SequenceThe sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Arg-Arg-Ala.
TagsHis tag N-Terminus
Additional sequence informationPDI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids. The PDI is fused to a 12 amino acid His tag (515 a.a. total) at N-terminal.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Biological activityReductase Activity:
1.0 x 10-3 OD650nm/ min-2. By measuring the turbidity increase at 650 nm due to insulin reduction (Holmgren, A. (1979) J. Biol. Chem. 254, 9627–9632). The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time (Mart´nez-Galisteo, E., Padilla, C. A., Garcia-Alfonso, C., Lo´pez-Barea, J. and Barcena, J. A. (1993) Biochimie (Paris) 75, 803–809).
0.5 µmol active RNase A min-1 µmol P4HB-1. According to the re-activation of reduced and denatured RNase A (Lyles, M. M. and Gilbert, H. F. (1991) Biochemistry 30, 613-619).
% SDS-PAGE. This protein was purified by proprietary chromatographic techniques.
Purity greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Additional notesFor long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
pH: 7.50 Constituent: PBS
This product is an active protein and may elicit a biological response in vivo, handle with caution.
ReconstitutionReconstitute in sterile 18Mohm/cm water at not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
V erb a avian erythroblastic leukemia viral oncogene homolog 2 like
FunctionThis 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.
Sequence similaritiesBelongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.
Cellular localizationEndoplasmic reticulum lumen. Melanosome. Cell membrane. Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.