14-536
MAP Kinase 2/Erk2 Protein, inactive, Human, 50 g
Unactive, N-terminal GST-tagged, recombinant human full length MAP Kinase 2, for use in Kinase Assays.
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About This Item
Recommended Products
biological source
human
Quality Level
recombinant
expressed in E. coli
mol wt
Mw 67.8 kDa
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable (kinase)
NCBI accession no.
UniProt accession no.
shipped in
dry ice
General description
N-terminal GST-tagged, recombinant human full length MAP Kinase 2
Product Source: Expressed in E. coli
Application
Research Category
Metabolism
Inflammation & Immunology
Metabolism
Inflammation & Immunology
Research Sub Category
Obesity
Metabolic Disorders
Osteoporosis
Arthritis
Obesity
Metabolic Disorders
Osteoporosis
Arthritis
Biochem/physiol Actions
Protein Target: MAPK2
Target Sub-Family: CMGC
Quality
routinely evaluated by phosphorylation of MBP substrate
Physical form
Glutathione agarose affinity chromatography
Storage and Stability
6 months at -20°C
Other Notes
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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.
signalword
Warning
hcodes
Hazard Classifications
Skin Sens. 1
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Scientific reports, 6, 28260-28260 (2016-06-16)
Although the translational function of tRNA has long been established, extra translational functions of tRNA are still being discovered. We previously developed a computational method to systematically predict new tRNA-protein complexes and experimentally validated six candidate proteins, including the mitogen-activated
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