Recombinant Human Mitogen-Activated Protein Kinase 3 (MAPK3) Protein (His)

Name: Recombinant Human Mitogen-Activated Protein Kinase 3 (MAPK3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03137P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MAPK3.

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Product Overview

Description	Recombinant Human Mitogen-Activated Protein Kinase 3 (MAPK3) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P27361
Target Symbol	MAPK3
Synonyms	ERK 1; ERK-1; ERK1; ERT 2; ERT2; Extracellular Signal Regulated Kinase 1; Extracellular signal related kinase 1; Extracellular signal-regulated kinase 1; HGNC6877; HS44KDAP; HUMKER1A; Insulin Stimulated MAP2 Kinase; Insulin-stimulated MAP2 kinase; MAP kinase 1; MAP kinase 3; MAP Kinase; MAP kinase isoform p44; MAPK 1; MAPK 3; MAPK; MAPK1; Mapk3; MGC20180; Microtubule Associated Protein 2 Kinase; Microtubule-associated protein 2 kinase; Mitogen Activated Protein Kinase 3; Mitogen-activated protein kinase 1; Mitogen-activated protein kinase 3; MK03_HUMAN; OTTHUMP00000174538; OTTHUMP00000174541; p44 ERK1; p44 MAPK; p44-ERK1; p44-MAPK; P44ERK1; P44MAPK; PRKM 3; PRKM3 ; Protein Kinase Mitogen Activated 3
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GGEPRRTEGVGPGVPGEVEMVKGQPFDVGPRYTQLQYIGEGAYGMVSSAYDHVRKTRVAIKKISPFEHQTYCQRTLREIQILLRFRHENVIGIRDILRASTLEAMRDVYIVQDLMETDLYKLLKSQQLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLINTTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINMKARNYLQSLPSKTKVAWAKLFPKSDSKALDLLDRMLTFNPNKRITVEEALAHPYLEQYYDPTDEPVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP
Expression Range	11-379aa
Protein Length	Partial
Mol. Weight	46.3kDa
Research Area	Cell Cycle
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Cytoplasm. Nucleus. Membrane, caveola. Cell junction, focal adhesion.
Protein Families	Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
Database References	HGNC: 6877 OMIM: 601795 KEGG: hsa:5595 STRING: 9606.ENSP00000263025 UniGene: PMID: 29084846 RASSF7 promotes cell proliferation through activating MEK1/MEK2-ERK1/ERK2 signaling pathway in hepatocellular carcinoma. PMID: 29729697 ERK1 Directly Interacts With JNK1 Leading to Regulation of JNK1/c-Jun Activity and Cell Transformation. PMID: 28106280 the D domain of LRRC4 anchors ERK1/2 in the cytoplasm and competitively inhibits MEK/ERK activation in glioma cells. PMID: 27884160 High ERK1 expression is associated with castration-resistant prostate cancer. PMID: 28844715 The antitumor activity of scopoletin may be due to its strong anti-angiogenic effect, which may be mediated by its effective inhibition of ERK1, VEGF-A, and FGF-2. PMID: 27133199 High ERK1 expression is associated with melanoma. PMID: 28193911 findings uncover a role of ERK1 in the regulation of furin activity by supporting a self-sustaining loop for high TGF-beta activity in glioma-initiating cells. PMID: 28484053 ERK1 phosphorylation is mediated by Src and Csk. PMID: 26234813 Integrin beta1 appears to serve as a partner of Stathmin induction of ERK and Akt signaling by inhibiting apoptosis in the cholangiocarcinoma cell. PMID: 28178656 High ERK1 expression is associated with gastric cancer. PMID: 27601158 Data indicate three biomarkers mitogen-activated protein kinase 3 (MAPK3), BCL2 apoptosis regulator (BCL2) and proto-oncogene c-Akt (AKT1) as potential predictors of neurological outcome following cardiac arrest (CA). PMID: 28147324 Inhibiting miR-21 attenuates hepatic fibrosis by suppressing both the ERK1 in hepatic stellate cells and epithelial-mesenchymal transition of hepatocyte. PMID: 27226339 High ERK1 expression is associated with paclitaxel resistance in cervical cancer. PMID: 26810068 High ERK1 expression is Associated with Nucleus Pulposus Cells' Degeneration. PMID: 27635110 Low expression of ERK is associated with resistance to sorafenib in liver cancer. PMID: 26711788 Increased ERK1 expression is associated with drug resistance in neoplasms. PMID: 26715278 The activation of ERK1 by MEK1, subsequent slower phosphorylation of the flanking sites results in inhibition of the kinase. Because the T207 and Y210 phosphosites of ERK1 are highly conserved within the eukaryotic protein kinase family, hyperphosphorylation within the kinase activation T-loop may serve as a general mechanism for protein kinase down-regulation after initial activation by their upstream kinases. PMID: 26823016 Over-expressed TWIST associates with markers of epithelial mesenchymal transition and predicts poor prognosis in breast cancers via ERK and AKT activation. PMID: 26295469 p44/42, a known apoptosis-promoting regulator and caspase 3 activator, was increased in brain tumor cells treated with violacein PMID: 25816226 miR-155 plays an important role in regulating the pathological network involving EMT process and ERK1 pathway during hepatic stellate cell activation. PMID: 25142507 This study identified and confirmed MAPK3 protein changes within the postsynaptic