PSMA7 Mouse anti-Human, Clone: OTI2A7, Invitrogen
Mouse Monoclonal Antibody
Manufacturer: Invitrogen MA524993
DescriptionComponent of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintece of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation.
|PBS with 1% BSA, 50% glycerol and 0.02% sodium azide; pH 7.3|
|RP5-1005F21.4, C6, HSPC, RC6-1, XAPC7, proteasome subunit RC6-1, proteasome subunit XAPC7, proteasome subunit alpha 4, proteasome subunit alpha type-7|
|-20° C, Avoid Freeze/Thaw Cycles|
|Full-length protein expressed in 293T cell transfected with human PSMA7 expression vector|
We continue to work to improve your shopping experience and your feedback regarding this content is very important to us. Please use the form below to provide feedback related to the content on this product.
Your feedback has been submitted. Fisher Scientific is always working to improve our content for you. We appreciate your feedback.Ok