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Manufactured by BioVendor

Lipocalin-2/NGAL Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:24p3, MSFI, LCN2
  • Species:Human
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Cat. No. Size Price

RD172102050 0.05 mg
PubMed Product Details
Technical Data


Recombinant protein


Total 206 AA. MW: 23.9 kDa (calculated). N-terminal His-tag and TEV cleavage site, 28 extra AA (highlighted). UniProtKB P80188 (Gln21-Gly198). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence



E. coli


Purity as determined by densitometric image analysis: >95%



< 0.1 EU/ug


Filtered (0.4 μm) and lyophilized in 0.5 mg/mL in 0.05 M phosphate buffer, 0.075 M NaCl, pH 7.4


Add 100ul of deionized water to prepare a working stock solution of 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.


Western blotting, ELISA


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized protein at -80 °C. Lyophilized protein remains stable until the expiry date when stored at -80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.


This product is intended for research use only.


Research topic

Energy metabolism and body weight regulation, Renal disease


Lipocalin-2 (LCN2) is a 25 kDa secretory glycoprotein, also called NGAL (neutrophil gelatinase-associated lipocalin); NL (neutrophil lipocalin); p25; oncogen 24p3 and 25 kDa alpha-2-microglobulin-related subunit of MMP-9 (LCN2 forms a covalently linked, disulfide-bridged heterodimer with the 92 kDa type V collagenase (MMP-9)). LCN2 is predominantly expressed in adipose tissue and liver. It belongs to the lipocalin superfamily that consists of over 20 small secretory proteins. Lipocalin folds consist of 8 antiparallel ß-sheets that surround a hydrophobic pocket. A common feature of this protein family, following from its structure, is its capacity to bind and transport small lipophilic substancies such as free fatty acids, retinoids, arachidonic acid and various steroids. Although Lipocalin-2 was identified more than a decade ago, the physiologic function of this protein remains poorly understood. LCN2 appears to be upregulated in cells under the “stress” (e.g. from infection, inflammation, in tissues undergoing involution to ischemia or neoplastic transformation). Plasma levels of LCN2 rise in inflammatory or infective condition. It mediates an immune response to bacterial infection by sequestering iron. In this case, LCN2 may represent a promising candidate as a therapeutic agent against bacterial infection. Several recent reports suggest that LCN2 might represent a sensitive biomarker for early renal injury. In cardiopulmonary bypass-induced acute renal injury and cisplatin-induced nephrotoxic injury, increased de novo synthesis of LCN2 in proximal tubule cells leads to sharply increased concentration of this protein in both urine and serum. LCN2 might also be critical for normal kidney formation in the earliest stages of mammalian development. LCN2 may play an important role in breast cancer, in complex with MMP-9, by protecting MMP-9 from degradation thereby enhancing its enzymatic activity and facilitating angiogenesis and tumor growth. LCN2 is also highly expressed after malignant transformation of the lung, colon and pancreatic epithelia. Circulating levels of LCN2 play a causative role in pathogenesis of obesity-induced metabolic disorders such as insulin resistance, Type 2 Diabetes Mellitus and cardiovascular disorders. In addition, serum LCN2 concentrations were positively associated with adipocyte-fatty acid binding protein (A-FABP), a novel serum marker for adiposity and metabolic syndrome.

Areas of investigation: Bacterial infection Renal injury Angiogenesis Oncology Diabetes mellitus Metabolic syndrome Features

Summary References (17)

