Recombinant Human HB-EGF Protein


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Recombinant Human HB-EGF Protein Summary

Details of Functionality
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Rubin, J.S. et al. (1991) Proc. Natl. Acad. Sci. USA 88:415. The ED50 for this effect is 0.15-0.75 ng/mL.
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human HB-EGF protein
Accession #
N-terminal Sequence
Asp63 (major), Gly32, Glu24
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE with silver staining
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
9.7 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
11-20 kDa, reducing conditions
Read Publications using
259-HE in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>97%, by SDS-PAGE with silver staining
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human HB-EGF Protein

  • diphtheria toxin receptor (heparin-binding epidermal growth factor-like growthfactor)
  • Dtr
  • DTRHEGFLdiphtheria toxin receptor (heparin-binding EGF-like growth factor)
  • Dts
  • DTSF
  • HB-EGF
  • Hegfl
  • heparin-binding EGF-like growth factor
  • heparin-binding epidermal growth factor
  • proheparin-binding EGF-like growth factor


Human HB-EGF (Heparin-Binding EGF-like growth factor) is a 12-16 kDa member of the EGF family of peptide growth factors (1-3). Also known as the DTR (diphtheria toxin receptor), it is further classified as a group 2 ErbB ligand based on its ability to activate both the EGF/ErbB1 and ErbB4 receptors (4, 5). HB-EGF is synthesized as a 208 amino acid (aa) type I transmembrane preproprecursor (1, 6). It contains a 19 aa signal sequence, a 43 aa prosegment, an 86 aa mature region (aa 63-148), an 11 aa juxtamembrane cleavage peptide, a 24 aa transmembrane segment, and a 25 aa cytoplasmic tail (aa 184-208). As an integral membrane protein, HB-EGF is expressed as a 19-27 kDa protein in mammalian cells (7-9). The variability in molecular weight (MW) is attributed to heterogeneity in glycosylation and/or the utilization of multiple proteolytic cleavage sites during maturation. Mature HB-EGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. It possesses an EGF-like domain between aa 104-144, and a heparin-binding motif between aa 93‑113. Although the aa range for "mature" HB-EGF is typically stated to be Asp63-Leu148, potential N-terminal start (cleavage) sites also exist at Gly32, Arg73, Val74, Ser77 and Ala82 (8, 10-12). Thus, differential processing (in part) likely accounts for the 16-23 kDa range in MW noted for mammalian-derived mature HB-EGF. Proteases suggested to contribute to HB-EGF processing include TACE, MMP-3 and -7, ADAM-17 and ADAM-12 (11, 13-16). When expressed recombinantly in E.coli, HB-EGF (aa 73-148) runs at 14 kDa in SDS-PAGE; when expressed in Baculovirus, HB-EGF (aa 63-148, 77-148 and 32-148) runs at 18 kDa, 15 kDa, and 19 kDa respectively (8, 12, 17). Over aa 63-148, human HB-EGF- shares 76% and 73% aa sequence identity with rat and mouse HB-EGF, respectively (1, 18). Cells known to express HB-EGF include bronchial epithelium (19), visceral and vascular smooth muscle (20, 21), CD4+ T cells (22), cardiac muscle (23), glomerular podocytes (24), keratinocytes (13) and IL-10-secreting regulatory macrophages (25). As noted earlier, HB-EGF is known to bind to both 170 kDa EGFR and 180 kDa ErbB4, and through heterodimerization, ErbB2 (13, 26). Activity associated with ErbB4 binding appears to be limited to non-mitogenic actions, while EGFR binding induces both mitogenic and non-mitogenic activity.
  1. Higashiyama, S et al. (1991) Science 251:936.
  2. Schneider, MR & E. Wolf (2009) J. Cell. Physiol. 218:460.
  3. G.V. Sherbet (2011) The Epidermal Growth Factor (EGF) Family in Growth Factors and Their Receptors in Cell Differentiation, Cancer and Cancer Therapy, Pages 173-198. Elsevier, NY.
  4. Iwamoto, R & E. Mekada (2000) Cytokine Growth Factor Rev. 11:335.
  5. Miyata, K. et al. (2012) Anticancer Res. 32:2347.
  6. SwissProt:Q99075.
  7. Raab, G. et al. (1994) Biochem. Biophys. Res. Commun. 204:592.
  8. Nakagawa, T. et al. (1996) J. Biol. Chem. 271:30858.
  9. Higashiyama, S. et al. (1995) J. Cell Biol. 128:929.
  10. Higashiyama, S. et al. (1992) J. Biol. Chem. 267:6205.
  11. Hinkle, C.L. et al. (2004) J. Biol. Chem. 279:24179.
  12. Ono, M. et al. (1994) J. Biol. Chem. 269:31315.
  13. Nanba, D. & S. Higashiyama (2004) Cytokine Growth Factor Rev. 15:13.
  14. Cheng, K. et al. (2007) Biochem. Pharmacol. 73:1001.
  15. Suzuki, M. et al. (1997) J. Biol. Chem. 272:31730.
  16. Asakura, M. et al. (2002) Nat. Med. 8:35.
  17. Marikovsky, M. et al. (1993) Proc. Natl. Acad. Sci. USA 90:3889.
  18. Abraham, J.A. et al. (1993) Biochem. Biophys. Res. Commun. 190:125.
  19. Tschumperlin, D.J. et al. (2004) Nature 429:83.
  20. Park, J.M. et al. (1998) Am. J. Physiol. 275:C1247.
  21. Miyagawa, J. et al. (1995) J. Clin. Invest. 95:404.
  22. Blotnick, S. et al. (1994) Proc. Natl. Acad. Sci. USA 91:2890.
  23. Iwamoto, R. et al. (2003) Proc. Natl. Acad. Sci. USA 100:3221.
  24. Bollee, G. et al. (2011) Nat. Med. 17:1242.
  25. Edwards, J.P. et al. (2009) J. Immunol. 182:1929.
  26. Elenius, K. et al. (1997) EMBO J. 16:1268.

