IP50
Protein G Immunoprecipitation Kit
sufficient for 50 assays
Synonym(s):
Immunoprecipitation kit
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.32
Pricing and availability is not currently available.
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usage
sufficient for 50 assays
Quality Level
technique(s)
immunoprecipitation (IP): suitable
storage temp.
2-8°C
Application
The kit is designed to allow maximal recovery of immunoprecipitates. It provides all the necessary reagents to perform immunoprecipitation from cell extracts of any protein to which a suitable antibody is available. Based on protein G, the kit binds to most commonly used antibodies. In addition, spin columns are provided to enable quick washes without the loss of protein G resin and thus protein yield is maximized.
Features and Benefits
- Minimal loss of antigen-antibody bound beads during washing.
- Minimal or no non-specific signals by increasing the stringency of the washing step.
Preparation Note
When preparing reagents, use ultrapure water (17M -cm)
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Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Flam. Liq. 3 - Skin Irrit. 2
Storage Class Code
3 - Flammable liquids
WGK
WGK 3
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Patricia Workman et al.
Journal of bacteriology, 194(13), 3512-3521 (2012-05-01)
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F Gautier et al.
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Peter J Eastmond
The Plant cell, 19(4), 1376-1387 (2007-04-24)
Hydrogen peroxide is a major by-product of peroxisomal metabolism and has the potential to cause critical oxidative damage. In all eukaryotes, catalase is thought to be instrumental in removing this H(2)O(2). However, plants also contain a peroxisomal membrane-associated ascorbate-dependent electron
Phu Vuong et al.
Journal of bacteriology, 190(5), 1507-1517 (2008-01-01)
In Escherichia coli, YaeT, together with four lipoproteins, YfgL, YfiO, NlpB, and SmpA, forms a complex that is essential for beta-barrel outer membrane protein biogenesis. Data suggest that YfgL and YfiO make direct but independent physical contacts with YaeT. Whereas
Drew Bennion et al.
Molecular microbiology, 77(5), 1153-1171 (2010-07-06)
BamA of Escherichia coli is an essential component of the hetero-oligomeric machinery that mediates β-barrel outer membrane protein (OMP) assembly. The C- and N-termini of BamA fold into trans-membrane β-barrel and five soluble POTRA domains respectively. Detailed characterization of BamA
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