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The Anti-TNF-α Protein A Scaffold molecule was selected against human TNF-α. The Anti-TNF-α Protein A Scaffold molecule is an ideal affinity ligand as a capture reagent in ELISA and as detection reagent in dot blot. The Anti-TNF-α Protein A Scaffold molecule is modified with a unique C-terminal cysteine for directed single-point chemical modification, facilitating labeling with fluorescent dyes, biotin or coupling to matrices.
Suitable as capture reagent in ELISA and as detection reagent in dot blot.
Anti-TNF-α Protein A scaffold molecule binds to human cytokine tumor necrosis factor α, TNF-α. Cross reactivity with other species has not been tested.
At +4°C is recommended for lyophilized protein. For reconstituted protein in physiological buffer, short-term storage at +4°C is recommended. For long-term storage, the protein solution should be aliquoted and then stored at -20°C. There is no decrease in
Human TNF-α (Tumour Necrosis Factor-alpha) is a nonglycosylated protein of 17 kD belonging to the TNF superfamily of cytokines. TNF-α is produced by activated macrophages and Tlymphocyte and forms trimers spontaneously. TNF-α shows a wide spectrum of biological activities that are mediated by binding to TNFRI and TNFRII receptors. Besides causing cytolysis and cytostasis of many tumour cell lines in vitro, TNF-α has an important role in host defences against pathogens. However, excess TNF-α seen in sepsis and diseases of autoimmune character, has severe pathological consequences and the neutralisation of TNF-α has been a successful treatment procedure for rheumatoid arthritis.
cytokine activity; identical protein binding; protease binding; protein binding; transcription regulatory region DNA binding; tumor necrosis factor receptor binding