FGF12 Human

Fibroblast Growth Factor 12 Human Recombinant
Cat. No.
BT8204
Source

Escherichia Coli. 

Synonyms

FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Shipped with Ice Packs
In Stock

Description

Fibroblast Growth Factor 12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.5kDa. The FGF12 is purified by proprietary chromatographic techniques. 

Product Specs

Introduction
FGF12, a member of the Fibroblast Growth Factor (FGF) family, exhibits mitogenic and cell survival properties, contributing to embryonic development, cell growth, morphogenesis, tissue repair, and tumor progression. Unlike most FGFs, FGF12 lacks an N-terminal signal sequence but possesses clusters of basic residues that act as a nuclear localization signal, leading to its nuclear accumulation upon mammalian cell transfection. Implicated in nervous system development and function, FGF12 interacts with IB2 (islet brain-2), a cellular kinase scaffold, and voltage-gated sodium channels, participating in intracellular signaling and ion exchange.
Description
Recombinant Human Fibroblast Growth Factor 12, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 181 amino acids with a molecular weight of 20.5 kDa. The protein undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, and 1mM DTT.
Solubility
Reconstitute the lyophilized Fibroblast Growth Factor 12 in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized FGF12 remains stable at room temperature for 3 weeks but should be stored desiccated below -18°C. Upon reconstitution, store Fibroblast Growth Factor 12 at 4°C for 2-7 days. For long-term storage, keep it below -18°C. Avoid freeze-thaw cycles.
Purity
Greater than 98.0% as determined by: (a) RP-HPLC analysis. (b) SDS-PAGE analysis.
Biological Activity
Determined by FGF12 binding ability in a functional ELISA. Immobilized FGFR4/Fc Chimera at 5 µg/mL (100 µL/well) exhibits a linear range of 1.6100 ng/mL for FGF12 binding.
Synonyms

FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.

Source

Escherichia Coli. 

Amino Acid Sequence

MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T.

Product Science Overview

Introduction

Fibroblast Growth Factor 12 (FGF12) is a member of the fibroblast growth factor (FGF) family, which consists of heparin-binding proteins involved in a wide range of biological processes, including cell growth, development, and tissue repair. FGF12, in particular, has garnered attention for its role in neural development and function.

Structure and Function

FGF12 is a medium-sized single-chain protein with a molecular weight of approximately 22 kDa. It shares a conserved core of about 120 amino acids with other members of the FGF family. The protein functions by binding to and activating high-affinity FGF receptors (FGFRs) on target cells, initiating a signal transduction cascade that involves kinases and transcription factors .

Biological Roles

FGF12 plays a crucial role in regulating neural development and function. It is involved in various cellular processes such as mitogenesis, differentiation, migration, and angiogenesis. Changes in FGF12 expression have been linked to the pathophysiology of several neurological diseases .

Recombinant Production

Recombinant human FGF12 is produced using standard biotechnological techniques. The gene encoding FGF12 is cloned into an expression vector, which is then introduced into a host organism, typically E. coli. The host cells express the FGF12 protein, which is subsequently purified using chromatographic methods to achieve high purity and biological activity .

Applications in Research and Medicine

Recombinant FGF12 is widely used in biomedical research to study its role in neural development and its potential therapeutic applications. It is employed in cell culture applications to maintain, expand, and differentiate various cell types. Additionally, FGF12 is used to investigate signaling interactions and pathways involved in neural development and disease .

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