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11032-88-5

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11032-88-5 Usage

Purification Methods

Colicin E1 is purified (8.6-fold to Specific Activity of 1.5 x 10units/mg) from E.coli JC411 by salt extraction of extracellular-bound colicin followed by (NH4)2SO4 (40-60% saturation) fractionation and ion-exchange chromatography on a DEAE-Sephadex A 50 column, and then by CM-Sephadex column chromatography [Schwartz & Helinski J Biol Chem 246 6318 1971].

Check Digit Verification of cas no

The CAS Registry Mumber 11032-88-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,1,0,3 and 2 respectively; the second part has 2 digits, 8 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 11032-88:
(7*1)+(6*1)+(5*0)+(4*3)+(3*2)+(2*8)+(1*8)=55
55 % 10 = 5
So 11032-88-5 is a valid CAS Registry Number.

11032-88-5Upstream product

11032-88-5Downstream Products

11032-88-5Related news

Histidine 440 controls the opening of COLICIN E1 (cas 11032-88-5) channels in a lipid-dependent manner08/19/2019

The in vitro activity of many pore-forming toxins, in particular, the rate of increase in the membrane conductance induced by the channel-forming domain (P178) of colicin E1 is maximum at an acidic pH. However, after P178 binding at acidic conditions, a subsequent pH shift from 4 to 6 on both si...detailed

Electrostatic interactions of COLICIN E1 (cas 11032-88-5) with the surface of Escherichia coli total lipid08/18/2019

The surface properties of colicin E1, a 522-amino acid protein, and its interaction with monolayers of Escherichia coli (E. coli) total lipid and 1,2-Dimyristoyl-sn-Glycero-3-Phosphocholine (DOPC) were studied using the Langmuir–Blodgett (LB) technique. Colicin E1 is amphiphilic, forming a prot...detailed

Resolving the 3D spatial orientation of helix I in the closed state of the COLICIN E1 (cas 11032-88-5) channel domain by FRET. Insights into the integration mechanism08/16/2019

Current evidence suggests that the closed-state membrane model for the channel-forming domain of colicin E1 involves eight amphipathic α-helices (helices I–VII and X) that adopt a two-dimensional arrangement on the membrane surface. Two central hydrophobic α-helices in colicin E1 (VIII and IX...detailed

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