FAIM Human

Fas Apoptotic Inhibitory Molecule Human Recombinant
Cat. No.
BT8155
Source
Escherichia Coli.
Synonyms
FAIM1, Fas Apoptotic Inhibitory Molecule, FAIM2, LFG, NMP35, Fas Apoptotic Inhibitory Molecule 1, FAIM.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85% 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

FAIM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-213aa) and having a molecular mass of 26.4kDa.
FAIM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Fas apoptotic inhibitory molecule, also known as FAIM, functions as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells. Additionally, FAIM protects against death receptor-triggered apoptosis and regulates B-cell signaling and differentiation. FAIM is associated with diseases such as hemorrhagic thrombocythemia and food allergy.
Description
Recombinant human FAIM protein, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 236 amino acids (residues 1-213) with a molecular mass of 26.4 kDa. The FAIM protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Sterile, clear, and colorless solution.
Formulation
FAIM protein solution (0.5 mg/mL) in 20 mM Tris-HCl buffer (pH 8.0), 0.4 M urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term 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
Greater than 85% purity as determined by SDS-PAGE.
Synonyms
FAIM1, Fas Apoptotic Inhibitory Molecule, FAIM2, LFG, NMP35, Fas Apoptotic Inhibitory Molecule 1, FAIM.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLLPFIR TLPLLCYNHL LVSPDSATLS PPYSLEKMTD LVAVWDVALS DGVHKIEFEH GTTSGKRVVY VDGKEEIRKE WMFKLVGKET FYVGAAKTKA TINIDAISGF AYEYTLEING KSLKKYMEDR SKTTNTWVLH MDGENFRIVL EKDAMDVWCN GKKLETAGEF VDDGTETHFS IGNHDCYIKA VSSGKRKEGI IHTLIVDNRE IPEIAS.

Product Science Overview

Introduction

The Fas Apoptotic Inhibitory Molecule (FAIM) is a protein that plays a crucial role in regulating apoptosis, or programmed cell death. This protein is particularly significant in the context of neurodegenerative diseases and immune responses. FAIM was originally discovered in 1999 and has since been the subject of extensive research due to its potential therapeutic applications .

Structure and Classification

FAIM is a 20-kDa cytosolic protein composed of 179 amino acids . It is highly conserved across mammalian species, indicating its essential role in cellular processes. There are two main isoforms of FAIM: FAIM1 and FAIM2. FAIM1 is predominantly expressed in immune cells, while FAIM2 is mainly found in neuronal cells .

Biological Properties and Functions

FAIM functions as an inhibitor of the Fas signaling pathway, which is a critical pathway for inducing apoptosis. By interfering with this pathway, FAIM helps to prevent unnecessary cell death, thereby contributing to cell survival and homeostasis . In neurons, FAIM2 has been shown to protect against stress-induced apoptosis, particularly in the retina .

Mode of Action

FAIM inhibits apoptosis by interacting with components of the Fas signaling pathway. Specifically, it binds to the Fas receptor and prevents the activation of caspase-8, a key enzyme in the apoptotic process . This interaction blocks the downstream signaling events that lead to cell death, thereby promoting cell survival.

Regulatory Mechanisms

The expression and activity of FAIM are regulated by various factors, including stress signals and cellular conditions. For instance, FAIM2 levels increase in response to retinal detachment, suggesting a role in protecting photoreceptor cells under stress . Additionally, FAIM interacts with other proteins such as p53 and HSP90, which further modulate its activity and stability .

Therapeutic Potential

Given its role in inhibiting apoptosis, FAIM has significant therapeutic potential, particularly in the treatment of neurodegenerative diseases and conditions involving excessive cell death. For example, recombinant human FAIM has been shown to dissolve pathological amyloid-β species, which are implicated in Alzheimer’s disease . This suggests that FAIM could be a valuable target for developing treatments for such conditions.

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