Recombinant Human HB-EGF Protein

R&D Systems, part of Bio-Techne | Catalog # 259-HE

R&D Systems, part of Bio-Techne
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Carrier Free
259-HE-050/CF
259-HE-250/CF
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With Carrier
259-HE-050
259-HE-250
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Key Product Details

Source

Sf 21 (baculovirus)

Accession #

Q99075

Conjugate

Unconjugated

Applications

Bioactivity

View all HB-EGF Proteins and Enzymes »

Product Specifications

Source

Spodoptera frugiperda, Sf 21 (baculovirus)-derived human HB-EGF protein
Asp63-Leu148

Purity

>97%, by SDS-PAGE with silver staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Asp63 (major), Gly32, Glu24

Predicted Molecular Mass

9.7 kDa

SDS-PAGE

11-20 kDa, reducing conditions

Activity

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.

Reviewed Applications

Read 1 review rated 5 using 259-HE in the following applications:

Formulation, Preparation and Storage

Carrier Free
What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Carrier: 259-HE
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution Reconstitute at 250 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage 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.
Carrier Free: 259-HE/CF
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 250 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage 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.

Background: HB-EGF

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.

References

  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.

Long Name

Heparin Binding EGF-like Growth Factor

Alternate Names

Dtr, Dts, HBEGF, Hegfl

Entrez Gene IDs

1839 (Human); 15200 (Mouse)

Gene Symbol

HBEGF

UniProt

Q99075

Additional HB-EGF Products

Product Documents for Recombinant Human HB-EGF Protein

Product Datasheets

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Download SDS 259-HE (with carrier)
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Product Specific Notices for Recombinant Human HB-EGF Protein

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