|Calculated MW||45626 Da|
|Application & Usage||Western blotting (1:500 – 1:2500). However, the optimal concentrations should be determined individually. HeLa and NIH3T3 cell lysates can be used as positive controls. The antibody recognizes the TRIP1(S µg1) of human and mouse origins. Reactivity to other species has not been tested.|
|Other Names||TRIP1, TRIP-1, Thyroid Receptor Interactor 1, TBP10, Tat-binding protein homolog 10, PSMC5, Proteasome (prosome, macropain) 26S Subunit, ATPase, 5, p45, p45/S µg, S µg1, S8|
|Formulation||100 µl affinity purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 30% glycerol, 1% BSA and 0.02% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||TRIP1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.|
|Cellular Location||Cytoplasm. Nucleus|
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Provided below are standard protocols that you may find useful for product applications.
Thyroid receptor interacting protein 1 (TRIP1) was originally identified as a protein that interacts with the thyroid receptor and is homologous to the yeast SUG1 protein, a transcriptional coactivator. It was later identified as an ATPase subunit of the 26S proteasome, a multicatalytic proteinase complex, and has also been shown to associate with nuclear receptors and transcription factors. TRIP1/SUG1 may function to regulate transcription factor abundance by targeting them for proteasome degradation.
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