For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 15; NC_000081.6 (91672640..91816124). Location: 15; 15 F1

E Coli

> 95%

Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.

Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.
Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

Manufactured in an ISO 9001:2008 and ISO 13485:2003 Certified Laboratory.

Manufactured in a lab with traceable raw materials. Bulk orders can typically be prepared to the customera??s specifications, please inquire.

Small volumes of LRRK2 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

About the Marker: Effective Size Range: 10kDa to 70kDa.
Protein bands: 10kDa, 14kDa, 18kDa, 22kDa, 26kDa, 33kDa, 44kDa and70kDa.
Double intensity bands: The 26kDa, 18kDa, 10kDa bands are at doubleintensity to make location and size approximation of proteins of interestquick and easy.
Ready-to-use: No need to heat, dilute or add reducing agents before use.

SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)

57.7kDa

leucine-rich repeat kinase 2

leucine-rich repeat serine/threonine-protein kinase 2

Leucine-rich repeat serine/threonine-protein kinase 2

LRRK2_MOUSE

LRRK2: a large multidomain protein kinase with a TKL-type kinase domain, multiple protein-protein interaction domains and a mitochondrial Rho domain (MIRO). May play a role in the etiology of Parkinson disease. May also have GTPase activity. 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. Interacts with PARK2, PRDX3 and TPCN2. Expressed throughout the ***** brain, but at a lower level than in heart and liver. Expressed in the cerebellum, cerebral cortex, medulla, spinal cord occipital pole, frontal lobe, temporal lobe and putamen. Expression is particularly high in brain dopaminoceptive areas. Defects in LRRK2 are the cause of Parkinson disease type 8 (PARK8). A slowly progressive neurodegenerative disorder characterized by bradykinesia, rigidity, resting tremor, postural instability, neuronal loss in the substantia nigra, and the presence of neurofibrillary MAPT (tau)-positive and Lewy bodies in some patients.

Protein type: Kinase, protein; EC 2.7.11.1; Protein kinase, TKL; Protein kinase, Ser/Thr (non-receptor); TKL group; LRRK family

Cellular Component: dendrite cytoplasm; Golgi apparatus; extracellular space; mitochondrion; lysosome; dendrite; terminal button; inclusion body; trans-Golgi network; ribonucleoprotein complex; cytosol; lipid raft; mitochondrial outer membrane; synaptic vesicle; cell soma; membrane; mitochondrial matrix; mitochondrial inner membrane; cytoplasm; synapse; intracellular; cytoplasmic vesicle; endosome; neuron projection; intracellular membrane-bound organelle; endoplasmic reticulum; perikaryon; cell projection; axon; mitochondrial membrane; plasma membrane; cell junction

Molecular Function: tubulin binding; GTPase activity; identical protein binding; clathrin binding; GTP-dependent protein kinase activity; protein homodimerization activity; Rho GTPase binding; GTP binding; nucleotide binding; actin binding; GTPase activator activity; protein kinase activity; MAP kinase kinase activity; transferase activity; protein serine/threonine kinase activity; protein binding; SNARE binding; protein kinase A binding; transferase activity, transferring phosphorus-containing groups; syntaxin-1 binding; kinase activity; glycoprotein binding; ATP binding

Biological Process: regulation of synaptic transmission, glutamatergic; activation of MAPKK activity; positive regulation of protein binding; activation of MAPK activity; protein amino acid autophosphorylation; regulation of neuron maturation; determination of ***** life span; protein amino acid phosphorylation; tangential migration from the subventricular zone to the olfactory bulb; negative regulation of protein amino acid phosphorylation; small GTPase mediated signal transduction; regulation of dopamine receptor signaling pathway; cell differentiation; negative regulation of protein binding; regulation of mitochondrial depolarization; Golgi organization and biogenesis; positive regulation of autophagy; neuromuscular junction development; positive regulation of dopamine receptor signaling pathway; olfactory bulb development; MAPKKK cascade; peptidyl-threonine phosphorylation; endocytosis; regulation of locomotion; positive regulation of programmed cell death; peptidyl-serine phosphorylation; regulation of membrane potential; positive regulation of protein ubiquitination; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; intracellular distribution of mitochondria; autophagy; positive regulation of protein amino acid phosphorylation; response to oxidative stress; regulation of excitatory postsynaptic membrane potential; phosphorylation; neurite morphogenesis; positive regulation of GTPase activity

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