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Merck

L9918

Sigma-Aldrich

Anti- LRRK2 (C-terminal region)

enhanced validation

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

别名:

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

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.44

生物源

rabbit

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous solution

分子量

antigen ~240 kDa

物種活性

rat, mouse, human

加強驗證

recombinant expression
Learn more about Antibody Enhanced Validation

濃度

~1.0 mg/mL

技術

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

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

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

一般說明

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.

特異性

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

應用

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).

生化/生理作用

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.

外觀

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

免責聲明

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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儲存類別代碼

10 - Combustible liquids

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


分析证书(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)
Vasanti S Anand et al.
The FEBS journal, 276(22), 6428-6435 (2009-10-07)
Leucine-rich repeat kinase 2 (LRRK2) is a large, complex, multidomain protein containing kinase and GTPase enzymatic activities and multiple protein-protein interaction domains. Mutations linked to autosomal dominant forms of Parkinson's disease result in amino acid changes throughout the protein and
The R1441C mutation of LRRK2 disrupts GTP hydrolysis
Lewis PA, et al.
Biochemical and biophysical research communications, 357(3), 668-671 (2007)
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)
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)

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