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EP022431064

Eppendorf® Protein LoBind tubes

capacity 0.5 mL, PCR clean, pkg of 100 ea (2 x 50ea)

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About This Item

UNSPSC Code:
41121703

material

(push fit)
polypropylene cap

sterility

non-sterile

feature

PCR clean

packaging

pkg of 100 ea (2 x 50ea)

manufacturer/tradename

Eppendorf® 022431064

parameter

-18,000 × g max. RCF

capacity

0.5 mL

diam.

7.3 mm

color

clear

suitability

suitable for PCR

binding type

low binding surface

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General description

Avoid losing valuable samples during centrifugation, incubation and storage! Rely on the excellent protection offered by the hinged Safe-Lock lid. It contains all of our experience from 50 years of continuous optimization and development. Trust the original Eppendorf Safe-Lock Tubes, because your samples deserve only the best.
Protein LoBind Tubes, snap cap, Protein LoBind, 0.5 mL, PCR clean, colorless, 100 tubes (2 bags × 50 tubes)
  • Eppendorf LoBind material ensures optimized sample recovery for improved assay results
  • Free of surface coating (e.g., silicone) to minimize the risk of sample interference
  • Lot-certified PCR clean purity grade: free of human DNA, DNase, RNase and PCR inhibitors
  • Available in tube, microplate, and deepwell plate formats for easy-up scaling
  • Precise lid sealing to minimize evaporation

Features and Benefits

Eppendorf Protein LoBind Tubes are specifically designed to ensure you get maximal protein recovery.

Legal Information

Eppendorf is a registered trademark of Eppendorf AG

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Cláudia P Grou et al.
The Journal of biological chemistry, 283(21), 14190-14197 (2008-03-25)
According to current models of peroxisomal biogenesis, newly synthesized peroxisomal matrix proteins are transported into the organelle by Pex5p. Pex5p recognizes these proteins in the cytosol, mediates their membrane translocation, and is exported back into the cytosol in an ATP-dependent
Arzu Umar et al.
Proteomics, 7(2), 323-329 (2006-12-14)
Proteomics assays hold great promise for unraveling molecular events that underlie human diseases. Effective analysis of clinical samples is essential, but this task is considerably complicated by tissue heterogeneity. Laser capture microdissection (LCM) can be used to selectively isolate target
Kelly Hodge et al.
Journal of proteomics, 88, 92-103 (2013-03-19)
Mass spectrometry, in the past five years, has increased in speed, accuracy and use. With the ability of the mass spectrometers to identify increasing numbers of proteins the identification of undesirable peptides (those not from the protein sample) has also
Byung-Gyu Kim et al.
Proteomics, 6(4), 1166-1174 (2006-01-20)
Runx2 is a key transcription factor in osteoblast differentiation, and its activity is regulated by fibroblast growth factors (FGFs). Craniosynostosis, characterized by premature suture closure, results from mutations that generate constitutively active FGF receptors (FGFRs). We previously showed that FGF/FGFR-activated
Steven J Bark et al.
Journal of proteome research, 6(11), 4511-4516 (2007-09-14)
Differential recovery of peptides due to nonspecific adsorption can seriously compromise reproducibility and quality of proteomic data for peptide analyses by liquid chromatography-mass spectrometry (LC-MS). This study demonstrates large variations in reproducibility and quantitation of LC-MS data for peptides derived

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