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L9918

Sigma-Aldrich

Anti-LRRK2 (C-terminal region) antibody produced in rabbit

enhanced validation

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-AURA17, Anti-Dardarin, Anti-Leucine-rich repeat protein kinase 2, Anti-PARK8, Anti-RIPK7, Anti-ROCO2

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.44

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~240 kDa

species reactivity

rat, mouse, human

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

concentration

~1.0 mg/mL

technique(s)

western blot: 2-4 μg/mL using HEK-293T cells expressing human LRRK2, and using rat and mouse brain extracts (S2 fraction)

UniProt accession no.

Q5S007

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... LRRK2(120892)
mouse ... Lrrk2(66725)
rat ... Lrrk2(300160)

Related Categories

General description

Leucine-rich repeat protein kinase 2 (LRRK2) comprises multiple domains, including a leucine-rich repeat (LRR) domain, a Roc (Ras of complex proteins) GTPase domain followed by a C-terminal of ROC (COR) domain, a Ser/Thr kinase domain and a C-terminal Trp-Asp-40 (WD40) domain. The N-terminal region (?900 amino acids) contains ankyrin (ANK) repeats. The LRRK2 homologue LRRK1 shares domain structure similarity with LRRK2.

Specificity

Anti-LRRK2 (C-terminal region) antibody is specific for LRRK2 (approx. 240 kDa) in mice, rats and humans.

Application

Anti-LRRK2 (C-terminal region) antibody is suitable for use in western blot (2-4 μg/mL using HEK-293T cells expressing human LRRK2, and using S2 fractions of rat and mouse brain extracts).

Biochem/physiol Actions

LRRK2 is a μLtimeric kinase that also functions as a GTPase. LRRK2 activates a calcium/calmodulin-dependent protein kinase kinase (CaMKK)-β/AMPK signaling pathway and subsequently mediates autophagy. Genetic alterations in LRRK2 cause late-onset Parkinson′s disease . Anti-LRRK2 (C-terminal region) antibody is specific for LRRK2 (approx. 240 kDa) in mice, rats and humans. Staining of the LRRK2 band by immunoblotting is specifically inhibited by the LRRK2 immunizing peptide.
LRRK2 mRNA is expressed throughout the brain predominantly within regions of the basal ganglia that are associated with Parkinson′s disease. The presence of multiple protein interaction domains suggests that in addition to its kinase and GTPase activities, LRRK2 may serve as a scaffold protein for the assembly of multiprotein signaling complex. R1441C mutation has been shown to disrupt GTPase activity. G2019S and R1441C, both associated with increased kinase activity.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Certificates of Analysis (COA)

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Kinase activity of mutant LRRK2 manifests differently in hetero-dimeric vs. homo-dimeric complexes
Leandrou E, et al.
The Biochemical Journal, 476(3), 559-579 (2019)
The R1441C mutation of LRRK2 disrupts GTP hydrolysis
Lewis PA, et al.
Biochemical and biophysical research communications, 357(3), 668-671 (2007)
Crystal structure of the WD40 domain dimer of LRRK2
Zhang P, et al.
Proceedings of the National Academy of Sciences of the USA, 116(5), 1579-1584 (2019)
Expression and localization of Parkinson's disease-associated leucine-rich repeat kinase 2 in the mouse brain
Higashi S, et al.
Journal of Neurochemistry, 100(2), 368-381 (2007)
Patricia Gómez-Suaga et al.
Human molecular genetics, 21(3), 511-525 (2011-10-21)
Mutations in the leucine-rich repeat kinase-2 (LRRK2) gene cause late-onset Parkinson's disease, but its physiological function has remained largely unknown. Here we report that LRRK2 activates a calcium-dependent protein kinase kinase-β (CaMKK-β)/adenosine monophosphate (AMP)-activated protein kinase (AMPK) pathway which is
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