APP Recombinant Protein
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| Amount : | 20 µg |
| Purification : | Greater than 85.0% as determined by SDS-PAGE. |
| Content : | APP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT. |
| Storage condition : | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. |
| AA sequence : | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSLEVP TDGNAGLLAE PQIAMFCGRL NMHMNVQNGK WDSDPSGTKT CIDTKEGILQ YCQEVYPELQ ITNVVEANQP VTIQNWCKRG RKQCKTHPHF VIPYRCLVGE FVSDALLVPD KCKFLHQERM DVCETHLHWH TVAKETCSEK STNLHDYGML LPCGIDKFRG VEFVCCPLAE ESDNVDSADA EEDDSDVWWG GADTDYADGS EDKVVEVAEE EEVAEVEEEE ADDDEDDEDG DEVEEEAEEP YEEATERTTS IATTTTTTTE SVEEVVRE. |
| Alternative Name : | Amyloid beta A4 protein, ABPP, APPI, APP, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, APP, A4, AD1, AAA, PN2, ABETA, CTFgamma. |
Source : Escherichia Coli.
APP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (18-289 a.a) and having a molecular mass of 34.7kDa (Molecular size on SDS-PAGE will appear higher).APP is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Amyloid beta A4 protein (APP) functions as a cell surface receptor and transmembrane precursor protein which is cleaved by secretases to form a number of peptides. A number of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to stimulate transcriptional activation, whereas others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. APP gene mutations are implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy).
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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