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Manufactured by BioVendor

Midkine Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:MK, NEGF-2, Neurite growth promoting factor 2
  • Species:Human
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Cat. No. Size Price

RD172042100 0.1 mg
PubMed Product Details
Technical Data


Recombinant protein


The Human Midkine is created as a recombinant protein with N terminal fusion of HisTag. The Human Midkine His-Tagged Fusion Protein, produced in E. coli, is 14.6 kDa protein containing 121 amino acid residues of the human Midkine and 10 additional amino acid residues – HisTag. UniProtKB P21741.

Amino Acid Sequence



E. coli




12% SDS-PAGE separation of Human Midkine
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 5μg/lane
3. non-reduced and non-heated sample, 5μg/lane


Filtered (0,4 μm) and lyophilized in 0.5 mg/mL in 0.05 M phosphate buffer, 0.1 M NaCl, pH 7.2


Add PBS pH 7.2 to prepare a working stock solution of approximately 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 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.


This product is intended for research use only.


Research topic



Midkine (MK, also called neurite growth promoting factor 2, NEGF-2), a product of a retinoic acid responsive gene, is a secreted 13 kDa protein belonging to the family of heparin binding growth/differen­tiation factors. MK shares 45% sequence identity with other member of this family called Pleiotrophin (HB-GAM). Midkine is composed of two domains held together by disulfide linkages. The C-terminally located domain contains two heparin binding sites and is usually responsible for midkine activity. Part of the MK activity is enhanced by dimerization of MK.

Midkine has been found in vertebrates from human to zebrafish and is most strongly expresed in midgestation. In the adult MK expression is restricted. In addition to normal development, MK is also involved in the pathogenesis of diseases e.g. inflammatory diseases, human carcinomas such as esophageal, stomach, colon, pancreatic, thyroid, lung, urinary, hepatocellular, neuroblastoma, glioblastoma, Wilm´s tumor etc. High MK levels are associated with poor prognosis in some type of cancer. The increased expresion in many carcinomas indicates that MK can be applied to the diagnosis of malignancy. Midkine is expressed during the reparative stage of bone fractures, also supresses infection of certain viruses including HIV in target cells. Anti-apoptotic and cell protecting activity of midkine makes it to be a promissing in therapy.

Areas of investigation: Oncology, Inflammatory diseases, Preservation and repair of injured tissues.

Product References (1)


  • Shrivastava DA, Shrivastava DA, Kallianpur DS, Sharma DG, S Tijare DM. Estimation of Serum Midkine in Oral Squamous Cell Carcinoma and Oral Premalignancy. Gulf J Oncolog. 2021 Jan;1(35):21-26. PubMed PMID: 33716209. See more on PubMed
Summary References (12)

References to Midkine

  • Choudhuri R., Zhang, H. T., Donnini, S., Ziche, M. and Bicknell, R.: An angiogenic role for the neurokines midkine and pleiotrophin in tumorigenesis. Cancer Res. 57, 1814–1819. (1997)
  • Ye, C., Qi, M., Fan, Q.-W., Ito, K., Akiyama, S., Kasai, Y., Matsuyama, M., Muramatsu, T. and Kadomatsu, K.: Expression of midkine in the early stage of carcinogenesis in human colorectal cancer. Brit. J. Cancer 79, 179–184. (1999)
  • Konishi, N., Nakamura, M., Nakaoka, S., Hiasa, Y., Cho, M., Uemura, H., Hirao, Y., Muramatsu, T. and Kadomatsu, K.: Immunohistochemical analysis of midkine expression in human prostate carcinoma. Oncology 57,253–257. (1999)
  • Ohta, S., Muramatsu, H., Senda, T., Zou, K., Iwata, H. and Muramatsu, T.: Midkine is expressed during repair of bone fracture and promotes chondrogenesis. J. Bone Miner. Res. 14, 1132–1144. (1999)
  • Ikematsu, S., Yano, A., Aridome, K., Kikuchi, M., Kumai, H., Nagano, H., Okamoto, K., Oda, M., Sakuma, S., Aikou, T., Muramatsu, H., Kadomatsu, K. and Muramatsu, T.: Serum midkine levels are increased in patients with various types of carcinomas. Brit. J. Cancer. 83, 701–706. (2000)
  • Callebaut, C., Nisole, S., Briand, J. P., Krust, B. and Hovanessian, A. G.: Inhibition of HIV infection by the cytokine midkine. Virology 281, 248–264. (2001)
  • Sato, W., Kadomatsu, K., Yuzawa, Y., Muramatsu, H., Hotta, N., Matsuo, S. and Muramatsu T.: Midkine is involved in neutrophil infiltration into the tubulointerstitium in ischemic renal injury. J. Immunol. 167, 3463–3469. (2001)
  • Shimada, H., Nabeya, Y., Okazumi, S., Matsubara, H., Kadomatsu, K., Muramatsu, T., Ikematsu, S., Sakuma, S. and Ochiai, T.: Increased serum midkine concentration as a possible tumor marker in patients with superficial esophageal cancer. Oncol. Rep. 10, 411–414. (2003)
  • Ikematsu, S., Nakagawara, A., Nakamura, Y., Sakuma, S., Wakai, K., Muramatsu, T. and Kadomatsu, K.: Correlation of elevated level of blood midkine with poor prognostic factors of human neuroblastomas. Br. J. Cancer 88, 1522–1526. (2003)
  • Ikematsu, S., Okamoto, K., Yoshida, Y., Oda, M., Sugano-Nagano, H., Ashida, K., Kumai, H., Kadomatsu, K., Muramatsu, H., Muramatsu, T. and Sakuma, S.: High levels of urinary midkine in various cancer patients. Biochem. Biophys. Res. Commun. 306, 329–332. (2003)
  • Maruyama, K., Muramatsu, H., Ishiguro, N., and Muramatsu, T.: Midkine, a heparin-binding growth factor, is fundamentally involved in the pathogenesis of rheumatoid arthritis. Arthritis Rheum. 50, 1420–1429.
  • Obata, Y., Kikuchi, S., Lin, Y., Yagyu, K., Muramatsu, T., Kumai, H.: Serum midkine concentrations and gastric cancer. Cancer Sci. 96, 54 – 56 (2005)
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