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Pierce 31000-NeutrAvidin Protein 原裝現(xiàn)貨

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  • 上海葉舟生物科技有限公司
  • 2022-06-20 14:55:24
  • 上海市
  • Pierce
  • 647

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產(chǎn)品名稱:NeutrAvidin Protein
貨號(hào):Pierce 31000
規(guī)格:10 MG

【詳細(xì)說(shuō)明】

產(chǎn)品名稱:NeutrAvidin Protein
貨號(hào):Pierce 31000
規(guī)格:10 MG
Thermo Scientific NeutrAvidin Protein is a specially-prepared form of avidin biotin-binding protein that decreases background in Western blotting and ELISA; available items include standard HRP, AP and fluorescent conjugates for biotin-based assays.
NeutrAvidin Protein is deglycosylated native avidin from egg whites. Removal of the excess carbohydrate by an exclusive process yields a protein with a more neutral isoelectric point and less nonspecific binding properties. Purified and conjugated forms of NeutrAvidin Protein provide exceptional performance in Western blot, ELISA and IHC applications that require biotin-binding probes. Assay specificity, sensitivity, and signal-to-noise ratios with NeutrAvidin Protein are generally equivalent or better than with the significantly more expensive streptavidin.
Highlights:
Near-neutral isoelectric point – pI = 6.3, more neutral than native avidin
Nearly devoid of glycosylation – decreased possibility of lectin binding compared to native avidin
No RYD recognition sequence – no known off-target binding domains like streptavidin
Affordable – significantly less expensive than streptavidin
Available in multiple formats – choose purified NeutrAvidin Protein, prepared HRP and AP conjugates or activated forms for a variety of techniques.
Product Details:
Avidin is a glycoprotein found in the egg white and tissues of birds, reptiles and amphibia. The biotin-binding protein contains four identical subunits having a combined mass of 67,000-68,000 daltons. Removing the glycosylation from avidin yields NeutrAvidin Protein with a mass of 60,000 daltons. Carbohydrate-based lectin-binding is reduced to undetectable levels, yet biotin-binding affinity is retained. NeutrAvidin Protein offers the advantages of a neutral pI to minimize nonspecific adsorption, along with lysine residues that remain available for derivatization or other customized conjugation. NeutrAvidin Protein yields the lowest nonspecific binding among the known biotin binding proteins. The specific activity for biotin-binding is approximay 14µg/mg of protein, which is near the theoretical maximum activity.
 

    
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