产品名称：Recombinant Human Heparin-binding EGF-like Growth Factor（rHuHB-EGF）

产品价格：

产品介绍：

Synonyms	HBEGF, DT-R
Accession	Q99075
GeneID	1839
Source	Escherichia coli.
Molecular Weight	Approximately 9.7 kDa, a single non-glycosylated polypeptide chain containing 86 amino acids.
Quantity	10μg/50μg/1000μg
AA Sequence	DLQEADLDLL RVTLSSKPQA LATPNKEEHG KRKKKGKGLG KKRDPCLRKY KDFCIHGECK YVKELRAPSC ICHPGYHGER CHGLSL
Purity	> 97 % 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 20 mM PB, pH 7.4, 130 mM NaCl.
Endotoxin	Less than 1 EU/μg of rHuHB-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 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.
SDS-PAGE
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, 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. Human HB-EGF shares about 73 % and 76 % a.a. sequence identity with murine and rat HB-EGF.

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