map-1

Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. MeTAP1 Protein, Mycobacterium tuberculosis, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 32.9 kDa and the accession number is P9WK20.

Mitogen-Activated Protein Kinase Scaffold Protein 1 (MAPKSP1) was identified as an interacting protein that belongs to the LAMTOR3 family. MAPKSP1 restricted to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1 MEK1, MAP kinase MAPK3 ERK1, and MAP kinase MAPK1 ERK2. MAPKSP1 interacts with MAP2K1 MEK1 and MAPK2 and enhances the activation of MAPK2, and thus is thought to function as an adaptor to enhance the efficiency of the MAP kinase cascade.

The translational suppressor eIF4E binding protein-1, 4E-BP1 functions as a key regulator in cellular growth, differentiation, apoptosis and survival. The Eif4ebp1 gene, encoding 4E-BP1, is a direct target of a transcription factor activating transcription factor-4 (ATF4), a master regulator of gene expression in stress responses. 4E-BP1 is characterized by its capacity to bind specifically to eIF4E and inhibit its interaction with eIF4G. Phosphorylation of 4E-BP1 regulates eIF4E availability, and therefore, cap-dependent translation, in cell stress. Binding of eIF4E to eIF4G is inhibited in a competitive manner by 4E-BP1. Phosphorylation of 4E-BP1 decreases the affinity of this protein for eIF4E, thus favouring the binding of eIF4G and enhancing translation. 4E-BP1 is important for beta-cell survival under endoplasmic reticulum (ER) stress. 4E-BP1 mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. Recently, 4E-BP1 was found to be a key factor, which converges several oncogenic signals, phosphorylates the molecules, and drives the downstream proliferative signals. Recent studies showed that high expression of phosphorylated 4E-BP-1 (p-4E-BP1) is associated with poor prognosis, tumor progression, or nodal metastasis in different human cancers.

Mitogen-activated protein kinase kinase kinase 8, also known as Cancer Osaka thyroid oncogene, Proto-oncogene c-Cot, Serine threonine-protein kinase cot, Tumor progression locus 2 and MAP3K8, is a cytoplasm protein that belongs to the protein kinase superfamily, STE Ser Thr protein kinase family and MAP kinase kinase kinase subfamily. MAP3K8 is expressed in several normal tissues and human tumor-derived cell lines. Isoform 1 of MAP3K8 is activated specifically during the S and G2 M phases of the cell cycle. MAP3K8 is required for TLR4 activation of the MEK ERK pathway. It can activate NF-kappa-B 1 by stimulating proteasome-mediated proteolysis of NF-kappa-B 1 p15. MAP3K8 plays a role in the cell cycle. The longer form has some transforming activity, although it is much weaker than the activated cot oncoprotein. MAP3K8 oncogene linked to human endometrial carcinoma suggesting that it may be another molecule involved in human endometrial cancer. MAP3K8 may also be an important mediator of intracellular mechanotransduction in human bone marrow-derived mesenchymal stem cells (MSCs).

MPK5 Protein, Japonica rice, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 48.0 kDa and the accession number is Q10N20.

MAPK14 contains 1 protein kinase domain and belongs to the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation, and development. MAPK14 can be detected in the brain, heart, placenta, pancreas, and skeletal muscle and it is expressed to a lesser extent in the lung, liver, and kidney. MAPK14 is activated by various environmental stresses and proinflammatory cytokines. The activation requires its phosphorylation by MAP kinase kinases (MKKs), or its autophosphorylation triggered by the interaction of MAP3K7IP1 TAB1 protein with MAPK14. The substrates of p38 alpha include transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which suggest the roles of p38 alpha in stress-related transcription and cell cycle regulation, as well as in genotoxic stress response. In response to activation by environmental stress, pro-inflammatory cytokines, and lipopolysaccharide, MAPK14 phosphorylates some transcription factors, such as ELK1 and ATF2, and several downstream kinases, such as MAPKAPK2 and MAPKAPK5. MAPK14 plays a critical role in the production of some cytokines, for example, IL-6. It may play a role in the stabilization of EPO mRNA during hypoxic stress. Isoform Mxi2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2.

MAPKAPK5 contains 1 protein kinase domain and belongs to the protein kinase superfamily, CAMK Ser Thr protein kinase family. MAPKAPK5 has significant sequence homology to mitogen-activated protein kinase (MAPK)-activated protein kinase (MAPKAPK). It is widely distributed. MAPKAPK5 can be phosphorylated by an extracellular-regulated kinase (ERK), and p38 kinase but not by c-jun N-terminal kinase (JNK)in vitro. Recombinant GST-MAPKAPK5 protein can phosphorylate a peptide derived from the regulatory light chain of myosin II. Phosphorylation of MAPKAPK5 by ERK and p38 kinase increased its activity by 9 and 15 fold respectively. Taken together, these data suggest that MAPKAPK5 is a novel in vitro substrate for ERK and p38 kinase. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1 ERK, MAPK14 p38-alpha, and MAPK11 p38-beta. MAPKAPK5 also mediates stress-induced small heat shock protein 27 phosphorylation.

