Millipore Sigma Vibrant Logo
Attention: We have moved. Merck Millipore products are no longer available for purchase on MerckMillipore.com.Learn More

PF078 Heparin Binding Epidermal Growth Factor, Human, Recombinant, S. frugiperda

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: HB-EGF

View Products on Sigmaaldrich.com
PF078
  
Purchase on Sigma-Aldrich

Overview

Replacement Information

Key Spec Table

Purity
≥97% by SDS-PAGE
Description
OverviewRecombinant, human heparin binding epidermal growth factor expressed in S. frugiperda insect cells. The mature HB-EGF is generated by the removal of the 62 amino acid (~9.5 kDa) signal. Protein is heterogeneously O-glycosylated and migrates as an ~12 kDa protein in SDS-PAGE. Titrate the protein for optimal results in individual systems.
Catalogue NumberPF078
Brand Family Calbiochem®
SynonymsHB-EGF
References
ReferencesDavis-Fleischer, K.M. and Besner, G.E. 1998. Front. Biosci. 3, D288.
Ouchi, N., et al. 1997. Biochem. J. 328, 923.
Raab, G. and Klagsbrun, M. 1997. Biochim. Biophys. Acta 1333, F179.
Suzuki, M., et al. 1997. J. Biol. Chem. 272, 31730.
Nakata, A., et al. 1996. Circulation 94, 2778.
Miyagawa, J., et al. 1995. J. Clin. Invest. 95, 404.
Higashiyama, S., et al. 1991. Science 251, 936.
Product Information
FormSolid
FormulationLyophilized from a sterile-filtered PBS solution, 50 µg of BSA/µg of cytokine, pH 7.4.
Quality LevelMQ100
Applications
Data setup Error. Pagelet <collection_feature_application_id-PROLIF> not found.
Application NotesProliferation studies
Biological Information
Biological activityEC₅₀ of 2-5 ng/ml as measured by its ability to stimulate ³H-thymidine incorporation in the EGF-responsive fibroblast cell line, Balb/3T3
Purity≥97% by SDS-PAGE
Physicochemical Information
ContaminantsEndotoxins: ≤1 EU per µg cytokine
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage -20°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
PF078 0

Documentation

Heparin Binding Epidermal Growth Factor, Human, Recombinant, S. frugiperda SDS

Title

Safety Data Sheet (SDS) 

Heparin Binding Epidermal Growth Factor, Human, Recombinant, S. frugiperda Certificates of Analysis

TitleLot Number
PF078

References

Reference overview
Davis-Fleischer, K.M. and Besner, G.E. 1998. Front. Biosci. 3, D288.
Ouchi, N., et al. 1997. Biochem. J. 328, 923.
Raab, G. and Klagsbrun, M. 1997. Biochim. Biophys. Acta 1333, F179.
Suzuki, M., et al. 1997. J. Biol. Chem. 272, 31730.
Nakata, A., et al. 1996. Circulation 94, 2778.
Miyagawa, J., et al. 1995. J. Clin. Invest. 95, 404.
Higashiyama, S., et al. 1991. Science 251, 936.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision16-September-2008 RFH
SynonymsHB-EGF
ApplicationProliferation studies
DescriptionRecombinant, human heparin binding epidermal growth factor expressed in S. frugiperda insect cells. The mature HB-EGF is a human recombinant protein whose DNA sequence encoding the N-terminal 148 amino acid residues of human HB-EGF precursor was expressed in Sf 21 insect cells using a baculovirus expression system. The mature recombinant protein (86 amino acids) generated by the removal of the 62 amino acid residue signal and propeptide has a predicted molecular mass of ~9.5 kDa. The recombinant protein is heterogeneously O-glycosylated and migrates as an ~12 kDa protein in SDS-PAGE. Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a ~22 kDa O-glycosylated protein that is a potent mitogen and chemoattractant for vascular smooth muscle cells, fibroblasts, and epithelial cells but not endothelial cells. The natural protein has an apparent molecular mass of ~19-23 kDa and exists in multiple forms as a result of heterogeneous O-glycosylation and/or N-terminal truncation. HB-EGF is synthesized as a membrane-anchored precursor (proHB-EGF) that is proteolytically cleaved to release the soluble mature growth factor. The two forms are active as juxtacrine and paracrine/autocrine growth factors respectively. Recent studies show MMP-3 as one of the enzymes that cleaves HB-EGF implicating a role for MMP-3 in the regulation of HB-EGF from being a juxtacrine to a paracrine/autocrine factor. HB-EGF activates two EGF receptor subtypes, HER1/ErbB1, and HER4 and binds to heparan sulfate proteoglycan. The proHB-EGF is postulated as the high affinity receptor for diphtheria toxin (DT). Recent evidence suggests that the coexpression of proHB-EGF and CD9 on macrophages may strongly promote the development of atherosclerosis by a juxtacrine mechanism. Transcription of HB-EGF can be induced in vascular endothelial cells as well as aortic smooth muscle cells which may also play an important role in the pathogenesis of atherosclerosis. Useful for proliferation studies.
FormSolid
FormulationLyophilized from a sterile-filtered PBS solution, 50 µg of BSA/µg of cytokine, pH 7.4.
Purity≥97% by SDS-PAGE
ContaminantsEndotoxins: ≤1 EU per µg cytokine
Biological activityEC₅₀ of 2-5 ng/ml as measured by its ability to stimulate ³H-thymidine incorporation in the EGF-responsive fibroblast cell line, Balb/3T3
SolubilityReconstitute in PBS to ≥1 µg/ml containing ≥0.1%HSA or BSA.
Storage Avoid freeze/thaw
-20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Toxicity Standard Handling
ReferencesDavis-Fleischer, K.M. and Besner, G.E. 1998. Front. Biosci. 3, D288.
Ouchi, N., et al. 1997. Biochem. J. 328, 923.
Raab, G. and Klagsbrun, M. 1997. Biochim. Biophys. Acta 1333, F179.
Suzuki, M., et al. 1997. J. Biol. Chem. 272, 31730.
Nakata, A., et al. 1996. Circulation 94, 2778.
Miyagawa, J., et al. 1995. J. Clin. Invest. 95, 404.
Higashiyama, S., et al. 1991. Science 251, 936.