FABP12 Human

Fatty Acid Binding Protein-12 Human Recombinant
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Description

Tissue Distribution and Expression

FABP12 exhibits restricted tissue expression:

Tissue/Cell TypeExpression LevelSource
Retinoblastoma cellsHigh
Testis (rodent)Moderate
Prostate cancer cellsElevated in metastatic cases
Male germline stem cellsDetected

The Human Protein Atlas notes limited expression in standard human tissues, suggesting context-specific roles .

Lipid Metabolism and Signaling

  • Facilitates fatty acid trafficking to organelles (e.g., nucleus, mitochondria) .

  • Activates peroxisome proliferator-activated receptor gamma (PPARγ), a nuclear receptor linked to lipid metabolism and cancer progression .

Disease Associations

  • Prostate Cancer: Elevated FABP12 levels correlate with aggressive metastasis by inducing epithelial-to-mesenchymal transition (EMT) and enhancing fatty acid-dependent energy production .

  • Neurological Disorders: Predicted involvement in brain lipid metabolism, though direct evidence is limited .

Biomarker Potential

  • Prostate Cancer: Serum FABP12 levels may serve as a prognostic marker for metastasis .

  • Metabolic Disorders: Linked to lipid dysregulation, though further validation is needed .

Therapeutic Targets

  • Inhibiting FABP12-PPARγ signaling could suppress metastasis in prostate cancer .

  • Small-molecule modulators of FABP12 are under exploration for metabolic and inflammatory diseases .

Research Gaps and Future Directions

  • Mechanistic Insights: Clarify FABP12’s ligand preferences and tissue-specific regulatory pathways.

  • Disease Models: Expand studies to neurodegenerative diseases and metabolic syndromes.

  • Drug Development: Design FABP12-specific inhibitors to minimize off-target effects .

Product Specs

Introduction
FABP12, a member of the calycin superfamily and fatty-acid binding protein (FABP) family, functions as a carrier protein for fatty acids and other lipophilic substances such as eicosanoids and retinoids. These proteins are thought to facilitate the transfer of fatty acids between extra- and intracellular membranes. FABP12 plays a role in lipid transport and is expressed in several retinoblastoma cell lines. Notably, FABP12 has not been detected in fetal tissues.
Description
Recombinant Human FABP12, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 164 amino acids (1-140 a.a). It has a molecular weight of 18kDa. FABP12 is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A sterile, colorless solution.
Formulation
The FABP12 protein solution (0.5mg/ml) is supplied in a buffer containing 20mM Tris-HCl (pH 7.5), 0.15M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90.0% by SDS-PAGE analysis.
Synonyms
Fatty acid-binding protein 12, FABP12.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMIDQLQ GTWKSISCEN SEDYMKELGI GRASRKLGRL AKPTVTISTD GDVITIKTKS IFKNNEISFK LGEEFEEITP GGHKTKSKVT LDKESLIQVQ DWDGKETTIT RKLVDGKMVV ESTVNSVICT RTYEKVSSNS VSNS.

Product Science Overview

Introduction

Fatty Acid Binding Protein-12 (FABP12) is a member of the fatty acid-binding protein (FABP) family, which plays a crucial role in the intracellular transport of fatty acids and other lipophilic substances such as eicosanoids and retinoids . These proteins are essential for the transfer of fatty acids between extra- and intracellular membranes, facilitating various metabolic processes.

Discovery and Gene Information

FABP12 is one of the more recently identified members of the FABP family. The gene encoding FABP12 has been identified, but detailed studies on the protein itself are still limited . The FABP12 gene is a protein-coding gene associated with lipid binding and transporter activity . It is predicted to be located in the cytosol and is involved in pathways related to triglyceride metabolism and general metabolism .

Structure and Function

FABPs are small, structurally conserved cytosolic proteins characterized by a water-filled interior-binding pocket surrounded by ten anti-parallel beta sheets, forming a beta barrel. Two alpha-helices cap the pocket at the superior surface, which is thought to regulate binding . FABP12, like other FABPs, is believed to play a role in lipid transport within cells .

Expression and Role

FABP12 is expressed in several retinoblastoma cell lines, indicating its potential role in lipid transport within these cells . The protein’s exact functions and mechanisms are still under investigation, but it is believed to be involved in the intracellular transport of fatty acids and other lipophilic molecules, contributing to various metabolic processes .

Evolutionary Significance

The FABP family demonstrates strong evolutionary conservation and is present in a wide range of species, including Drosophila melanogaster, Caenorhabditis elegans, mice, and humans . This conservation suggests that FABPs, including FABP12, play fundamental roles in cellular metabolism and lipid transport.

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