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If you have any questions, you are always welcome to contact us. We'll get back to you as soon as possible, withing 24 hours on weekdays.
Customer service
All questions about your order, return and delivery must be sent to our customer service team by e-mail at yourstore@yourdomain.com
Sale & Press
If you are interested in selling our products, need more information about our brand or wish to make a collaboration, please contact us at press@yourdomain.com
Intracellular heat shock protein 70 (HSP70) belongs to the stress response system and can protect cells from different apoptotic stimuli. Extracellular HSP70 on the other hand can activate cells of the innate and adaptive immune system. Acute overexpression of intracellular HSP70 could even increase the susceptibility of melanoma cells to cytotoxic Tlymphocytes (CTLs) that use the granuleexocytosis pathway for killing (Dressel et al. 1999). To decipher the molecular pathway of this increased susceptibility to CTLs, the effect of the acute overexpression of HSP70 on gene expression was analysed in cells, in which Hsp70 is under the control of a tetracyclineinducible promoter. To reduce the complexity of CTLinduced apoptosis, further experiments were performed with granzyme (Gr)B, a component of the cytotoxic granules of CTLs and NK cells, that has been shown to interact with HSP70. Heparan sulphates on the other hand are involved in GrBbinding to target cells of CTLs and are modified in their sulphation pattern by sulphatases 1 and 2. The role of HSP70 and sulphatases 1 and 2 in GrBinduced apoptosis is analysed.
⚠️ WARNING (California Proposition 65):
This product may contain chemicals known to the State of California to cause cancer,
birth defects, or other reproductive harm.
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