Background
IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B-cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6R α and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant human IL-6 is a 20.9 kDa protein containing 184 amino acid residues.
Specifications
Additional Names
26 kDa protein, IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2
Preparation
The ED50 was determined by the dose - dependent stimulation of the proliferation of IL - 6 dependent murine 7TD1 cells is ? 0.1 ng/ml, corresponding to a specific activity of ? 1 x 107units/mg.
Location
PVPPGEDSKD VAAPHRQPLT SSERIDKQIR YILDGISALR KETCNKSNMC ESSKEALAEN NLNLPKMAEK DGCFQSGFNE ETCLVKIITG LLEFEVYLEY LQNRFESSEE QARAVQMSTK VLIQFLQKKA KNLDAITTPD PTTNASLLTK LQAQNQWLQD MTTHLILRSF KEFLQSSLRA LRQM
Source
E. coli
Reactivity
n/a
Tested Application
n/a
Storage
The lyophilized IL-6 recombinant protein is stable for at least 2 years from date of receipt at -20ËšC. Reconstituted IL-6 is stable for at least 3 months when stored in working aliquots with a carrier protein at -20ËšC. As with any protein, exposing IL-6 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.
Species Reactivity
n/a
Purity
Greater than 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per μg (1EU/μg).
