NGB Human, His

Neuroglobin Human Recombinant, His Tag
Cat. No.
BT10418
Source
Escherichia Coli.
Synonyms
NGB.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 90% 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

Neuroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-151a.a) and having a molecular mass of 18kDa. NGB is fused to 10 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Neuroglobin is a 151 amino acid protein found primarily in the brain and retina of vertebrates. As a member of the globin family, it plays a role in oxygen supply, neuronal protection during hypoxia, and potentially brain signal transduction. Neuroglobin levels increase in response to low oxygen conditions, both in lab settings and during events like stroke. Studies suggest that neuroglobin can improve neuron survival after oxygen deprivation and may act as a sensor for oxidative stress in the brain.
Description
Recombinant Human Neuroglobin, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 161 amino acids (including a 10 amino acid His-tag at the N-terminus) and has a molecular weight of 18kDa. The protein is purified using proprietary chromatographic methods.
Physical Appearance
White, lyophilized powder.
Formulation
The product is filtered through a 0.4µm filter and lyophilized from a 0.5mg/ml solution in phosphate buffered saline.
Purity
Purity is greater than 90% as determined by SDS-PAGE.
Solubility
To prepare a working solution, add deionized water to the lyophilized powder to achieve a concentration of approximately 0.5mg/ml. Allow the pellet to dissolve completely. Please note that the product is not sterile. Filter it through a sterile filter before use in cell culture.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. Reconstituted protein is stable at 4°C for up to two weeks and shows no change in that time frame.
Synonyms
NGB.
Source
Escherichia Coli.
Amino Acid Sequence

MKHHHHHHAS MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG VKLSSFSTVG ESLLYMLEKC LGPAFTPATR AAWSQLYGAV VQAMSRGWDG E.

Product Science Overview

Structure and Expression

Neuroglobin is a single, non-glycosylated polypeptide chain with a molecular mass of approximately 18 kDa . The recombinant form of neuroglobin, tagged with a His (histidine) tag, is produced in Escherichia coli (E. coli) expression systems . The His tag, typically consisting of six histidine residues, is fused to the N-terminus of the protein, facilitating its purification through affinity chromatography .

Function and Significance

Neuroglobin is believed to function as an oxidative stress-responsive sensor in the brain, playing a role in signal transduction . Its expression is upregulated in response to neuronal hypoxia and focal cerebral ischemia, suggesting its involvement in neuroprotection . Experimental studies have shown that inhibiting neuroglobin expression reduces neuronal survival after hypoxia, while overexpression enhances it .

Applications

Recombinant neuroglobin with a His tag is widely used in laboratory research to study its structure, function, and potential therapeutic applications. The His tag allows for easy purification and detection of the protein, making it a valuable tool for biochemical and biophysical studies .

Physical Properties and Storage

The recombinant neuroglobin is typically provided as a lyophilized (freeze-dried) powder, which should be reconstituted in deionized water to prepare a working stock solution . It is recommended to store the lyophilized protein at -20°C and avoid repeated freezing and thawing cycles to maintain its stability .

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