Recombinant Human MELK Protein

Name: Recombinant Human MELK Protein
Brand: Beta LifeScience
SKU: BL-0287SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_014791
Synonym	HPK38, KIAA0175
Background	MELK or maternal embryonic leucine zipper kinase is a member of the CAMKL kinase family. MELK is a key regulator of the proliferation of malignant brain tumors including their stem cells (1). MELK transcript abundance correlates with malignancy grade in human astrocytomas and represents a therapeutic target for the management of the most frequent brain tumors in adult and children. MELK also plays a role in mammary carcinogenesis through inhibition of the pro-apoptotic function of Bcl-GL (2). Therefore, the kinase activity of MELK could be a promising molecular target for development of therapy for patients with breast cancers.
Description	Recombinant human MELK (1-340) 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	1-340
Molecular Weight	~61 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 Human MELK 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 involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.
Subcellular Location	Cell membrane; Peripheral membrane protein.
Protein Families	Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
Database References	HGNC: 16870 OMIM: 607025 KEGG: hsa:9833 STRING: 9606.ENSP00000298048 UniGene: PMID: 28536141 In common culture conditions, the authors found that small molecule inhibition, genetic deletion, or acute depletion of MELK did not significantly affect cellular growth. PMID: 28926338 Synthesis of MCL1, an antiapoptotic protein known to play a role in cancer cell survival during cell division, depends on the function of MELK-elF4B signaling. PMID: 27528663 Inhibition of MELK (genetically and pharmacologically) induces radiation sensitivity. PMID: 27225691 MELK is a host factor required for optimal uncoating of the HIV-1 core to promote viral cDNA synthesis. PMID: 28683086 Here, the authors report that mutagenizing MELK with CRISPR/Cas9 has no effect on the fitness of basal breast cancer cell lines or cell lines from six other cancer types. Cells that harbor null mutations in MELK exhibit wild-type doubling times, cytokinesis, and anchorage-independent growth. PMID: 28337968 MELK-inhibitor has a role in triple-negative breast cancer cells demonstrating context-dependent response with p53 as a key determinant PMID: 28235006 MELK is an oncogenic kinase involved in the pathogenesis and recurrence of hepatocellular carcinoma. PMID: 27693640 Inhibition or depletion of MELK reduced cell proliferation and anchorage-dependent and -independent growth in various ovarian cancer cell lines through a G2/M cell cycle arrest, eventually resulting in apoptosis. PMID: 28214016 Report IL11RA and MELK amplification in gastric cancer cell lines and primary gastric adenocarcinomas. PMID: 27920471 MELK expression in hepatocellular carcinoma is extremely intense compared to its expression reported in other types of cancer and could be a promising effective tumor marker of HCC. PMID: 27798878 targeting MELK by the inhibition of both its catalytic activity and its protein stability might sensitize tumours to DNA-damaging agents or radiation therapy by lowering the DNA-damage threshold PMID: 26431963 Together, these data indicate that MELK is a normally non-essential kinase, but is critical for basal-like breast cancer. PMID: 24844244 EZH2 protects glioma stem cells from radiation-induced cell death in a MELK/FOXM1-dependent manner PMID: 25601206 we report characterization of possible roles of MELK in acute myeloid leukemia PMID: 25365263 insight has been brought by the discovery of a protein complex of FOXM1 with the mitotic kinase MELK in cancer stem cells in brain cancers, as this protein complex appears to be cancer-specific PMID: 25017123 advanced cancers with OTSSP167 started in 2013, as the first-in-class MELK inhibitor. This review summarizes the current molecular understanding of MELK and the recent preclinical studies about MELK as a cancer therapeutic target. PMID: 24795222 MELK promotes cell migration and invasion via the FAK/Paxillin pathway, and plays an important role in the occurrence and development of gastric cancer. PMID: 24885567 our current knowledge of MELK function and recent discoveries in MELK signaling pathway were discussed. PMID: 24185907 The structural and biochemical analyses unravel the molecular mechanisms for the autophosphorylation/activation of MELK and the dependence of its catalytic activity on reducing agents. PMID: 23922895 Report MELK inhibitor that suppresses the growth of a wide range of human tumor cell lines. PMID: 23283305 Data indicate that expression-based risk indices of three genes UBE2C, TPX2, and MELK were more strongly associated with poor 5-year survival in adenocarcinoma patients. PMID: 23357462 MELK is upregulated in high-grade prostate cancer PMID: 22945237 MELK could be associated with increased resistance of colorectal cancer cells against radiation and 5-FU. PMID: 21806965 High MELK is associated with brain tumor. PMID: 21558073 MELK expression is increased in breast cancer tissue and this is associated with poor survival. The most important factors controlling Bcl-G activity are post-translational modification by Fau & MELK. PMID: 19671159 pEg3 is a potential regulator of the G2/M progression and may act antagonistically to the CDC25B phosphatase,pEg3 kinase is able to specifically phosphorylate CDC25B in vitro. One phosphorylation site was identified and corresponded to serine 323 PMID: 12400006 analysis of MELK substrate specificity and activity regulation PMID: 16216881 the kinase activity of MELK is likely to affect mammary carcinogenesis through inhibition of the pro-apoptotic function of Bcl-GL PMID: 17280616 a critical role for MELK in the proliferation of brain tumors, including their stem cells, and suggest that MELK may be a compelling molecular target for treatment of high-grade brain tumors. PMID: 17722061 Maternal embryonic leucine zipper kinase transcript abundance correlates with malignancy grade in astrocytomas PMID: 17960622

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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.