Kinesis Needle Seal; Shimadzu SIL-10ADvp; SIL-10AXL - EACH
282.90 €
In Stock
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product details
Catalog number: 10333 - CHR6266
Product Category: Business & Industrial > Science & Laboratory
Gentaur
Size: EACH
A04956-1
Anti-STIL/SIL Antibody Picoband™
Western blot, 0.25-0.5μg/ml, Human, Mouse, Rat;_x000D_Immunohistochemistry (Paraffin-embedded Section), 2-5μg/ml, Human;_x000D_Flow Cytometry, 1-3μg/1x10<sup>6</sup> cells, Human;_x000D_Direct ELISA, 0.1-0.5μg/ml, Human
384.81 €
40-668
sIL-2 Receptor a Recombinant Protein
The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Rα, IL-2Rβ, and IL-2Rγ. The IL-2Rα is a type I transmembrane protein consisting of a 219 amino acid extracellular domain, a 19 amino acid transmembrane domain and a 13 amino acid intracellular domain, which is not involved in the transduction of IL-2 signals. Proteolytic processing of IL-2Rα releases the entire extracellular domain of IL-2Rα, thereby generating a 219 amino acid soluble protein called soluble IL-2Rα (sIL-2Rα). The homodimeric form binds IL-2 (KD=10mM) and facilitates IL-2 signaling. The secreted sIL-2Rα is expressed on leukemia cells, lymphoma cells, and newly activated T and B cells, as well as on approximately 10% of NK cells. Recombinant Human sIL-2Rα is a 24.8 kDa protein containing 219 amino acid residues consisting of only the extracellular domain of IL-2Rα. Due to glycosylation, IL-2Rα has an approximate molecular weight of 31 kDa based on SDS-PAGE gel and Mass Spectrometry.
602.62 €
40-670
sIL-4 Receptor alpha Recombinant Protein
IL-4 can signal through type I and type II receptor complexes, which share a common gamma chain (γc). The type I receptor contains, in addition to the γc, an IL-4Rα subunit, whereas the type II receptor contains the IL-13Rα. The secreted extracellular domain of IL-4Rα, called sIL-4Rα, binds IL-4 and antagonizes its activity. It plays an important role in regulating the differentiation of naïve CD4+ T cells and class switching to IgG1 and IgE. CHO cell-derived Recombinant Human sIL-4 Receptor α is a 23.9 kDa glycoprotein corresponding to 209 amino acid residues of the extracellular domain of IL-4Rα. As a result of glycosylation, Recombinant Human sIL-4 Receptor α migrates with an apparent molecular mass of approximately 50-65 kDa by SDS-PAGE gel, under reducing conditions.