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Key Documents

P4505

Sigma-Aldrich

Protamine sulfate

powder

Synonyme(s) :

Clupeine

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About This Item

Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

product name

Protamine sulfate salt from herring, Grade III, histone, free(Millon test)

Source biologique

fish (herring)

Type

Grade III

Forme

powder

Impuretés

histone, free (Millon test)

Solubilité

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.

Actions biochimiques/physiologiques

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Les clients ont également consulté

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L T Hansen et al.
International journal of food microbiology, 66(3), 149-161 (2001-06-29)
The antimicrobial effect of protamine (clupeine) on a range of gram-positive and gram-negative foodborne pathogens and spoilage bacteria, was evaluated using an agar dilution assay and a broth dilution assay with Alamar Blue as growth indicator. Protamine was tested alone
L Willmitzer et al.
Biophysics of structure and mechanism, 6(2), 95-110 (1980-01-01)
The thermodynamics of protamine-DNA interation was investigated with clupeine Z from herring labeled at its amino terminus with fluorescein. The ionic strength dependence, the influence of protamine phosphorylation, of the native DNA conformation, using native and heat-denatured DNA, and of
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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