Dual specificity mitogen-activated protein kinase kinase 4, also known as MAP kinase kinase 4, MAPKK4, JNK-activating kinase 1, MAPK ERK kinase 4, SAPK ERK kinase 1, c-Jun N-terminal kinase kinase 1, JNKK, and MAP2K4, is a protein that belongs to the protein kinase superfamily, STE Ser Thr protein kinase family and MAP kinase kinase subfamily. MAP2K4 JNKK1 is a protein kinase that is a direct activator of MAP kinases in response to various environmental stresses or mitogenic stimuli. MAP2K4 JNKK1 has been shown to activate MAPK8 JNK1, MAPK9 JNK2, and MAPK14 p38, but not MAPK1 ERK2 or MAPK3 ERK1. MAP2K4 JNKK1 is phosphorylated, and thus activated by MAP3K1 MEKK. The stress-activated protein kinase (SAPK) pathways represent phosphorylation cascades that convey pro-apoptotic signals. The mitogen-activated protein kinase kinase (MAPKK) homolog MAP2K4 ( MKK4, SEK, JNKK1 ) is a centrally-placed mediator of the SAPK pathways.

MAPKAPK2 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli with N-10xHis, C-Myc. The accession number is P49138.

Serine threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1 ERK2 and MAPK3 ERK1 are the 2 MAPKs which play an important role in the MAPK ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG SCF. Depending on the cellular context, the MAPK ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1 RSK1, RPS6KA3 RSK2, RPS6KA2 RSK3, RPS6KA6 RSK4, SYK, MKNK1 MNK1, MKNK2 MNK2, RPS6KA5 MSK1, RPS6KA4 MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade.

MKNK1 Protein, Human, Recombinant (His) is expressed in E. coli with C-6xHis. The accession number is Q9BUB5.

Phosphoinositide-3-kinase-interacting protein 1(PIK3IP1) is an enzyme that in humans is encoded by the PIK3IP1 gene.It is a negative regulator of phosphatidylinositol-3-kinase (PI3K), suppresses the development of hepatocellular carcinoma. The gene encoding PIK3IP1 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.

ERK2 Protein, Mouse, Recombinant (His & GST) is expressed in Baculovirus insect cells with His and GST tag. The predicted molecular weight is 69.1 kDa and the accession number is P63085.

Inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a reduction in its DNA-binding activity. Inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells. Can also induce activation of MAP kinase p38 and c-Jun N-terminal kinase (JNK).

Mouse Interleukin 33 (IL-33) is a 30 kDa proinflammatory cytokine which may also regulates gene transcription in producer cells. IL-33 is constitutively expressed in smooth muscle and airway epithelia. IL-33 was identified based on sequence and structural homology with IL-1 family cytokines. It is up‑regulated in arterial smooth muscle, dermal fibroblasts, and keratinocytes following IL-1 alpha or IL‑1 beta stimulation. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1. BindingIL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces the expression of IL-4, IL-5, IL-13 and also leads to severe pathological changes in mucosal organs.

Interleukin-33 (IL-33) belongs to the IL-1 superfamily. IL33 is highly expressed in endothelial venules found in tonsils, Peyer patches and mesenteric lymph nodes, but almost undetectable in placenta. IL33 induces the production of T helper-2 (Th2)-associated cytokines. IL-33 is a cytokine that mediates its biological effects by binding to and signals through IL1RL1 ST2 and IL-1 Receptor Accessory Protein (IL1RAP), activating intracellular molecules in the NF-κB and MAP kinase signaling pathways that drive production of type 2 cytokines from polarized Th2 cells.

MAPK14 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 48.6 kDa and the accession number is P47811.

Dual specific phosphatase 14 MAP-kinase phophatase-6 (DUSP14 MKP6) is a member of Dual-specificity phosphatases that is a subclass of protein tyrosine phosphatases (PTP) families that can dephosphorylate bothe phosphotyrosine and phosphoserine phosphothreonine residues in substrates. Unlike many other DUSPs, DUSP14 only contains a catalytic domain within the C-terminal region. In signal transduction, DUSP14 has been considered as negative regulator of the mitogen-activated protein kinase (MAPK) extracellular signal-regulated kinase 1 2 (ERK 1 2) pathway. DUSP14 phosphatase activity has been confirmed to be inhibited by PTP inhibitor Ⅳ. PTP inhibitor binds to the catalytic site of DUSP14. PTP inhibitor Ⅳ effectively and specifically inhibited DUSP14-mediated dephosphorylation of JNK, a member of the mitogen-activated protein kinase (MAPK) family through dephosphorylation of both the Ser Thr and Tyr residues of MAPKs.

ERK2 Protein, Human, Recombinant (GST) is expressed in Baculovirus insect cells with GST tag. The predicted molecular weight is 67 kDa and the accession number is P28482-1.

Nemo-like kinase contains 1 protein kinase domain and belongs to the protein kinase superfamily, CMGC Ser Thr protein kinase family, and MAP kinase subfamily. It also contains a TQE activation loop motif in which autophosphorylation of the threonine residue (Thr-298) is sufficient for kinase activation. As a serine threonine-protein kinase, Nemo-like kinase regulates some transcription factors with key roles in cell fate determination. It is a positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7 TAK1, and HIPK2. Activation of this pathway causes binding to and phosphorylation of the histone methyltransferase SETDB1. The NLK-SETDB1 complex subsequently interacts with PPARG, leading to methylation of PPARG target promoters at histone H3K9 and transcriptional silencing. The resulting loss of PPARG target gene transcription inhibits adipogenesis and promotes osteoblastogenesis in mesenchymal stem cells (MSCs). Nemo-like kinase also is a negative regulator of the canonical Wnt beta-catenin signaling pathway.

MFI2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 77.47 kDa and the accession number is P08582-1.

JNK1 Protein, Human, Recombinant (His) is expressed in Baculovirus Insect Cells with N-6xHis. The accession number is P45983.

MAPKAP1 Protein, Human, Recombinant (His) is expressed in E. coli with C-6xHis. The accession number is Q9BPZ7.