Recombinant Mouse MSK2 Protein

Beta LifeScience SKU/CAT #: BL-0884SG

Recombinant Mouse MSK2 Protein

Beta LifeScience SKU/CAT #: BL-0884SG
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Product Overview

Tag GST
Host Species Mouse
Accession BC012964
Synonym RPS6KA4; RSK-B; RSKB
Background MSK2 or mitogen- and stress-activated protein kinase-2 is a member of the serine/threonine kinases family that contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including CREB1 and c-fos. MSK2 is also known as ribosomal protein S6 kinase 4 (RPS6KA4) that are activated by the mitogen-activated protein kinases ERK1, ERK2, and p38.
Description Recombinant full-length mouse MSK2 was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source Sf9 insect cells
AA Sequence Full Length
Molecular Weight ~114 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Active
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Mouse MSK2 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors.
Subcellular Location Nucleus.
Protein Families Protein kinase superfamily, AGC Ser/Thr protein kinase family, S6 kinase subfamily
Database References

Gene Functions References

  1. regulator of nucleosomal remodelling in the diabetic milieu PMID: 27350436
  2. chromatin modifier, MSK1/2, has a role in suppressing endocrine and promoting acinar differentiation during pancreatic development PMID: 27973548
  3. Accelerated apoptotic death and in vivo turnover of erythrocytes have been found in mice lacking functional MSK1/MSK2. PMID: 26611568
  4. Results suggest that MSK1/2 plays a significant role in the regulation of ischemia-induced progenitor cell proliferation and neurogenesis PMID: 25451279
  5. MSK1/2 knockout results in reduced IL-10 secretion. PMID: 23382072
  6. data reveal a critical role for MSK1/2 as regulators of both basal and activity-dependent progenitor cell proliferation and morphological maturation in the subgranular zone PMID: 23020821
  7. Comparison of the effects of SB-747651A, both in vitro and in cells, demonstrated that SB-747651A exhibited improved selectivity over H89 and Ro 31-8220 and therefore represents a useful tool to study MSK function in cells. PMID: 21970321
  8. MSK1/2 are involved in the activation of feedback mechanisms that dampen oxazolone-induced skin inflammation. PMID: 21166721
  9. These data provide in vivo evidence that MSK1/2 signaling represents a novel tumor-promoting axis in skin carcinogenesis. PMID: 21314333
  10. MSK1/2 regulate pri-miR-212/132 transcription via the phosphorylation of CREB. PMID: 20307261
  11. MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts. PMID: 11909979
  12. findings suggested that MSK1/2 might play a critical role in the survival of lipopolysaccharide-stimulated RAW 264.7 cells PMID: 15681159
  13. correlated to a reduction in the T-Cell Receptor-induced up-regulation of the IL-2 receptor CD25 and a requirement for MSK in IL-2-induced CREB phosphorylation PMID: 17668895

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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