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Merck
CN

C9619

CAMK1δ, active, GST tagged human

PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

CKLiK, CaMKID, RP11-462F151.1

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About This Item

NACRES:
NA.32
UNSPSC Code:
12352200
Specific activity:
117-159 nmol/min·mg
Assay:
≥70% (SDS-PAGE)
Recombinant:
expressed in baculovirus infected Sf9 cells
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recombinant

expressed in baculovirus infected Sf9 cells

product line

PRECISIO® Kinase

assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

117-159 nmol/min·mg

mol wt

~68 kDa

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Quality Level

Gene Information

human ... CAMK1D(57118)

Biochem/physiol Actions

CAMK1δ or Ca2+/calmodulin-dependent kinase I-like kinase (CKLiK) is activated by Ca2+ and calmodulin and is detected in CD34+-derived neutrophils and eosinophils, as well as in mature peripheral blood granulocytes.CAMK1δ exhibits Ca2+/CaM-dependent activity that is enhanced in vitro by phosphorylation of its Thr180 by CaM-K kinase (CaM-KK)alpha, consistent with detection of CAMK1δ-activating activity in HeLa cells.

Physical form

Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.

Legal Information

PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Regulatory Information

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Sandra Verploegen et al.
Blood, 106(3), 1076-1083 (2005-04-21)
Activation of granulocyte effector functions, such as induction of the respiratory burst and migration, are regulated by a variety of relatively ill-defined signaling pathways. Recently, we identified a novel Ca2+/calmodulin-dependent kinase I-like kinase, CKLiK, which exhibits restricted mRNA expression to
Yumi Ishikawa et al.
FEBS letters, 550(1-3), 57-63 (2003-08-26)
In this report, we cloned a novel calmodulin-kinase (CaM-KIdelta) from HeLa cells and characterized its activation mechanism. CaM-KIdelta exhibits Ca(2+)/CaM-dependent activity that is enhanced (approximately 30-fold) in vitro by phosphorylation of its Thr180 by CaM-K kinase (CaM-KK)alpha, consistent with detection

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