Anti-Pin1 Antibody Picoband®

Overview

This antibody is intended for detection of PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.

Vendor notes: Boster Bio Anti-Pin1 Antibody Picoband® catalog # PB9316. Tested in Flow Cytometry, ICC/IF, IHC, WB applications. This antibody reacts with Human, Monkey, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Key elements and design rationale

• Antibody format: Rabbit Polyclonal Rabbit IgG
• Immunogen / epitope context: E.coli-derived human Pin1 recombinant protein (Position: M1-E163). Human Pin1 shares 95% amino acid (aa) sequence identity with mouse Pin1. (reported region: M1-E163).
• Molecular weight context: reported MW: 18 kDa; calculated MW: 18243 MW
• Reactivity: Human,Monkey,Mouse,Rat
• Applications: Flow Cytometry, ICC/IF, IHC, WB

As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.

Biological background

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1. Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, also called DOD, is an enzyme that in humans is encoded by the PIN1 gene. It is mapped to 19p13.2. The enzyme binds to a subset of proteins and thus plays a role as a post phospho PIN1rol in regulating protein function. Studies have shown that the deregulation of PIN1 may play a pivotal role in various diseases. Notably, the up-regulation of PIN1 may be implicated in certain cancers, and the down-regulation of Pin1 may be implicated in Alzheimer's disease. Inhibitors of PIN1 may have therapeutic implications for cancer and immune disorders. PIN1 activity regulates the outcome of proline-ed kinase (e.g. MAPK, CDK or GSK3) signalling and consequently regulates cell proliferation (in part through control of cyclin D1 levels and stability) and cell survival. PIN1 also has an essential role in maintaining cell proliferation and regulating cyclin D1 function. Functional note: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins (PubMed:21497122, PubMed:22033920). Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). 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 (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). 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 (PubMed:22608923). . Reported localization: Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122). . Expression/tissue context: The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells. .

Research relevance and current trends

• Alzheimer's Disease: Researchers commonly examine how PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) relates to this theme using model systems and orthogonal readouts.
• Cell Cycle: Researchers commonly examine how PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) relates to this theme using model systems and orthogonal readouts.
• Cell Division: Researchers commonly examine how PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) relates to this theme using model systems and orthogonal readouts.

Common research applications

• Western blotting: compare relative PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) levels across conditions; band patterns may reflect isoforms and processing.
• IHC/IHC-F: assess spatial distribution of PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) across tissue regions and cell types using matched controls.
• Flow cytometry: quantify target-positive populations and shifts in expression; gating strategy and background staining controls are essential.

Notes for experimental interpretation

• Specificity notes: No cross reactivity with other proteins.
• Cross-reactivity: No cross-reactivity with other proteins
• Family / similarity context: Contains 1 PpiC domain.
• Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
• Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.

Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.