Name :
Recombinant Human Protein disulfide-isomerase/PDI Protein (His Tag)
Biological Activity :
Background :
Protein disulfide-isomerase, also known as Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55 and P4HB, is a peripheral membrane protein that belongs to the protein disulfide isomerase family. P4HB is highly abundant. In some cell types, it seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. P4HB localizes near CD4-enriched regions on lymphoid cell surfaces. It is identified by mass spectrometry in melanosome fractions from stage I to stage IV. P4HB reduces and may activate fusogenic properties of HIV-1 gp12 surface protein, thereby enabling HIV-1 entry into the cell. P4HB catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, it seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. P4HB may therefore cause structural modifications of exofacial proteins. Inside the cell, it seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, P4HB functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, it facilitates aggregation (anti-chaperone activity). P4HB may be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. It also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.
Biological Activity :
Measured by its ability to promote aggregation of insulin in the presence of DTT. The specific activity is > 7.5 A650/min/mg
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
NP_000909.2
NCBI Gene ID :
Synonyms :
Synonyms :
prolyl 4-hydroxylase, beta polypeptide
Amino Acid Sequence :
Molecular Weight :
The recombinant human PH4B consists of 499 amino acids and has a predicted molecular mass of 56.4 kDa. In SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 60 kDa due to glycosylation.
Purity :
> 95 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the human PH4B (NP_000909.2) corresponding to amino acid (Met 1-Lys 505) was expressed with a C-terminal polyhistidine tag.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
DSI Protein, Human; ERBA2L Protein, Human; GIT Protein, Human; P4Hbeta Protein, Human; PDI Protein, Human; PDIA1 Protein, Human; PHDB Protein, Human; PO4DB Protein, Human; PO4HB Protein, Human; PROHB Protein, Human Protein disulfide-isomerase/PDI 背景信息 Protein disulfide-isomerase, also known as Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55 and P4HB, is a peripheral membrane protein that belongs to the protein disulfide isomerase family. P4HB is highly abundant. In some cell types, it seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. P4HB localizes near CD4-enriched regions on lymphoid cell surfaces. It is identified by mass spectrometry in melanosome fractions from stage I to stage IV. P4HB reduces and may activate fusogenic properties of HIV-1 gp12 surface protein, thereby enabling HIV-1 entry into the cell. P4HB catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, it seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. P4HB may therefore cause structural modifications of exofacial proteins. Inside the cell, it seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, P4HB functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, it facilitates aggregation (anti-chaperone activity). P4HB may be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. It also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.
References & Citations :
Kivirikko KI, et al., 1989, FASEB J., 3 (5): 1609-17. Pihlajaniemi T, et al.,1991, J Hepatol., 13, Suppl 3: S2 Fenouillet E., et al., 2001, J. Infect. Dis. 183:744-752. Gevaert K., et al., 2003, Nat. Biotechnol. 21:566-569. Barbouche R., et al., 2003, J. Biol. Chem. 278:3131-3136.
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