FIBP Human

FGF-1 Intracellular-Binding Protein Human Recombinant

Cat. No.

BT9795

Source

E.coli.

Synonyms

FGFIBP, FIBP-1, Acidic fibroblast growth factor intracellular-binding protein, aFGF intracellular-binding protein, FGF-1 intracellular-binding protein, FIBP.

Appearance

Sterile Filtered colorless solution.

Purity

Greater than 95% 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.

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Description

FIBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 387amino acids (1-364) and having a molecular mass of 44.3kDa. The FIBP is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

FGF-1 Intracellular-Binding Protein (FIBP), a member of the Fibroblast growth factors (FGFs) family, binds to internalized FGF-1 and is believed to play a role in the mitogenic function of FGF-1. FGF activity influences development, adult tissue homeostasis, angiogenesis, and cancer progression. FIBP is primarily located in the nucleus and is highly expressed in the heart, skeletal muscle, and pancreas, with lower levels of expression in the brain, placenta, liver, and kidney.

Description

Recombinant human FIBP, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 387 amino acids (1-364) with a molecular weight of 44.3 kDa. A 23 amino acid His-Tag is fused to the N-terminus of FIBP. The protein undergoes purification using proprietary chromatographic techniques.

Physical Appearance

A sterile, colorless solution that has been filtered for sterility.

Formulation

FIBP protein is supplied at a concentration of 0.5 mg/ml in a buffer solution containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.

Stability

For short-term storage (2-4 weeks), keep the vial refrigerated at 4°C. For long-term storage, freeze the protein at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.

Purity

The purity of FIBP is greater than 95% as determined by SDS-PAGE analysis.

Synonyms

FGFIBP, FIBP-1, Acidic fibroblast growth factor intracellular-binding protein, aFGF intracellular-binding protein, FGF-1 intracellular-binding protein, FIBP.

Source

E.coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMTSELDI FVGNTTLIDE DVYRLWLDGY SVTDAVALRV RSGILEQTGA TAAVLQSDTM DHYRTFHMLE RLLHAPPKLL HQLIFQIPPS RQALLIERYY AFDEAFVREV LGKKLSKGTK KDLDDISTKT GITLKSCRRQ FDNFKRVFKV VEEMRGSLVD NIQQHFLLSD RLARDYAAIV FFANNRFETG KKKLQYLSFG DFAFCAELMI QNWTLGAVGE APTDPDSQMD DMDMDLDKEF LQDLKELKVL VADKDLLDLH KSLVCTALRG KLGVFSEMEA NFKNLSRGLV NVAAKLTHNK DVRDLFVDLV EKFVEPCRSD HWPLSDVRFF LNQYSASVHS LDGFRHQALW DRYMGTLRGC LLRLYHD.

Product Science Overview

Introduction

Fibroblast Growth Factor 1 (FGF-1), also known as acidic fibroblast growth factor (aFGF), is a member of the fibroblast growth factor family. This family of proteins is involved in a variety of biological processes, including cell growth, development, and tissue repair. FGF-1 is a non-glycosylated, single polypeptide protein that plays a crucial role in stimulating DNA synthesis and cell proliferation.

Structure and Function

FGF-1 is a small protein with a molecular mass of approximately 18 kDa in its reduced form and 16 kDa in its non-reduced form. It does not have a definitive signal sequence, which means it is not secreted through classical pathways. Instead, FGF-1 forms a disulfide-linked dimer inside cells, which associates with a complex of proteins at the cell membrane. This complex helps flip FGF-1 through the membrane to the exterior of the cell.

Once outside the cell, FGF-1 dissociates into monomeric form in the reducing conditions of the surrounding tissue. It can then enter systemic circulation or be sequestered in tissues by binding to heparan sulfate proteoglycans of the extracellular matrix.

Biological Activity

FGF-1 is capable of binding with all four fibroblast growth factor receptors (FGFRs) and exerts its intracellular effects through downstream pathways such as PLCγ and MAPK. This binding and subsequent signaling are essential for various cellular processes, including proliferation, differentiation, and migration. FGF-1 is particularly known for its role in promoting angiogenesis (the formation of new blood vessels) and wound healing.

Recombinant FGF-1

Recombinant human FGF-1 is produced using various expression systems, including E. coli and HEK293 cells. The recombinant protein is optimized for use in cell culture, differentiation studies, and functional assays. It is available in different purity grades, with research-grade FGF-1 being commonly used in laboratory settings.

Applications and Research

Recombinant FGF-1 has been widely used in research to study its effects on cell proliferation and differentiation. For example, it has been shown to stimulate dose-dependent proliferation of human primary fibroblast cell lines. This makes it a valuable tool for studying cellular processes and developing therapeutic strategies for tissue repair and regeneration.

Clinical Implications

Dysregulated FGF-1 signaling has been associated with various pathological conditions, including tumor invasion and metastasis. Understanding the mechanisms of FGF-1 action and its interactions with other cellular components is crucial for developing targeted therapies for cancer and other diseases.

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FIBP Human

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