Anti-P4HB Antibody (Mouse Monoclonal antibody) General Information
Reacts with: Human
Recombinant Human P4HB protein (Catalog#10827-H08H)
This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human P4HB (rh P4HB; Catalog#10827-H08H; NP_000909.2; Met 1-Lys 505). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
Monoclonal Mouse IgG1 Clone #03
0.2 μm filtered solution in PBS with 5% trehalose
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
Immunofluorescence staining of Human P4HB in Hela cells. Cells were fixed with 4% PFA, permeabilzed with 1% Triton X-100 in PBS, blocked with 10% serum, and incubated with Mouse anti-Human P4HB monoclonal antibody (1:60) at 37℃ 1 hour. Then cells were stained with the Alexa Fluor®488-conjugated Goat Anti-mouse IgG secondary antibody (green) and counterstained with DAPI (blue). Positive staining was localized to endoplasmic reticulum.
Human P4HB (PDI) expression in HeLa cells. The cells were treated according to manufacturer’s manual (BD Pharmingen™ Cat. No. 554714), and stained with Purified Mouse anti-P4HB (PDI) (10827-MM03), then a FITC-conjugated second step antibody. The fluorescence histograms were derived from gated events with the forward and side light-scatter characteristics of intact cells.
Protein disulfide-isomerase, also known as Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55 and P4HB, is a peripheral membrane protein which 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 a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.