Recombinant Rat Heparin-binding EGF-like Growth Factor

Synonyms HBEGF, DT-R

Accession Q06175

GeneID 25433

Source Escherichia coli.

Molecular Weight Approximately 9.7 kDa, a single non-glycosylated polypeptide chain containing 86 amino acids.

Quantity 10µg/50µg/1mg

AA Sequence DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL

Purity > 95 % by SDS-PAGE and HPLC analyses.

Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.

Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, 300 mM NaCl, pH 7.4, 5 % trehalose.

Endotoxin Less than 1 EU/μg of rRtHB-EGF as determined by LAL method.

Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

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.

Usage This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

Reference 1. Jin K, Mao XO, Sun Y, et al. 2002. J Neurosci. 22:5365-73.

2. Higashiyama S, Abraham JA, Miller J, et al. 1991. Science. 251:936-9.

Background Heparin-binding epidermal growth factor (HB-EGF)-like growth factor (EGF) is found in cerebral neurons. Its expression is increased after hypoxic or ischemic injury, which also stimulates neurogenesis. HB-EGF has been implicated as a participant in a variety of normal physiological processes such as blastocyst implantation and wound healing, and in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. HB-EGF is an 87 amino acid mitogenic and chemotactic glycoprotein containing an EGF-like domain with six conserved cysteine residues. Rat HB-EGF shares about 76 % a.a. sequence identity with human HB-EGF.