P4505
Protamine sulfate salt from herring
Grade III, histone, free(Millon test)
Synonym(s):
Clupeine
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About This Item
biological source
fish (herring)
Quality Level
type
Grade III
form
powder
impurities
histone, free (Millon test)
solubility
6 M HCl: 25 mg/mL, clear, colorless to very faintly yellow
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Application
May be used for the removal of DNA from protein samples or for the purification of DNA binding proteins. It may be used as an alternative to polybrene in retroviral-mediated gene transfer.
Biochem/physiol Actions
Protamine in the form of solid lipid nanoparticles (SLN) promoted transfection with plasmid DNA more efficiently and with less cytotoxicity than comparable SLNs composed of Esterquat-1.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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I Saiki et al.
Japanese journal of cancer research : Gann, 81(6-7), 668-675 (1990-06-01)
We have investigated the anti-angiogenic effect of a polymeric peptide based on the Arg-Gly-Asp (RGD) core sequence of fibronectin as a monomer unit, i.e., poly(RGD), in syngeneic mice and in vitro. Single intratumoral administration of poly(RGD) on day 0, 1
C Toniolo et al.
Biochimica et biophysica acta, 576(2), 429-439 (1979-02-26)
The three main components YI, YII, and Z of clupeine, a protamine from herring, have been purified and characterized. The conformational preferences of clupeines have been examined as a funciton of pH, temperature, added salts, and presence of structure-disrupting agents
Moyra Lawrence et al.
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L Ferrara et al.
European journal of biochemistry, 126(2), 389-394 (1982-08-01)
The three main fractions of clupeine, the protamine extracted from herring sperm, have been investigated by 13C nuclear magnetic resonance techniques. The dynamic behaviour, examined through the evaluation of the spin lattice relaxation times (T1) of individual carbon resonances assigned
N Navaratnam et al.
European journal of biochemistry, 171(3), 623-629 (1988-02-01)
Galactosyltransferase was purified from Golgi membranes of lactating-rat mammary gland and studied with respect to its physical and enzymic (lactose synthetase) properties. The enzyme occurred in both monomeric (43-46 kDa) and apparently dimeric (90 kDa) forms. It was very unstable
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