|Application ||FC, IHC-P, WB, E|
|Other Accession||Q6DGG0, Q9CR16|
|Calculated MW||40764 Da|
|Antigen Region||85-115 aa|
|Other Names||Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, Rotamase D, PPID, CYP40, CYPD|
|Target/Specificity||This PPID antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 85-115 amino acids from the N-terminal region of human PPID.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PPID Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA- binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large- cell lymphoma (ALK+ ALCL) cell lines. May be involved in hepatitis C virus (HCV) replication and release.|
|Cellular Location||Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm|
|Tissue Location||Widely expressed.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Mayya V.,et.al., Sci. Signal. 2:RA46-RA46(2009).
Gevaert K., et.al., Nat. Biotechnol. 21:566-569(2003).
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