Anti-Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) Antibody
Our Anti-Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) chicken polyclonal primary antibody detects cat, human, mouse, other mammals (predicted), and rat Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1), and is IgY preparation. It is validated for use in ICC, IHC-Frozen, IHC-Paraffin-embedded, WB.
HeLa cells stained with Chicken polyclonal antibody to Peptidylprolyl isomerase (1:1,000 dilution, green) and Mouse monoclonal antibody to Fibrillarin (Nop1p) M-1372-250 (red). Peptidylprolyl isomerase (Pin-1) stains the nuclear matrix and, much more faintly, the cytoplasm. The fibrillarin antibody marks nucleoli.
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SKU: C-1398-50
Ships: 5-7 business days
Product Details
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1)
The enzyme Peptidylprolyl isomerase (Pin1) is responsible for flipping the proline ring from the cis to trans conformation. This enzyme regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity (ref: SWISSPROT). Pin1 is concentrated in the nucleus in small punctate structures and is particularly obvious in tumor cells.
IgY preparation
Polyclonal
IgY
ICC, IHC, WB
Chicken
21 kDa
Recombinant full length Peptidylprolyl isomerase (Pin1) purified from E.coli
Human
Feline, Human, Mouse, Rat
Spin vial briefly before opening. Reconstitute with 50 µL sterile-filtered, ultrapure water. Centrifuge to remove any insoluble material. After reconstitution of lyophilized antibody, aliquot and store at -20°C for a higher stability. Avoid freeze-thaw cycles.
Lyophilized
Lyophilized IgY preparation, with sodium azide.
WB: 1:5000-1:10000
ICC: 1:500-1:1000
ICC: 1:500-1:1000
Unconjugated
The specificity of this antibody has been confirmed by WB. This antibody detects ~21 kDa Pin1 protein. Human, rat, mouse and feine. Predicted to react with other mammalian tissue.
For research use only.
United States
12 months after date of receipt (unopened vial).
DOD; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; PPIase Pin1; Peptidyl-prolyl cis-trans isomerase Pin1; rotamase Pin1; PPIase Pin-1; PIN1
Q13526
UniProt Summary: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN. May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells. Catalyzes cis-trans isomerization of phosphorylated phosphoglycerate kinase PGK1 under hypoxic conditions to promote its binding to the TOM complex and targeting to the mitochondrion. Acts as a negative regulator of adipocyte browning by binding to phosphorylated PRDM16, targeting PRDM16 for degradation.
UniProt Summary: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN. May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells. Catalyzes cis-trans isomerization of phosphorylated phosphoglycerate kinase PGK1 under hypoxic conditions to promote its binding to the TOM complex and targeting to the mitochondrion. Acts as a negative regulator of adipocyte browning by binding to phosphorylated PRDM16, targeting PRDM16 for degradation.
5300
25°C (ambient)

