|IP||1-4 μL/mg of lysate|
**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********
Mouse P4HB was immunoprecipitated using:
Lane A:0.5 mg 293T Whole Cell Lysate2 µL anti-Mouse P4HB rabbit polyclonal antibody and 15 μl of 50 % Protein G agarose.Primary antibody:
Anti-Mouse P4HB rabbit polyclonal antibody,at 1:200 dilutionSecondary antibody:
Clean-Blotô IP Detection Reagent (HRP) at 1:1000 dilutionDeveloped using the DAB staining technique.
Performed under reducing conditions.Predicted band size: 57 kDa
Observed band size: 57 kDa
Anti-P4HB rabbit polyclonal antibody at 1:500 dilution
Lane A: HepG2 Whole Cell Lysate
Lane B: 293T Whole Cell LysateLysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique.
Performed under reducing conditions.Predicted band size:57 kDa
Observed band size:55 kDa
(We are unsure as to the identity of these extra bands.)
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 gp120 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.
|Product Description||Host||Clonality||Application||Catalog# (PDF)|
|Anti-P4HB Antibody (FITC)||Rabbit||Monoclonal||FCM||10827-R016-F|
|Anti-P4HB Antibody (FITC)||Mouse||Monoclonal||FCM||10827-MM03-F|