|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.|
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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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