Description
Accession
P34130
Source
Optimized DNA sequence encoding Human Neurotrophin-4 mature chain was expressed in Escherichia Coli.
Molecular weight
Human Neurotrophin-4 is generated by the proteolytic removal of the signal peptide and propeptide, the molecule has a calculated molecular mass of approximately 14 kDa. Recombinant human NT-4 is a disulfide-linked homodimer protein consisting of two 131 amino acid residue subunits, and migrates as an approximately 29 kDa protein under non-reducing and as 14 kDa under reducing conditions in SDS-PAGE.
Purity
>97%, as determined by SDS-PAGE and HPLC
Biological Activity
The ED(50) was determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures, and was found to be in a range of-50 ng/ml.
Protein Sequence
MLPLPSCSLP ILLLFLLPSV PIESQPPPST LPPFLAPEWD LLSPRVVLSR GAPAGPPLLF LLEAGAFRES AGAPANRSRR GVSETAPASR RGELAVCDAV SGWVTDRRTA VDLRGREVEV LGEVPAAGGS PLRQYFFETR CKADNAEEGG PGAGGGGCRG VDRRHWVSEC KAKQSYVRAL TADAQGRVGW RWIRIDTACV CTLLSRTGRA
Endotoxin
Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than.1 ng/µg(1EU/µg).
Presentation
Recombinant NT-4was lyophilized from a.2 μm filtered PBS solution pH7.5.
Reconstitution
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than.1 mg/mL. This solution can then be diluted into other buffers.
Storage
The lyophilized protein is stable for at least years from date of receipt at -20° C. Upon reconstitution, this cytokine can be stored in working aliquots at° -° C for one month, or at -20° C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage
This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.
Molecular function