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P4HB protein (Active)
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Recombinant Full-length Human P4HB (SwissProt ID P07237) with an N-terminal 6xHis-tag is a single, non-glycosylated, polypeptide chain containing 508 amino acids and having a molecular mass of 57 kDa.
E. coli
>95% by 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.
Reductase 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). Isomerase Activity: 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).
Lyophilised:
Reconstitute in sterile 18Mohm/cm water at not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Preservative: None
Constituents: 50mM Potassium phosphate, pH 7.5
Concentration information loading...
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Ar g-Arg-Ala.
Our Abpromise guarantee covers the use of ab73280 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Enzyme Assays:
Reductase Activity: Use at an assay dependent dilution.
Isomerase Activity: Use at an assay dependent dilution.
SDS-PAGE: Use at an assay dependent dilution.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
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.
Belongs to the protein disulfide isomerase family.
Contains 2 thioredoxin domains.
Endoplasmic 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.
Target information above from: UniProt accessionP07237
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
ab73280 has not yet been referenced specifically in any publications.
Publishing research using ab73280? Please let us know so that we can cite the reference in this datasheet
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