Menin Protein, Human

Menin Protein is an endocrine tumor suppressor and transcriptional regulator. By binding to various transcription factors and signaling molecules, Menin Protein plays roles in activating or inhibiting gene transcription and regulating multiple signaling pathways such as TGFβ and Wnt in different tissues. Menin Protein is crucial in processes including cell growth, cell cycle, genomic stability, and bone development. Menin Protein, Human is a recombinant Menin protein expressed by E. coli without a tag^[1][2][3].

Menin Protein is encoded by the MEN1 gene and regulates gene transcription by binding to transcriptional activators (such as MLL1 and c-Myb) and repressors (such as JunD and NFκB). Menin Protein can both promote gene expression by recruiting histone-modifying enzymes to facilitate H3K4me3 and inhibit transcription by recruiting HDAC, EZH2, and other factors. Menin Protein is involved in multiple signaling pathways, including TGFβ/SMAD, Wnt/β-catenin, and Ras/ERK, with distinct functions in different tissues—for example, inhibiting proliferation in islet cells and collaborating with MLL fusion proteins to drive HOX gene expression and promote cancer in leukemic cells. Additionally, Menin Protein is regulated by post-translational modifications such as phosphorylation and SUMOylation, as well as signaling pathways like prolactin and TGFβ. The central pocket in its structure serves as a key functional domain for binding multiple proteins^[1][2][3].

Overexpression of Menin in pregnant βMen1 mice leads to reduced islet β-cell proliferation, increased blood glucose, and impaired glucose tolerance^[3].

Human

E. coli

Tag Free

O00255-1 (M1-L615)

4221

Full Length

MGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGWSPVGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYRDEHIYPYMYLAGYHCRNRNVREALQAWADTATVIQDYNYCREDEEIYKEFFEVANDVIPNLLKEAASLLEAGEERPGEQSQGTQSQGSALQDPECFAHLLRFYDGICKWEEGSPTPVLHVGWATFLVQSLGRFEGQVRQKVRIVSREAEAAEAEEPWGEEAREGRRRGPRRESKPEEPPPPKKPALDKGLGTGQGAVSGPPRKPPGTVAGTARGPEGGSTAQVPAPTASPPPEGPVLTFQSEKMKGMKELLVATKINSSAIKLQLTAQSQVQMKKQKVSTPSDYTLSFLKRQRKGL

Approximately 68 kDa

≥ 85%, as determined by reducing SDS-PAGE.

Solution

1.Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH7.5, 200 mM NaCl, 20% glycerol, 1 mM DTT.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
2.Supplied as a 0.22 μm filtered solution of 50 mM HEPES, pH7.5, 200 mM NaCl, 20% glycerol.
Please refer to the lot-specific COA for specific buffer information.

<1 EU/μg, determined by LAL method.

Please use rapid thawing with running water to thaw the protein.

Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.

• [1]. Balogh K, et al. Menin and its interacting proteins: elucidation of menin function. Trends Endocrinol Metab. 2006 Nov;17(9):357-64.  [Content Brief]

  [2]. Matkar S, et al. Menin: a scaffold protein that controls gene expression and cell signaling. Trends Biochem Sci. 2013 Aug;38(8):394-402.  [Content Brief]

  [3]. Karnik SK, et al. Menin controls growth of pancreatic beta-cells in pregnant mice and promotes gestational diabetes mellitus. Science. 2007 Nov 2;318(5851):806-9.  [Content Brief]