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5127 Sigma-Aldrich

CD270 human

recombinant, expressed in E. coli, 0.5 mg protein/mL

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Properties

Related Categories Attachment Factors, CD160 to CD340, Cell Biology, Cell Culture, Cell Signaling and Neuroscience,
biological source   human
recombinant   expressed in E. coli
description   0.1 mg recombinant human CD270 in 20 mM Tris-HCl buffer, containing NaCl, KCl, EDTA, L-arginine, DTT and glycerol.
sterility   Filtered sterilized solution
assay   ≥90% (SDS-PAGE)
form   liquid
packaging   pkg of 100 μg
concentration   0.5 mg protein/mL
accession no.   NP_003811.2
UniProt accession no.   Q92956
storage temp.   −20°C
Gene Information   human ... TNFRSF14(8764)

Description

Application

Coating a plate well (6 well plate) with this recombinant CD270 protein in a specific culture medium at 5-10 μg/well allows for use 1) as a coating matrix protein for human T or B cell functions and differentiation regulation studies in vitro, 2) as potential biomarker protein for infectious diseases and auto-immuno disease diagnostic development, or 3) as an antigen for specific antibody production.

Use this procedure as a guideline to determine optimal coating conditions for the culture system of choice.
1. Thaw CD270 and dilute to desired concentration using serum-free medium or PBS. The final solution should be sufficiently dilute so the volume added covers the surface evenly (1-10 μg/well, 6 well plate).
2. Add appropriate amount of diluted material to culture surface.
3. Incubate at room temperature for approximately 1.5 hours.
4. Aspirate remaining material.
5. Rinse plates carefully with water and avoid scratching bottom surface of plates.
6. Plates are ready for use. They may also be stored at 2-8 °C damp or air dried if sterility is maintained.

Sequence

MASMTGGQQMGRGHHHHHHGNLYFQG^GEFLPSCKEDEYPVGSECCPKCSPGYRVKEACGELTGTVCEPCPPGTYIAHLNGLSKCLQCQMCDPAMGLRASRNCSRTENAVCGCSPGHFCIVQDGDHCAACRAYATSSPGQRVQKGGTESQDTLCQNCPPGTFSPNGTLEECQHQTKCSWLVTKAGAGTSSSHWV

Preparation Note

The extracellular domain of recombinant human CD270 (39 - 202 aa) was constructed with codon optimization and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal and expressed in E. coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
2

Documents

Certificate of Analysis

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Peer-Reviewed Papers
15

References

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