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Midkine Murine E. coli

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


RBG20097005 5 µg
RBG20097020 20 µg
RBG20097100 100 μg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Midkine (MK) and its functionally-related protein pleiotrophin are heparin-binding neurotrophic factors that signal through the same receptor, known as anaplastic lymphoma kinase (ALK). MK plays an important regulatory role in epithelial-mesenchymal interactions during fetal development and in postnatal lung development. MK chemoattracts embryonic neurons, neutrophils and macrophages, and exerts angiogenic, growth and survival activities during tumorgenesis. Recombinant Murine Midkine is a 13.3 kDa protein containing 120 amino acid residues including five intra-molecular disulfide bonds.

Amino Acid Sequence

VAKKKEKVKKGSECSEWTWGPCTPSSKDCGMGFREGTCGAQTQRVHCKVPCNWKKEFGADCKYKFESWGACDGSTGTKARQGTLKKARYNAQCQETIRVTKPCTSKTKSKTKAKKGKGKD

Source

E. coli

Purity

98%

Biological Activity

Determined by its ability to chemoattract human neutrophils using a concentration range of 10–100 ng/ml.

Endotoxin

Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.

Storage/Expiration

 –20°C

Summary

Research topic

Oncology, Animal studies

Summary

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.

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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