S3762
Streptavidin−FITC from Streptomyces avidinii
essentially salt-free, lyophilized powder, ≥5 units/mg protein
Product Name
Streptavidin−FITC from Streptomyces avidinii, essentially salt-free, lyophilized powder, ≥5 units/mg protein
conjugate
FITC conjugate
form
essentially salt-free, lyophilized powder
specific activity
≥5 units/mg protein
extent of labeling
3-9 mol FITC per mol streptavidin
storage temp.
−20°C
Quality Level
Application
The optimal working dilution should be determined empirically using a range of dilutions from a 1 mg/ml stock in buffer.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Other Notes
One unit will bind 1 μg biotin.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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The motion of a single molecule, the lambda-receptor, in the bacterial outer membrane.
Oddershede L et al
Biophysical Journal, 83(6), 3152-3161 (2002)
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Thoeni G et al
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Weijia Li et al.
Journal of cellular physiology, 235(2), 1141-1154 (2019-07-28)
Ovarian cancer (OC) is a fatal cancer in women, mainly due to its aggressive nature and poor survival rate. The lncRNA-miRNA-mRNA (long noncoding RNA-microRNA-messenger RNA) interaction is promising biomarkers for the improving prognosis of OC. Therefore, we explored the regulatory
Anke P Willems et al.
Biochimica et biophysica acta. General subjects, 1863(10), 1471-1479 (2019-05-24)
Sialylation of glycoproteins and glycolipids is important for biological processes such as cellular communication, cell migration and protein function. Biosynthesis of CMP-sialic acid, the essential substrate, comprises five enzymatic steps, involving ManNAc and sialic acid and their phosphorylated forms as
Lene Oddershede et al.
Biophysical journal, 83(6), 3152-3161 (2002-12-24)
Using optical tweezers and single particle tracking, we have revealed the motion of a single protein, the lambda-receptor, in the outer membrane of living Escherichia coli bacteria. We genetically modified the lambda-receptor placing a biotin on an extracellular site of
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