IMPAD1 Mouse Bioactive

Inositol Monophosphatase Domain Containing 1 Mouse Recombinant Bioactive
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Description

Metabolic Regulation

IMPAD1 catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to AMP in the Golgi lumen, preventing PAP-induced cytotoxicity . This activity is essential for glycosaminoglycan sulfation during skeletal development .

Cancer Progression

Studies highlight IMPAD1's dual role in lung cancer metastasis:

  • AMPK-Notch1-HEY1 Pathway Activation: Accumulated AMP upregulates pAMPK, driving Notch1/HEY1 signaling to promote metastasis .

  • Mitochondrial ROS Suppression: Inhibits Complex I of the electron transport chain, reducing ROS levels and enhancing cancer cell survival .

  • EMT Regulation: Repressed by miR-200/miR-96 during epithelial-to-mesenchymal transition (EMT), IMPAD1 upregulation alters Golgi dynamics and secretome composition to facilitate invasion .

Research Applications

IMPAD1 Mouse Bioactive is utilized in:

  • Western Blotting: Detected at ~42 kDa in neuroblastoma (Neuro-2A) and pheochromocytoma (PC-12) cell lines .

  • Immunocytochemistry: Localizes to the cytoplasm in chondrocyte-differentiated mesenchymal stem cells .

  • Functional Assays: Validates enzymatic activity via PAP-to-AMP conversion kinetics .

Clinical and Pathological Relevance

ConditionIMPAD1 Association
GRAPP-Type ChondrodysplasiaMutations disrupt skeletal development via impaired glycosaminoglycan sulfation .
Lung Cancer MetastasisHigh IMPAD1 correlates with reduced survival and increased lymph node metastasis .
Immune Microenvironment ModulationSecretome alterations suppress CD4+/CD8+ T cell populations, promoting immune evasion .

Key Research Findings

  1. In Vivo Metastasis: IMPAD1 knockdown reduces lung cancer metastasis in mouse models by 60–70% .

  2. Golgi Dynamics: Interaction with Synaptotagmin XI (Syt11) enhances vesicular trafficking, modifying extracellular matrix components like collagen and fibronectin .

  3. Therapeutic Targeting: ADORA1 inhibition reverses AMPK-HEY1 signaling in IMPAD1-overexpressing cells, suggesting potential therapeutic avenues .

Product Specs

Introduction
Inositol monophosphatase 3 (IMPAD1), a member of the inositol monophosphatase family, is localized in the Golgi apparatus. It functions as an enzyme that catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). Mutations in the IMPAD1 gene are associated with GRAPP type chondrodysplasia, characterized by joint dislocations. Additionally, a pseudogene of IMPAD1 is found on the long arm of chromosome 1.
Description
IMPAD1 Mouse Recombinant, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 332 amino acids (residues 34-356) and has a molecular mass of 36.2 kDa. On SDS-PAGE, the apparent molecular size will be approximately 28-40 kDa. This recombinant protein is expressed with a 6 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The IMPAD1 protein solution is provided at a concentration of 0.5 mg/ml in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For longer periods, it is recommended to store the product frozen at -20°C. To ensure long-term stability, the addition of a carrier protein (0.1% HSA or BSA) is recommended. Multiple freeze-thaw cycles should be avoided.
Purity
The purity of this product is greater than 95.0% as determined by SDS-PAGE analysis.
Biological Activity
The specific activity, a measure of the enzyme's ability to hydrolyze Adenosine 3, 5-diphosphate, is greater than 5,000 pmol/min/µg. This activity is determined at pH 7.5 and 25°C.
Synonyms
Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH HH.

Product Science Overview

Structure and Expression

IMPAD1 is a glycosylated polypeptide chain consisting of 332 amino acids . It is primarily localized in the Golgi apparatus , where it plays a crucial role in cellular processes.

Biological Function

IMPAD1 catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP) . This reaction is essential for maintaining the balance of inositol phosphates within the cell, which are critical for various cellular functions, including signal transduction and membrane biogenesis.

Tissue Distribution

The expression of IMPAD1 is restricted to specific tissues, with a significant presence in the brain . This tissue-specific expression suggests that IMPAD1 may have specialized functions in neural cells.

Recombinant Bioactive Form

The recombinant bioactive form of IMPAD1, produced in Sf9 Baculovirus cells, is used in various research applications . This form retains the enzyme’s biological activity, making it a valuable tool for studying its function and regulation in vitro.

Research Applications

IMPAD1 is studied for its role in neurodevelopmental disorders and neurodegenerative diseases. Its involvement in inositol phosphate metabolism makes it a potential target for therapeutic interventions aimed at modulating cellular signaling pathways.

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