Human 4-1BB Ligand Recombinant Protein LyophilizedIHU41BBLGRLY5UG
Human 4-1BB Ligand Recombinant Protein Lyophilized from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in with a purity of Greater than 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per and#956;g (1EU/and#956;g)..
- Species: Human
- Target: TNFSF9
Purity: Greater than 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per and#956;g (1EU/and#956;g).
- Source: E. coli
- Storage Conditions: The lyophilized 4-1BB Ligand recombinant protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted 4-1BB Ligand is stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. As with any protein, exposing 4-1BB Ligand recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.
4-1BBL, a member of the TNF superfamily, is expressed in B cells, dendritic cells, activated T cells and macrophages. 4-1BBL binds to its receptor 4-1BB, and provides a co-stimulatory signal for T cell activation and expansion. The human 4-1BBL gene codes for a 254 amino acid type II transmembrane containing a 28 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 205 amino acid extracellular domain. The soluble form of 4-1BBL contains the TNF-like portion of the extracellular domain of 4-1BBL. Recombinant human 4-1BBL is a soluble 19.5 kDa protein consisting of 185 amino acid residues.
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This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.
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