Publications for HB-EGF (259-HE)(67)

We have publications tested in 5 confirmed species: Human, Mouse, Fish - Prionace glauca (Blue Shark), N/A, Zebrafish.

We have publications tested in 8 applications: Bioassay, Cell Culture, ELISA (Standard), ELISA Development, ELISA Standard, In Vivo, Stimulation, Surface Plasmon Resonance.

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ELISA (Standard)
ELISA Development
ELISA Standard
In Vivo
Surface Plasmon Resonance
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Fish - Prionace glauca (Blue Shark)
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Showing Publications 1 - 10 of 67. Show All 67 Publications.
Publications using 259-HE Applications Species
Qin, Y;Xu, Y;Yi, H;Shi, L;Wang, X;Wang, W;Li, F; Unique structural characteristics and biological activities of heparan sulfate isolated from the mantle of the scallop Chlamys farreri Carbohydrate polymers 2024-01-15 [PMID: 37985034] (Surface Plasmon Resonance, N/A) Surface Plasmon Resonance N/A
Cigliola, V;Shoffner, A;Lee, N;Ou, J;Gonzalez, TJ;Hoque, J;Becker, CJ;Han, Y;Shen, G;Faw, TD;Abd-El-Barr, MM;Varghese, S;Asokan, A;Poss, KD; Spinal cord repair is modulated by the neurogenic factor Hb-egf under direction of a regeneration-associated enhancer Nature communications 2023-08-11 [PMID: 37567873] (In Vivo, Zebrafish) In Vivo Zebrafish
Baldelli, A;Koivisto, L;Oguzlu, H;Guo, Y;Häkkinen, L;Pratap-Singh, A;Larjava, H; Spray-dried microparticles of encapsulated gefitinib for slow-release localized treatment of periodontal disease International journal of pharmaceutics 2023-06-24 [PMID: 37364780] (Bioassay, Human) Bioassay Human
EF Cohn, BLL Clayton, M Madhavan, S Yacoub, Y Federov, K Paul-Fried, TJ Shafer, PJ Tesar Pervasive environmental chemicals impair oligodendrocyte development bioRxiv : the preprint server for biology, 2023-02-12;0(0):. 2023-02-12 [PMID: 36798415] (Bioassay, Mouse) Bioassay Mouse
ALM Caldwell, L Sancho, J Deng, A Bosworth, A Miglietta, JK Diedrich, MN Shokhirev, NJ Allen Aberrant astrocyte protein secretion contributes to altered neuronal development in multiple models of neurodevelopmental disorders Nature Neuroscience, 2022-08-30;25(9):1163-1178. 2022-08-30 [PMID: 36042312] (Bioassay, Mouse) Bioassay Mouse
Y Tang, DJ Kwiatkowsk, EP Henske Midkine expression by stem-like tumor cells drives persistence to mTOR inhibition and an immune-suppressive microenvironment Nature Communications, 2022-08-26;13(1):5018. 2022-08-26 [PMID: 36028490] (Bioassay, Mouse) Bioassay Mouse
S Martin, KC Allan, O Pinkard, T Sweet, PJ Tesar, J Coller Oligodendrocyte differentiation alters tRNA modifications and codon optimality-mediated mRNA decay Nature Communications, 2022-08-25;13(1):5003. 2022-08-25 [PMID: 36008413] (Bioassay, Mouse) Bioassay Mouse
S Gnosa, L Puig-Blasc, KB Piotrowski, ML Freiberg, S Savickas, DH Madsen, U Auf dem Ke, P Kronqvist, M Kveiborg ADAM17-mediated EGFR ligand shedding directs macrophage promoted cancer cell invasion JCI Insight, 2022-09-22;0(0):. 2022-09-22 [PMID: 35998057] (Stimulation, Human) Stimulation Human
G Guo, K Gong, N Beckley, Y Zhang, X Yang, R Chkheidze, KJ Hatanpaa, T Garzon-Muv, P Koduru, A Nayab, J Jenks, AA Sathe, Y Liu, C Xing, SY Wu, CM Chiang, B Mukherjee, S Burma, B Wohlfeld, T Patel, B Mickey, K Abdullah, M Youssef, E Pan, DE Gerber, S Tian, JN Sarkaria, SK McBrayer, D Zhao, AA Habib EGFR ligand shifts the role of EGFR from oncogene to tumour suppressor in EGFR-amplified glioblastoma by suppressing invasion through BIN3 upregulation Nature Cell Biology, 2022-08-01;24(8):1291-1305. 2022-08-01 [PMID: 35915159] (Human) Human
MC Beer, H Kuhrt, L Kohen, P Wiedemann, A Bringmann, M Hollborn Kir4.2 Potassium Channels in Retinal Pigment Epithelial Cells In Vitro: Contribution to Cell Viability and Proliferation, and Down-Regulation by Vascular Endothelial Growth Factor Biomolecules, 2022-06-18;12(6):. 2022-06-18 [PMID: 35740973] (Bioassay, Human) Bioassay Human
Show All 67 Publications.

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Gene Symbol HBEGF