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Manufactured by BioVendor

Neudesin Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF
  • Species:Human
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Cat. No. Size Price

RD172276100 0.1 mg
PubMed Product Details
Technical Data


Recombinant protein


Total 151 AA. MW 16.9 kDa (calculated). UniProtKB acc. No. Q9UMX5 (Gly32-Phe172). N-terminal his-tag (10 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence



E. coli


Purity as determined by densitometric image analysis: >95%


14% SDS-PAGE separation of Human Neudesin
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and boiled sample, 2.5μg/lane
3. non-reduced and non-boiled sample, 2.5μg/lane


< 0.1 EU/μg


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 200μl of deionized water to prepare a working stock solution of 0.5 mg/mL and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in 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, Neural tissue markers, Oncology


Human neudesin (alternative names: Cell immortalization-related protein 2, CIR2; Neuron-derived neurotrophic factor, NENF; Secreted protein of unknown function, SPUF; candidate oncogene GIG47) protein comprises 172 amino acid residues including 31 residues of the hypothesised signal sequence. The human neudesin gene was mapped to chromosome 1p33. Neudesin belongs to the MAPR (membrane-associated progesterone receptor) family which includes PGRMC1, PGRMC2, neudesin, and neuferricin, and is a subfamily of the Cyt-b5 family, which consists of heme-binding proteins with a Cyt-b5-like heme/steroid-binding domain in their central regions. Neudesin neurotrophic activity is dependent on the binding of heme to its cytochrome b5-like heme/steroid-binding domain. Mouse neudesin mRNA is expressed abundantly in the developing brain and spinal cord in embryos, but is expressed widely in postnatal tissues including brain, heart, lung, and kidney. In the brain the mRNA was expressed in neurons but not glial cells. The protein exhibited significant neurotrophic activity in primary cultured mouse neurons but no mitogenic activity was observed in primary cultured mouse astrocytes. Neudesin activated the mitogen-activated protein (MAP) and phosphatidyli­nositol-3 (PI-3) kinase pathways. It has been found that neudesin is expressed in the mouse embryonic cerebral cortex and the neural precursor cells where it significantly promotes neuronal differentiation but inhibits astrocyte differentiation. In addition, it transiently promotes neural cell proliferation in the neural precursor cells during the early stages of development. Over-expression of neudesin has been observed in primary breast tumors as well as other human tumors including carcinomas of the uterine cervix, malignant lymphoma, colon, lung, skin, and leukemia. The ectopic expression of neudesin (GIG47 oncogene) in MCF7 cells promoted invasiveness in the presence of 50% serum and also increased tumorigenicity in in vivo tumor formation assay. The tumorigenesis mechanism involving neudesin might be mediated by the activation of MAPK and PI3K pathways. Neudesin may play a role in the breast tumorigenesis, thus representing a novel target for the treatment of breast cancer. Abundant expression of neudesin in white adipose tissue of adult mice has been reported. Neudesin-hemin significantly suppressed adipogenesis in 3T3-L1 cells. On the other hand, the knockdown of neudesin by RNA interference markedly promoted adipogenesis in 3T3-L1 cells and decreased MAPK activation during adipocyte differentiation. These findings suggest that neudesin plays a critical role in the early stage of adipocyte differentiation. Robust neudesin expression has been observed in hypothalamic nuclei known to regulate food intake, and its expression was altered under the diet-induced obese (DIO) condition relative to the fed state. Hypothalamic neudesin mRNA was regulated by brain-derived neurotrophic factor (BDNF) signaling, itself an important regulator of appetite. Delivery of purified recombinant BDNF into the lateral cerebral ventricle of mice decreased hypothalamic neudesin expression, while pharmacological inhibition of trkB signaling increased neudesin (NENF) mRNA expression. Furthermore, recombinant NENF administered via an intracerebroven­tricular cannula decreased food intake and body weight and increased hypothalamic Pomc and Mc4r mRNA expression. The appetite-suppressing effect of NENF was abrogated in obese mice fed a high-fat diet, demonstrating a diet-dependent modulation of NENF function. The existence of a hypothetical regulatory circuit involving BDNF, NENF, and melanocortin signaling has been proposed.

Product References (1)


  • Kratochvilova H, Lacinova Z, Klouckova J, Kavalkova P, Cinkajzlova A, Trachta P, Krizova J, Benes M, Dolezalova K, Fried M, Vlasakova Z, Pelikanova T, Spicak J, Mraz M, Haluzik M. Neudesin in obesity and type 2 diabetes mellitus: the effect of acute fasting and weight reducing interventions. Diabetes Metab Syndr Obes. 2019 Mar 28;12:423-430. doi: 10.2147/DMSO.S193259. eCollection 2019. PubMed PMID: 30992678. PubMed CentralPMCID: PMC6445223. See more on PubMed
Summary References (7)

References to Neudesin

  • Byerly MS, Swanson RD, Semsarzadeh NN, McCulloh PS, Kwon K, Aja S, Moran TH, Wong GW, Blackshaw S. Identification of hypothalamic neuron-derived neurotrophic factor as a novel factor modulating appetite. Am J Physiol Regul Integr Comp. 2013 Jun 15;304 (12):R1085-95
  • Han KH, Lee SH, Ha SA, Kim HK, Lee C, Kim DH, Gong KH, Yoo J, Kim S, Kim JW. The functional and structural characterization of a novel oncogene GIG47 involved in the breast tumorigenesis. BMC Cancer. 2012;12:274
  • Kimura I, Konishi M, Asaki T, Furukawa N, Ukai K, Mori M, Hirasawa A, Tsujimoto G, Ohta M, Itoh N, Fujimoto M. Neudesin, an extracellular heme-binding protein, suppresses adipogenesis in 3T3-L1 cells via the MAPK cascade. Biochem Biophys Res Commun. 2009 Mar 27;381 (1):75-80
  • Kimura I, Konishi M, Miyake A, Fujimoto M, Itoh N. Neudesin, a secreted factor, promotes neural cell proliferation and neuronal differentiation in mouse neural precursor cells. J Neurosci Res. 2006 Jun;83 (8):1415-24
  • Kimura I, Nakayama Y, Yamauchi H, Konishi M, Miyake A, Mori M, Ohta M, Itoh N, Fujimoto M. Neurotrophic activity of neudesin, a novel extracellular heme-binding protein, is dependent on the binding of heme to its cytochrome b5-like heme/steroid-binding domain. J Biol Chem. 2008 Feb 15;283 (7):4323-31
  • Kimura I, Nakayama Y, Zhao Y, Konishi M, Itoh N. Neurotrophic effects of neudesin in the central nervous system. Front Neurosci. 2013;7:111
  • Kimura I, Yoshioka M, Konishi M, Miyake A, Itoh N. Neudesin, a novel secreted protein with a unique primary structure and neurotrophic activity. J Neurosci Res. 2005 Feb 1;79 (3):287-94
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