Search
Search
Invitrogen
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.promotions']}}
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.viewpromo']}}
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.promocode']}}: {{promo.promoCode}} {{promo.promoTitle}} {{promo.promoDescription}}. {{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.learnmore']}}
Immunogen sequence: PESEELTAER ITEFCHRFLE GKIKPHLMSQ ELPEDWDKQP VKVLVGKNFE DVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE NIVIAKMDST ANEVEAVKVH SFPTLKFFPA SADRTVIDYN GERTLDGFKK FLESGGQDGA GDDDDLEDLE EAEEPDMEED DDQKAVKDEL; Positive Samples: THP-1, SW620, CEM, NIH/3T3, RAW264.7, Mouse liver, Mouse kidney; Cellular Location: Cell membrane, Endoplasmic reticulum, Endoplasmic reticulum lumen, Melanosome, Peripheral membrane protein
Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, the protein seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. It may therefore cause structural modifications of exofacial proteins. Inside the cell, PDI seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, it functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, it facilitates aggregation (anti-chaperone activity). PDI may be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. It also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
仅用于科研。不用于诊断过程。未经明确授权不得转售。