Enzyme

P4HB

PDI, Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55

Homo sapiens (Human)

Partial

3034602; 3611107; 2846539; 14702039; 15489334; 1597478; 9150948; 12665801; 2079031; 1286669; 9399589; 3342239; 1699755; 10636893; 11181151; 12485997; 12095988; 12218051; 12218052; 12643545; 15158710; 14592831; 15644496; 17081065; 21269460; 24275569; 25683117; 8580850; 8672469; 10383197;

56.6 kDa

N-terminal 6xHis-tagged

E.Coli

>95% as determined by SDS-PAGE and HPLC.

0.2 μm filtered PBS, pH 7.0 ,lyophilized

Less than 1.0 EU/μg as determined by LAL method.

Thiol Protein Reductase Activity is 0.001 Δ650nm/ min-2, determined by measuring the turbidity
increase at 650 nm due to insulin reduction.The activity is expressed as the ratio of the slope of a
linear part of the turbidity curve to the lag time.

PDIA1_HUMAN

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997}.

MRGSGSHHHH HH+APEEEDHV LVLRKSNFAE ALAAHKYLLV EFYAPWCGHC KALAPEYAKA AGKLKAEGSE IRLAKVDATE ESDLAQQYGV RGYPTIKFFR NGDTASPKEY TAGREADDIV NWLKKRTGPA ATTLPDGAAA ESLVESSEVA VIGFFKDVES DSAKQFLQAA EAIDDIPFGI TSNSDVFSKY QLDKDGVVLF KKFDEGRNNF EGEVTKENLL DFIKHNQLPL VIEFTEQTAP KIFGGEIKTH ILLFLPKSVS DYDGKLSNFK TAAESFKGKI LFIFIDSDHT DNQRILEFFG LKKEECPAVR LITLEEEMTK YKPESEELTA ERITEFCHRF LEGKIKPHLM SQELPEDWDK QPVKVLVGKN FEDVAFDEKK NVFVEFYAPW CGHCKQLAPI WDKLGETYKD HENIVIAKMD STANEVEAVK VHSFPTLKFF PASADRTVID

19-456aa

Signal Transduction