FABP12 Human

Fatty Acid Binding Protein-12 Human Recombinant
Cat. No.
BT6341
Source
Escherichia Coli.
Synonyms
Fatty acid-binding protein 12, FABP12.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

FABP12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 18kDa.
FABP12 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

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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