The TXNDC11 Polyclonal Antibody (PAC037078) is a valuable tool for researchers studying the TXNDC11 protein, which is involved in oxidative stress response and protein folding processes. This antibody, produced in rabbits, shows high specificity for human samples and has been verified for use in Western blot experiments. By binding to TXNDC11, the antibody enables precise detection and examination of the protein across different cell types, making it a useful resource for investigations in fields such as biochemistry and physiology.TXNDC11, also known as thioredoxin domain containing 11, is crucial for maintaining cellular redox balance and ensuring proper protein function.
Its role in responding to oxidative stress and facilitating correct protein folding makes it a target of interest for researchers studying conditions such as neurodegenerative diseases, cardiovascular disorders, and metabolic syndromes. Unraveling the mechanisms of TXNDC11 can provide insights into disease pathogenesis and potentially lead to the development of innovative therapeutic strategies.
Immunohistochemistry of paraffin-embedded human small intestine tissue using PACO37078 at dilution of 1:100.
Immunofluorescent analysis of HepG2 cells using PACO37078 at dilution of 1:100 and Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
Immunohistochemistry of paraffin-embedded human lung cancer using PACO37078 at dilution of 1:100.
Background:
May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation.
Synonyms:
Thioredoxin domain-containing protein 11 (EF-hand-binding protein 1), TXNDC11, EFP1
UniProt Protein Function:
May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H2O2 generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H2O2 generation.
