LCN2 Human

Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant
Cat. No.
BT6159
Source
Escherichia Coli.
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by: 
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec'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

LCN2 Human Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains consisting of two 178 amino acids and having a molecular mass of 41.0kDa. 

Product Specs

Introduction
Recombinant Human Lipocalin-2, also known as Neutrophil Gelatinase Associated Lipocalin (NGAL), is a member of the lipocalin family. This family, comprising 25 proteins including a1-microglobulin and b-lactoglobulin, is characterized by the ability to bind small, hydrophobic molecules within their hydrophobic core. This allows them to act as transporters for substances such as retinol, biliverdins, and prostaglandins. NGAL is believed to play a role in regulating inflammatory responses and is found in elevated levels in the blood of patients following a stroke.
Description
Recombinant Human LCN2, produced in E. coli, is a non-glycosylated homodimeric protein. It consists of two identical polypeptide chains, each composed of 178 amino acids, resulting in a molecular weight of 41.0 kDa.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
LCN2 protein was lyophilized from a 0.2 µm filtered solution concentrated in PBS (pH 7.4) containing 0.05% Tween-20.
Stability
Lyophilized LCN2 is stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store the desiccated protein below -18°C. Upon reconstitution, LCN2 should be stored at 4°C for short-term use (2-7 days) and below -18°C for future use. For extended storage periods, adding a carrier protein such as 0.1% HSA or BSA is advised. Avoid repeated freeze-thaw cycles.
Purity
The purity of LCN2 is greater than 95.0% as determined by:
(a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis.
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity
The ED50, determined by a cell proliferation assay using human TF-1 cells, is less than 0.5 ng/ml. This corresponds to a specific activity greater than 2.0 × 1,000,000 IU/mg.
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
Source
Escherichia Coli.
Amino Acid Sequence
QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG LPENHIVFPV PIDQCIDG 

Product Science Overview

Discovery and Structure

Lipocalin-2 was initially identified in 1989 through the detection of its messenger RNA, named 24p3, in simian virus 40-infected kidney cells of mouse models. It was first isolated in human neutrophil granules, leading to its name, neutrophil gelatinase-associated lipocalin (NGAL) . The protein is a 25-kDa glycoprotein that is protease-resistant due to its complex formation with matrix metalloprotease-9 (MMP-9) in human neutrophils .

Function and Mechanism

NGAL plays a crucial role in the innate immune response by sequestering iron and preventing its use by bacteria, thus limiting their growth . It binds to bacterial siderophores, which are iron-chelating molecules, and also to the mammalian siderophore 2,5-dihydroxybenzoic acid (2,5-DHBA). This binding ensures that excess free iron does not accumulate in the cytoplasm, preventing the formation of reactive oxygen species .

Upon encountering invading bacteria, toll-like receptors on immune cells stimulate the synthesis and secretion of NGAL. Secreted NGAL then limits bacterial growth by sequestering iron-containing siderophores . Additionally, NGAL functions as a growth factor and participates in synaptic plasticity .

Clinical Significance

NGAL is used as a biomarker for kidney injury due to its protease resistance and low molecular weight, which allows it to be excreted and detected in urine . Injured epithelial cells in the kidney secrete a monomeric form of NGAL, while activated neutrophils secrete a dimeric form. This distinction can potentially improve acute kidney injury (AKI) diagnostics by differentiating NGAL of inflammatory origin from that of renal origin .

In AKI patients, NGAL levels are elevated in both blood and urine within two hours of injury, and plasma NGAL has been shown to be predictive of dialysis need . NGAL is also associated with chronic kidney disease, contrast-induced nephropathy, kidney transplant, and mortality . Monitoring NGAL levels provides a more precise and sensitive marker for diagnosing AKI compared to serum creatinine levels, reducing delayed diagnosis and treatment .

Therapeutic Potential

The therapeutic potential of NGAL is being explored in various clinical trials. Its role in iron regulation and immune response makes it a promising candidate for therapeutic interventions in diseases characterized by iron dysregulation and bacterial infections . Additionally, NGAL’s involvement in cell regulation, proliferation, and differentiation highlights its potential in cancer therapy .

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