NEFL Human

Neurofilament Light Human Recombinant
Cat. No.
BT28971
Source
Escherichia Coli.
Synonyms

Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 90.0% as determined 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

NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).

Product Specs

Introduction

Neurofilament light polypeptide (NEFL), encoded by the NEFL gene, is linked to Charcot-Marie-Tooth disease. This protein's light subunit, detectable in plasma and cerebrospinal fluid via immunoassays, serves as a biomarker for axonal damage in neurological disorders. Elevated NEFL levels can indicate conditions such as Huntington's disease, Amyotrophic Lateral Sclerosis, and multiple sclerosis.

Description

Recombinant Human NEFL, produced in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 2-543. It includes a 9 amino acid N-terminal His tag, resulting in a total calculated molecular mass of 62.5 kDa.

Physical Appearance
White lyophilized powder, filtered for sterility.
Formulation

NEFL is sterile filtered (0.4 µm) and lyophilized from a 0.5 mg/ml solution containing 15 mM Tris and 85 mM Glycine at pH 8.5.

Solubility

To prepare a working stock solution of approximately 0.5 mg/ml, add deionized water to the lyophilized pellet and allow it to dissolve completely.

Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. Reconstituted protein remains stable at 4°C for a limited period and shows no significant change after two weeks at 4°C.
Purity

Purity exceeds 90.0% as determined by SDS-PAGE analysis.

Synonyms

Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

Source
Escherichia Coli.
Amino Acid Sequence

MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.

Product Science Overview

Structure and Function

NF-L is a 68 kDa protein encoded by the NEFL gene. It consists of 542 amino acids, including a 91 amino acid N-terminal head, a 304 amino acid alpha-helical rod, and a 147 amino acid C-terminal tail . Neurofilaments are essential for maintaining the structural integrity and diameter of axons, which are the long projections of neurons that transmit electrical signals. The proper functioning of neurofilaments is critical for the maintenance of neuronal caliber and the efficient conduction of nerve impulses .

Role in Neurological Disorders

Neurofilament light chain is a biomarker that can be measured in cerebrospinal fluid (CSF) and plasma. It reflects axonal damage in a variety of neurological disorders. Elevated levels of NF-L are associated with diseases such as amyotrophic lateral sclerosis (ALS), multiple sclerosis (MS), Alzheimer’s disease, and Huntington’s disease . The detection of NF-L in CSF and blood has become widely used as a biomarker for ongoing axonal compromise, making it a valuable tool for disease monitoring and prognosis .

Recombinant NF-L

Recombinant human NF-L is produced using Escherichia coli (E. coli) expression systems. The recombinant protein is typically purified to a high degree of purity, often greater than 95%, and is used in various research applications. It is available in both carrier-free and carrier-containing formulations. The carrier-free version does not contain bovine serum albumin (BSA), which can interfere with certain applications .

Applications in Research

Recombinant NF-L is used in a variety of research areas, including the study of neurodegenerative diseases, axonal injury, and the development of diagnostic assays. Methods used for NF-L measurement include sandwich enzyme-linked immunosorbent assay (ELISA), electrochemiluminescence, and high-sensitive single molecule array (SIMOA) . These techniques allow for the precise quantification of NF-L levels in biological samples, aiding in the understanding of disease mechanisms and the development of therapeutic interventions.

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