References to Lipocalin-2/NGAL

  • Bachorzewska-Gajewska H, Malyszko J, Sitniewska E, Malyszko JS, Dobrzycki S. Neutrophil gelatinase-associated lipocalin (NGAL) correlations with cystatin C, serum creatinine and eGFR in patients with normal serum creatinine undergoing coronary angiography. Nephrol Dial Transplant. 2007 Jan;22 (1):295-6
  • Bachorzewska-Gajewska H, Malyszko J, Sitniewska E, Malyszko JS, Poniatowski B, Pawlak K, Dobrzycki S. NGAL (neutrophil gelatinase-associated lipocalin) and cystatin C: are they good predictors of contrast nephropathy after percutaneous coronary interventions in patients with stable angina and normal serum creatinine?. Int J Cardiol. 2008 Jul 4;127 (2):290-1
  • Berger T, Togawa A, Duncan GS, Elia AJ, You-Ten A, Wakeham A, Fong HE, Cheung CC, Mak TW. Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury. Proc Natl Acad Sci U S A. 2006 Feb 7;103 (6):1834-9
  • Brunner HI, Mueller M, Rutherford C, Passo MH, Witte D, Grom A, Mishra J, Devarajan P. Urinary neutrophil gelatinase-associated lipocalin as a biomarker of nephritis in childhood-onset systemic lupus erythematosus. Arthritis Rheum. 2006 Aug;54 (8):2577-84
  • Flo TH, Smith KD, Sato S, Rodriguez DJ, Holmes MA, Strong RK, Akira S, Aderem A. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature. 2004 Dec 16;432 (7019):917-21
  • Lin HH, Li WW, Lee YC, Chu ST. Apoptosis induced by uterine 24p3 protein in endometrial carcinoma cell line. Toxicology. 2007 May 20;234 (3):203-15
  • Miharada K, Hiroyama T, Sudo K, Nagasawa T, Nakamura Y. Lipocalin 2 functions as a negative regulator of red blood cell production in an autocrine fashion. FASEB J. 2005 Nov;19 (13):1881-3
  • Mishra J, Ma Q, Kelly C, Mitsnefes M, Mori K, Barasch J, Devarajan P. Kidney NGAL is a novel early marker of acute injury following transplantation. Pediatr Nephrol. 2006 Jun;21 (6):856-63
  • Mishra J, Ma Q, Prada A, Mitsnefes M, Zahedi K, Yang J, Barasch J, Devarajan P. Identification of neutrophil gelatinase-associated lipocalin as a novel early urinary biomarker for ischemic renal injury. J Am Soc Nephrol. 2003 Oct;14 (10):2534-43
  • Mitsnefes MM, Kathman TS, Mishra J, Kartal J, Khoury PR, Nickolas TL, Barasch J, Devarajan P. Serum neutrophil gelatinase-associated lipocalin as a marker of renal function in children with chronic kidney disease. Pediatr Nephrol. 2007 Jan;22 (1):101-8
  • Mori K, Nakao K. Neutrophil gelatinase-associated lipocalin as the real-time indicator of active kidney damage. Kidney Int. 2007 May;71 (10):967-70
  • Nguyen MT, Devarajan P. Biomarkers for the early detection of acute kidney injury. Pediatr Nephrol. 2008 Dec;23 (12):2151-7
  • Parikh CR, Jani A, Mishra J, Ma Q, Kelly C, Barasch J, Edelstein CL, Devarajan P. Urine NGAL and IL-18 are predictive biomarkers for delayed graft function following kidney transplantation. Am J Transplant. 2006 Jul;6 (7):1639-45
  • Trachtman H, Christen E, Cnaan A, Patrick J, Mai V, Mishra J, Jain A, Bullington N, Devarajan P. Urinary neutrophil gelatinase-associated lipocalcin in D+HUS: a novel marker of renal injury. Pediatr Nephrol. 2006 Jul;21 (7):989-94
  • Vaidya VS, Ramirez V, Ichimura T, Bobadilla NA, Bonventre JV. Urinary kidney injury molecule-1: a sensitive quantitative biomarker for early detection of kidney tubular injury. Am J Physiol Renal Physiol. 2006 Feb;290 (2):F517-29
  • van Dam RM, Hu FB. Lipocalins and insulin resistance: etiological role of retinol-binding protein 4 and lipocalin-2?. Clin Chem. 2007 Jan;53 (1):5-7
  • Wang Y, Lam KS, Kraegen EW, Sweeney G, Zhang J, Tso AW, Chow WS, Wat NM, Xu JY, Hoo RL, Xu A. Lipocalin-2 is an inflammatory marker closely associated with obesity, insulin resistance, and hyperglycemia in humans. Clin Chem. 2007 Jan;53 (1):34-41
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