85881
Streptavidin, immobilized on Agarose CL-4B
suitable for affinity chromatography
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About This Item
UNSPSC Code:
12190000
NACRES:
NA.21
Recommended Products
form
suspension
Quality Level
contains
0.02% NaN3 as preservative
technique(s)
affinity chromatography: suitable
capacity
≥15 μg/mL, packed gel capacity (biotin)
storage temp.
2-8°C
General description
streptavidin attached to 4% beaded cross-linked agarose via a C6-spacer (1.2 mg streptavidin/ml packed gel)
Physical form
50% suspension in 0.01 M sodium phosphate buffer, pH 7.2, containing 0.15 M sodium chloride
Other Notes
Isolation of cell surface glycoprotein by biotinylated concanavalin A and immobilized streptavidin.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Yahui Huang et al.
Clinical & experimental metastasis, 37(4), 477-487 (2020-07-03)
MACC1 (metastasis associated in colon cancer 1) is a key driver that induces metastasis in colon cancer. However, the mechanisms by which MACC1 expression is transcriptionally regulated and the factors enriched at the MACC1 promoter remain largely unknown. The binding
J W Buckie et al.
Analytical biochemistry, 156(2), 463-472 (1986-08-01)
An indirect affinity chromatography procedure utilizing biotinylated lectins and designed for the specific isolation of surface glycoproteins is described. The method is illustrated with intact acute leukemic lymphoblastic cells (ALL cells) with biotin-epsilon-aminocaproyl-concanavalin A (biocap-Con A) and streptavidin-Sepharose 4B. Biocap-Con
Jilian Su et al.
Molecular and cellular probes, 46, 101415-101415 (2019-06-23)
Vascular endothelial growth factor (VEGF) can promote cell division, proliferation and migration. In this study, we aimed to investigate roles of ultrasound-mediated destruction of VEGF-targeted and paclitaxel (PTX)-loaded lipid microbubbles (VTPLLM + US) in human breast cancer cells. The activity of MCF-7 cells
Romina B Cejas et al.
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Glycosylation is a very frequent post-translational modification in proteins, and the initiation of O-N-acetylgalactosamine (O-GalNAc) glycosylation has been recently described on relevant nuclear proteins. Here we evaluated the nuclear incorporation of a second sugar residue in the biosynthesis pathway of
Yen-Jung Chen et al.
Antioxidants & redox signaling, 31(2), 109-126 (2018-11-13)
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