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Merck
CN

P4530

Protamine-Agarose

saline suspension

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About This Item

UNSPSC Code:
41106500
MDL number:
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form

saline suspension

matrix

Cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

amino

matrix spacer

1 atom

capacity

~50 μg/mL binding capacity (DNA)

storage temp.

2-8°C

Application

Protamine-agarose is used in protein chromatography, affinity chromatography and specialty resins. Protamine-agarose has been used to determine that Pichia pastoris (methylotrophic yeast) provides a convenient heterologous system for the production of recombinant subunits of human type 2A protein phosphatase (PP2A). Protamine-agarose has also been used to purify and characterize a novel protamine kinase in HL60 cells as well as to study myocardial infarction.

Physical form

Suspension in 0.5 M NaCl containing 0.02% thimerosal

Disclaimer

For U.S. Customers: Contains mercury; Do not place in trash - dispose according to local, state, or federal laws.

Storage Class

12 - Non Combustible Liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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I M Helander et al.
European journal of biochemistry, 163(1), 51-55 (1987-02-16)
The ability of agarose-linked protamine to bind Salmonella typhimurium lipopolysaccharides was investigated. Radioactively labelled lipopolysaccharides were isolated both from a smooth strain (SH6749, labelled with [14C]galactose) and from a rough strain (SH5014, lipopolysaccharide chemotype Rb2, labelled with [3H]acetate). From 50-micrograms
S Shibata et al.
Journal of biochemistry, 112(4), 552-556 (1992-10-01)
Calphobindins (CPBs, placental annexins) are intracellular Ca(2+)- and phospholipid-dependent proteins like protein kinase C [EC 2.7.1.37]. We investigated the inhibitory effects of calphobindins on the protein kinase C activity in vitro. CPB I inhibited the protein kinase C activity for
M Junco et al.
FEBS letters, 263(1), 169-171 (1990-04-09)
Protein kinase C (PKC) and its proteolysis-derived protein kinase independent of Ca2+ and phospholipids (PKM), were purified from rat brain. By using histone H1 and protamine as substrates, we assayed the effect of several inhibitors of PKC and PKM. The
S A Reddy et al.
The Journal of biological chemistry, 265(14), 7748-7752 (1990-05-15)
Treatment of isolated rat hepatocytes with 10-100 nM insulin for 5-10 min increased by about 2-fold the activity of a protamine kinase which exhibited properties similar to those of a protamine kinase from bovine kidney (Damuni, Z., Amick, G. D.
M W Wooten et al.
European journal of biochemistry, 164(2), 461-467 (1987-04-15)
We describe a rapid purification of protein kinase C from rat brain cytosol employing a specific substrate, protamine-coupled to agarose. Sequential chromatography on DEAE-Sephacel, phenyl-Sepharose CL-4B, and protamine-agarose columns resulted in a 1,500-fold purification of protein kinase C. SDS-PAGE analysis

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