Leucine-rich repeat serine/threonine-protein kinase 2 (LRRK2), partial, human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 904-1450aa. Protein Length: Partial. Tag Info: C-terminal 6xHis-tagged. Target Protein Sequence: VKKKSNSISV GEFYRDAVLQ RCSPNLQRHS NSLGPIFDHE DLLKRKRKIL SSDDSLRSSK LQSHMRHSDS ISSLASEREY ITSLDLSANE LRDIDALSQK CCISVHLEHL EKLELHQNAL TSFPQQLCET LKSLTHLDLH SNKFTSFPSY LLKMSCIANL DVSRNDIGPS VVLDPTVKCP TLKQFNLSYN QLSFVPENLT DVVEKLEQLI LEGNKISGIC SPLRLKELKI LNLSKNHISS LSENFLEACP KVESFSARMN FLAAMPFLPP SMTILKLSQN KFSCIPEAIL NLPHLRSLDM SSNDIQYLPG PAHWKSLNLR ELLFSHNQIS ILDLSEKAYL WSRVEKLHLS HNKLKEIPPE IGCLENLTSL DVSYNLELRS FPNEMGKLSK IWDLPLDELH LNFDFKHIGC KAKDIIRFLQ QRLKKAVPYN RMKLMIVGNT GSGKTTLLQQ LMKTKKSDLG MQSATVGIDV KDWPIQIRDK RKRDLVLNVW DFAGREEFYS THPHFMTQRA LYLAVYDLSK GQAEVDAMKP WLFNIKARAS SSPVILV. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, autophagy, and vesicle trafficking. Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation. Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB35, and RAB43. Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A. Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A. Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization. Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Phosphorylates PRDX3. By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis. Independent of its kinase activity, inhibits the proteosomal degradation of MAPT, thus promoting MAPT oligomerization and secretion. In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity. Reference: "Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology." Zimprich A., Biskup S., Leitner P., Lichtner P., Farrer M., Lincoln S.J., Kachergus J.M., Hulihan M.M., Uitti R.J., Calne D.B., Stoessl A.J., Pfeiffer R.F., Patenge N., Carballo Carbajal I., Vieregge P., Asmus F., Mueller-Myhsok B., Dickson D.W. Gasser T. Neuron 44:601-607(2004). Function: nan