AIP Antibody (Rabbit mAb) [J10D14] Datasheet

Biological Description

Specificity	AIP Antibody (Rabbit mAb) [J10D14] detects endogenous levels of total AIP protein.
Background	Aryl hydrocarbon receptor–interacting protein (AIP) is an immunophilin-like co‑chaperone that associates with heat shock proteins and nuclear receptors and functions as a regulator of protein stability and signaling, best characterized in the context of the cytoplasmic AHR–AIP–Hsp90 complex and pituitary tumorigenesis. The protein contains an N‑terminal region with coiled-coil/Helix features and a C‑terminal tetratricopeptide repeat (TPR) domain that mediates interaction with Hsp90 and client proteins; these structural elements allow AIP to integrate into multi‑chaperone assemblies that stabilize receptors and signaling molecules in an inactive yet ligand‑responsive state. In the xenobiotic-sensing pathway, AIP forms a core part of the AHR complex, maintaining AHR in the cytoplasm with Hsp90, p23 and XAP2, controlling receptor folding, ligand binding and nuclear translocation, and thereby modulating transcriptional responses to environmental toxins and endogenous ligands. In endocrine tissues, germline loss‑of‑function mutations in AIP cause a pituitary adenoma predisposition syndrome within familial isolated pituitary adenomas (FIPA), where affected individuals develop early‑onset, aggressive macroadenomas that are most often growth hormone- or prolactin‑secreting, and AIP behaves as a tumor suppressor whose reduced function permits uncontrolled pituitary cell proliferation. Functional studies show that overexpression of wild‑type AIP in fibroblast and pituitary cell lines markedly reduces cell proliferation, whereas mutant AIP variants lose this antiproliferative effect, and all examined AIP mutations disrupt interaction with phosphodiesterase‑4A5, linking AIP’s tumor suppressor activity to regulation of cAMP signaling. In normal pituitary tissue, AIP colocalizes specifically with growth hormone and prolactin in secretory vesicles of somatotrophs and lactotrophs, while in sporadic pituitary adenomas AIP expression becomes widespread across tumor types and its subcellular localization shifts, with cytoplasmic rather than vesicular distribution in many adenomas, indicating that altered expression patterns and mislocalization accompany tumor development. Population and cohort studies show that 15–30% of FIPA families and a substantial fraction of apparently sporadic pediatric pituitary adenomas harbor inactivating germline AIP mutations, whereas more than half of such familial cases lack AIP mutations, suggesting genetic heterogeneity in pituitary adenoma predisposition beyond AIP. AIP variants and expression changes also appear in other cancers, and high AIP expression associates with more aggressive disease in colorectal and diffuse large B cell lymphoma, indicating that AIP can act as a tumor suppressor or oncogenic factor in a tissue‑specific manner, consistent with its role as a multi‑chaperone modulator that impacts different signaling networks depending on cellular context.

Specificity

AIP Antibody (Rabbit mAb) [J10D14] detects endogenous levels of total AIP protein.

Background

Aryl hydrocarbon receptor–interacting protein (AIP) is an immunophilin-like co‑chaperone that associates with heat shock proteins and nuclear receptors and functions as a regulator of protein stability and signaling, best characterized in the context of the cytoplasmic AHR–AIP–Hsp90 complex and pituitary tumorigenesis. The protein contains an N‑terminal region with coiled-coil/Helix features and a C‑terminal tetratricopeptide repeat (TPR) domain that mediates interaction with Hsp90 and client proteins; these structural elements allow AIP to integrate into multi‑chaperone assemblies that stabilize receptors and signaling molecules in an inactive yet ligand‑responsive state. In the xenobiotic-sensing pathway, AIP forms a core part of the AHR complex, maintaining AHR in the cytoplasm with Hsp90, p23 and XAP2, controlling receptor folding, ligand binding and nuclear translocation, and thereby modulating transcriptional responses to environmental toxins and endogenous ligands. In endocrine tissues, germline loss‑of‑function mutations in AIP cause a pituitary adenoma predisposition syndrome within familial isolated pituitary adenomas (FIPA), where affected individuals develop early‑onset, aggressive macroadenomas that are most often growth hormone- or prolactin‑secreting, and AIP behaves as a tumor suppressor whose reduced function permits uncontrolled pituitary cell proliferation. Functional studies show that overexpression of wild‑type AIP in fibroblast and pituitary cell lines markedly reduces cell proliferation, whereas mutant AIP variants lose this antiproliferative effect, and all examined AIP mutations disrupt interaction with phosphodiesterase‑4A5, linking AIP’s tumor suppressor activity to regulation of cAMP signaling. In normal pituitary tissue, AIP colocalizes specifically with growth hormone and prolactin in secretory vesicles of somatotrophs and lactotrophs, while in sporadic pituitary adenomas AIP expression becomes widespread across tumor types and its subcellular localization shifts, with cytoplasmic rather than vesicular distribution in many adenomas, indicating that altered expression patterns and mislocalization accompany tumor development. Population and cohort studies show that 15–30% of FIPA families and a substantial fraction of apparently sporadic pediatric pituitary adenomas harbor inactivating germline AIP mutations, whereas more than half of such familial cases lack AIP mutations, suggesting genetic heterogeneity in pituitary adenoma predisposition beyond AIP. AIP variants and expression changes also appear in other cancers, and high AIP expression associates with more aggressive disease in colorectal and diffuse large B cell lymphoma, indicating that AIP can act as a tumor suppressor or oncogenic factor in a tissue‑specific manner, consistent with its role as a multi‑chaperone modulator that impacts different signaling networks depending on cellular context.

Usage Information

Application

WB

Dilution

WB

1:1000 - 1:10000

Reactivity

Mouse, Rat, Human

Source

Rabbit Monoclonal Antibody

MW

38 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

References

https://pubmed.ncbi.nlm.nih.gov/24366639/
https://pubmed.ncbi.nlm.nih.gov/18381572/

AIP Antibody (Rabbit mAb) [J10D14]

Biological Description

Usage Information

References

Application Data