol Chem
PubMed ID:16219768
WW domain-containing oxidoreductase WOX1, also named WWOX or FOR, undergoes Tyr33 phosphorylation at its first N-terminal WW domain and subsequent nuclear translocation in response to sex steroid hormones and stress stimuli. The activated WOX1 binds tumor suppressor p53, and both proteins may induce apoptosis synergistically. Functional suppression of WOX1 by