Novex™ 18% Tris-Glycine Mini Protein Gels, 1.0 mm, 10-well
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货号 EC6505BOX
价格(CNY)
2,962.00
10 gels (1 box)
价格(CNY)
2,962.00
10 gels (1 box)
Novex® 18% Tris-Glycine Mini Gels are polyacrylamide gels based on traditional Laemmli protein electrophoresis. Novex® Tris-Glycine gels provide reproducible separation of a wide range of proteins into well-resolved bands. Each box contains 10 gels. Features of these gels:
• Individually packaged gels for optimal experiment design • Compatible with most protein standards • Usable for native and denaturing protein assays
Choose the right gel format for your experiments Novex® Tris-Glycine gels come in a variety of fixed concentrations from 4% to 18%, as well as gradients with ranges of 4–12%, 4–20%, 8–16%, and 10–20%. You can also select between our mini (8 cm x 8 cm) and our midi (8 cm x 13 cm) sizes, as well as multiple well-formats from 1 well to 26 wells.
Dexamethasone alters arachidonate release from human epithelial cells by induction of p11 protein synthesis and inhibition of phospholipase A2 activity.
Authors:Yao XL, Cowan MJ, Gladwin MT, Lawrence MM, Angus CW, Shelhamer JH,
Journal:J Biol Chem
PubMed ID:10358078
The effect of the glucocorticosteroid, dexamethasone, on arachidonic acid (AA) release and on protein levels of p11 and cytosolic phospholipase A2 (cPLA2) was studied in two epithelial cell lines, HeLa cells and BEAS-2B cells. Dexamethasone treatment of HeLa cells and BEAS-2B cells increased cellular p11 protein and mRNA levels in ... More
Receptor recognition and specificity of interleukin-8 is determined by residues that cluster near a surface-accessible hydrophobic pocket.
To determine the regions of interleukin-8 (IL-8) that allow high affinity and interleukin-8 receptor type 1 (IL8R1)-specific binding of chemokines, we produced chimeric proteins containing structural domains from IL-8, which binds to both IL8R1 and interleukin-8 receptor type 2 (IL8R2) with high affinity, and from GRO gamma, which does not ... More
The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1.
We have identified a novel generally expressed homologue of the erythrocyte membrane cytoskeletal protein 4.1, named 4.1G, based on the interaction of its COOH-terminal domain (CTD) with the immunophilin FKBP13. The 129-amino acid peptide, designated 4.1G-CTD, is the first known physiologic binding target of FKBP13. FKBP13 is a 13-kD protein ... More