density in schizophrenia PMID: 25048004 Sphingosine-1-phosphate promotes extravillous trophoblast cell invasion by activating MEK/ERK/MMP-2 signaling pathways via S1P/S1PR1 axis activation. PMID: 25188412 Results show that miR-483-5p expression level is up-regulated in polycystic ovary syndrome patients and inversely correlated with notch3 and MAPk3 levels and that Notch3 and MAPK3 are the direct targets of MIR483. PMID: 25622783 SKLB-M8 inhibited HUVEC proliferation, migration, invasion, and tube formation in vitro with the inhibition of phosphorylated ERK1/2. PMID: 25341684 Therefore, the positivity of p-ERK1/2 expression may serve as a vital biomarker in the development of non-small cell lung cancer PMID: 25596700 Low ERK1 expression is associated with hormone resistance in breast cancer. PMID: 25085753 Therefore, our study demonstrates that MAPK members (ERK1/2 and JNK) play a key role in CCR7 regulating SCCHN metastasis PMID: 25270024 High phosphorylated ERK1 is associated with low response to chemotherapy in nonsmall-cell lung carcinoma. PMID: 25449334 These results therefore indicate that p53-mediated up-regulation of MKP-3 contributes to the establishment of the senescent cellular phenotype through dephosphorylating ERK1/2 PMID: 25414256 ERK1/2 signal induced MNK catalytic activity enabled enterovirus type 1 internal ribosomal entry site-mediated translation/host cell cytotoxicity through negative regulation of the Ser/Arg (SR)-rich protein kinase (SRPK). PMID: 25187541 ERK, AKT, and GSK-3beta have roles in boldine-induced cell cycle arrest and apoptosis in T24 human bladder cancer cell line PMID: 24239461 Insulin-induced apoptotic commitment depended on the down-regulation of Erk-1, insulin growth factor-1 receptor (IGF-1R), and fibroblast growth factor receptor-1 (FGFR-1)-mediated signaling. PMID: 24818995 Enhanced t-ERK1 expression in infiltrating lymphoid cells was significantly associated with female gender, absence of vascular and perineural invasion, lymph node metastases and early depth of invasion as well as with longer disease-free survival times PMID: 24682903 Expression of TMPRSS4 in gastric cancer is significantly associated with lymph node and distant metastasis, high Erk1 expression, and poor prognosis. PMID: 23922976 ERK1 phosphorylates KIBRA at Ser(548) for cell proliferation and migratory activity PMID: 24269383 We conclude that pERK1/2 is a sensitive marker of early colon cancer, which disappears at later stages of cancer development. PMID: 23357054 In activated eosinophils ligation of Siglec-8 leads to ROS-dependent enhancement of IL-5-induced ERK phosphorylation, which results in a novel mode of biochemically regulated eosinophil cell death. PMID: 23684072 ERK1 localized to the cytosol and translocated to the nucleus upon cell activation and kinase phosphorylation. PMID: 23651922 Data indicate that tocilizumab enhanced the interferon-induced phosphorylation of STAT1 and inhibited SOCS3 expression and the phosphorylation of both STAT3 and ERK. PMID: 23274199 Extracellular signal-regulated kinase and glycogen synthase kinase 3beta regulate gephyrin postsynaptic aggregation and GABAergic synaptic function in a calpain-dependent mechanism PMID: 23408424 ERK1/2 signaling plays an important role in topoisomerase II poison-induced G2/M checkpoint activation. PMID: 23166842 MRK is a novel RhoC effector that controls LPA-stimulated cell invasion at least in part by regulating myosin dynamics, ERK and p38 PMID: 23319595 osteosarcoma patients whose tumors expressed pERK1 had a poorer clinical outcome than those whose tumors did not. PMID: 22935974 Results showed significantly higher levels of ERK1 protein in smokers vs. non-smokers. Analysis revealed a significant relation among the number of cigarettes smoked daily, the Fagerstrom Test for Nicotine Dependence score and the mRNA expression of ERK1. PMID: 21070506 constitutive activation of the ERK1 pathway in HER2/ERBB2-transformed cells prevents EGF deprivation-induced FLIPL upregulation and TRAIL resistance. PMID: 22722337 Lead specifically induces dysregulation of iron response element (IRP)1 protein by activating the ERK1/2 signaling pathway, indicating a novel role for IRP1 and the ERK/MAPK pathway in vascular endothelial functions. PMID: 22502979 CXCL12/CXCR4 protein signaling axis induces sonic hedgehog expression in pancreatic cancer cells via extracellular regulated kinase- and Akt kinase-mediated activation of nuclear factor kappaB PMID: 22995914 Aortic endothelial cells stimulated with HLA class I antibodies did not promote any detectable change in intracellular Ca(2+) concentration but instead induced MLC phosphorylation and stress fiber assembly. PMID: 22914643 The inhibition of Id-1 expression by MK615 is mediated via ERK1/2 activation. PMID: 22076920

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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.

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