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Merck

SAB4200808

Sigma-Aldrich

抗 肌球蛋白轻链激酶抗体,小鼠单克隆

clone K36, purified from hybridoma cell culture

别名:

Kinase-related protein (KRP), MLCK, Myosin light chain kinase, Smooth muscle, Telokin, smMLCK

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

mouse

抗體表格

purified from hybridoma cell culture

抗體產品種類

primary antibodies

無性繁殖

K36, monoclonal

形狀

buffered aqueous solution

分子量

~160 kDa

物種活性

bovine, human, mouse, chicken, pig, turkey

包裝

antibody small pack of 25 μL

濃度

~1 mg/mL

技術

immunoblotting: 0.25-0.5 μg/mL using chicken gizzard extract

同型

IgG2b

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

一般說明

Myosin Light Chain Kinase (MLCK) also known as MYLK is a Ca2+/calmodulin dependent myosin light chain phosphorylating agent. This enzyme plays a major role in the phosphorylation of the regulatory light chains of myosin which are essential for the shortening and tension development of smooth muscle cells resulting in smooth muscle contraction. Myosin light chain kinase are widely expressed in many different tissues and cells of eukaryote species. There are two genes mylk1 and mylk2 encoding the MLCK protein, mylk2 is exclusively expressed in skeletal muscle cells.

免疫原

Purified chicken gizzard myosin light chain kinase.

應用

Monoclonal Anti-Myosin Light Chain Kinase recognizes the myosin light chain kinase of smooth muscle and from non-muscle cells such as cultured fibroblasts. Reactivity has been observed with myosin light chain kinase from chicken, turkey, bovine, human, mouseand pig origin. The antibody is recommended to use in various immunological techniques, including Immunoblotting (~160kDa), Immunohistochemistry and immunofluorescence.

外觀

Supplied as a solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as a preservative.

其他說明

This product is for R&D use only, not for drug, household, or other uses.

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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Myosin Light Chain Kinase: A Potential Target for Treatment of Inflammatory Diseases.
Xiong, et al.
Frontiers in Pharmacology, 8, 292-292 (2017)
Renaud Léguillette et al.
American journal of respiratory and critical care medicine, 179(3), 194-204 (2008-11-18)
Airway smooth muscle (SM) of patients with asthma exhibits a greater velocity of shortening (Vmax) than that of normal subjects, and this is thought to contribute to airway hyperresponsiveness. A greater Vmax can result from increased myosin activation. This has
Jeffrey B Wyckoff et al.
Current biology : CB, 16(15), 1515-1523 (2006-08-08)
Tumor cells invading three-dimensional matrices need to remodel the extracellular matrix (ECM) in their path. Many studies have focused on the role of extracellular proteases; however, cells with amoeboid or rounded morphologies are able to invade even when these enzymes
S Topouzis et al.
Developmental biology, 178(2), 430-445 (1996-09-15)
Lineage analysis studies in the avian embryo have identified two types of smooth muscle cells (SMCs) in the tunica media of large elastic arteries; one that originates within the cardiac neural crest and is ectoderm in origin (Ect) and another
Zoe M Goeckeler et al.
The Journal of biological chemistry, 280(38), 33083-33095 (2005-08-02)
This study determined the effects of increased intracellular cAMP and cAMP-dependent protein kinase activation on endothelial cell basal and thrombin-induced isometric tension development. Elevation of cAMP and maximal cAMP-dependent protein kinase activation induced by 10 microm forskolin, 40 microm 3-isobutyl-1-methylxanthine

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