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MilliporeSigma

SRP5282

Sigma-Aldrich

ERK1, active, GST tagged human

PRECISIO®, recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Sinónimos:

HS44KDAP, HUMKER1A, MAPK3, MGC20180, P44ERK1, P44MAPK, PRKM3

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About This Item

Número de CAS:
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

product line

PRECISIO®

assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

672-1008 nmol/min·mg

mol wt

~72 kDa

NCBI accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... MAPK3(5595)

General description

ERK1 is a protein serine/threonine kinase that is a member of the extracellular signal-regulated kinases (ERKs), also known as mitogen-activated protein kinase 3 (MAPK3) which are activated in response to numerous growth factors and cytokines. ERK1 is ubiquitously distributed in tissues with the highest expression in heart, brain and spinal cord. Activated ERK1 translocates into the nucleus where it phosphorylates various transcription factors (e.g., Elk-1, c-Myc, c-Jun, c-Fos, and C/EBP beta). ERK pathway is necessary for experience-dependent plasticity and for long-term potentiation of synaptic transmission in the developing visual cortex. ERK activation affects the axonal growth by phosphorylation of microtubule-associated proteins and neurofilaments.

Physical form

Supplied in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10 mM glutathione, 0.1 mM EDTA, 0.25 mM DTT, 0.1 mM PMSF, 25% glycerol.

Preparation Note

After opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles.

Legal Information

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Manas Seal et al.
The journal of physical chemistry. B, 125(47), 12947-12957 (2021-11-18)
Knowledge about the structural and dynamic properties of proteins that form membrane-less organelles in cells via liquid-liquid phase separation (LLPS) is required for understanding the process at a molecular level. We used spin labeling and electron paramagnetic resonance (EPR) spectroscopy

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