Recombinant Human Neutrophil gelatinase-associated lipocalin protein (LCN2) (Active)

SKU:BHP10500273
Overview
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Recombinant LCN2 Human protein produced in E. coli, Tag-Free spanning 21-198aa. Suitable for binding assays, functional studies, and assay development.
Expression System E. coli
Tag Tag-Free
Purity >95% as determined by SDS-PAGE.
Species Homo sapiens (Human)
Molecular Weight 20.5 kDa
Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) - 500 ug, 100 ug, 10 ug
  • Lead time: In Stock at Manufacturer. Lead time is typically 5-10 business days.
  • Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Options selector
Catalog no. Size
CSB-AP000461HU-500UG 500 ug
CSB-AP000461HU-100UG 100 ug
CSB-AP000461HU-10UG 10 ug
Field Specification
Activity
  • Yes
Alternative Names NGAL, Lipocalin-2, Oncogene 24p3, Siderocalin LCN2, p25
Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.
Endotoxin Level Less than 1.0 EU/μg as determined by LAL method.
Expression System
  • E. coli
Form Lyophilized powder
Function
  • Iron-trafficking protein involved in multiple processes such as apoptosis
  • innate immunity and renal development. Binds iron through association with 2
  • 5-dihydroxybenzoic acid (2
  • 5-DHBA)
  • a siderophore that shares structural similarities with bacterial enterobactin
  • and delivers or removes iron from the cell
  • depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor
  • leading to release of iron and subsequent increase of intracellular iron concentration. In contrast
  • association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore
  • iron chelation and iron transfer to the extracellular medium
  • thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation
Molecular Weight 20.5 kDa
Product Type
  • Recombinant Protein
Purity >95% as determined by SDS-PAGE.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Species Homo sapiens (Human)
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
UniProt # P80188

Scientific Background

Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration.

Product Description

E. coli Expression

Recombinant Human Neutrophil gelatinase-associated lipocalin protein (LCN2) (Active) is a recombinant protein expressed in E. coli and purified to >95% as determined by SDS-PAGE. as determined by SDS-PAGE. Supplied as Lyophilized powder, tag-free. For research use only.

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Specifications

Molecular Weight 20.5 kDa
Expression Region 21-198aa
Expression System E. coli
Tag Tag-Free
Purity >95% as determined by SDS-PAGE.
Form Lyophilized powder
Storage Buffer Lyophilized from a 0.2 μm filtered PBS, pH 7.4, with 0.05 % Tween-20
Endotoxin Level Less than 1.0 EU/μg as determined by LAL method.
UniProt Accession P80188
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Functional Activity

Biologically Validated

Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.

Safety & Handling

For Research Use Only (RUO). Not intended for diagnostic or therapeutic use. Handle as potentially biohazardous material. Follow your institution's biosafety guidelines when working with recombinant proteins.

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What expression system was used to produce this protein?

This recombinant protein is expressed in E. coli, a widely used system for producing soluble, biologically active proteins at scale. The E. coli expression platform enables efficient folding and high yields, suitable for functional and binding assays.

What is the tag and purity of this product?

This protein is supplied as Tag-Free and has been purified to >95% as determined by SDS-PAGE. as determined by SDS-PAGE. High purity minimizes interference in downstream assays, particularly in cell-based bioactivity studies and ELISA development.

How should I reconstitute and store this product?

Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1–1.0 mg/mL. For long-term storage, add 5–50% glycerol and store in aliquots at -20°C or -80°C to avoid repeated freeze-thaw cycles. The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Is this protein biologically active?

Yes. Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.

What applications is this recombinant protein suitable for?

This recombinant protein is suitable for a range of in vitro research applications including binding assays, protein–protein interaction studies, cell proliferation/bioactivity assays, ELISA standard curve calibration, and assay development. Confirm suitability for your specific assay conditions with the product datasheet.

We offer flexible ordering options including bulk quantities, custom formulations, and endotoxin removal services for many of our recombinant proteins. Lead times and minimum order quantities vary by product. For custom conjugation, specialized buffer formulations, or volume pricing, please contact our support team. All customization requests are handled in partnership with our manufacturing suppliers and are subject to feasibility review.

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