Recombinant Mouse Sialidase-1 (NEU1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04856P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse Sialidase-1 (NEU1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04856P
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Product Overview

Description Recombinant Mouse Sialidase-1 (NEU1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb O35657
Target Symbol NEU1
Synonyms Neu1; Neu; Sialidase-1; EC 3.2.1.18; G9 sialidase; Lysosomal sialidase; N-acetyl-alpha-neuraminidase 1
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-10His
Target Protein Sequence EDDFSLVQPLVTMEQLLWVSGKQIGSVDTFRIPLITATPRGTLLAFAEARKKSASDEGAKFIAMRRSTDQGSTWSSTAFIVDDGEASDGLNLGAVVNDVDTGIVFLIYTLCAHKVNCQVASTMLVWSKDDGISWSPPRNLSVDIGTEMFAPGPGSGIQKQREPGKGRLIVCGHGTLERDGVFCLLSDDHGASWHYGTGVSGIPFGQPKHDHDFNPDECQPYELPDGSVIINARNQNNYHCRCRIVLRSYDACDTLRPRDVTFDPELVDPVVAAGALATSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWQKERVQVWPGPSGYSSLTALENSTDGKKQPPQLFVLYEKGLNRYTESISMVKISVYGTL
Expression Range 42-409aa
Protein Length Full Length of Mature Protein
Mol. Weight 46.3 kDa
Research Area Microbiology
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.
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 Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.
Subcellular Location Lysosome membrane; Peripheral membrane protein; Lumenal side. Lysosome lumen. Cell membrane. Cytoplasmic vesicle. Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles.
Protein Families Glycosyl hydrolase 33 family
Database References

KEGG: mmu:18010

STRING: 10090.ENSMUSP00000007253

UniGene: PMID: 29897583

  • Neu1 inhibits lipolysis induced by beta-adrenergic stimulation in adipocytes via interactions with Plin1 on lipid drops. PMID: 28429532
  • Neu1 is the only lysosomal multienzyme complex gene underexpressed in mucopolysaccharidosis type I mice. PMID: 27720939
  • Neu1 desialylation is a mechanism of Fc-independent platelet clearance in immune thrombocytopenia. PMID: 26185093
  • Data indicate a role for neuraminidase 1 (Neu1) in regulating Siglec E protein-toll-like receptor 4 (TLR4) interaction and endotoxemia. PMID: 25187624
  • elastin-derived peptides as an enhancer of atherogenesis and defines the Neuraminidase 1/PI3Kgamma signalling pathway as a key mediator PMID: 24357053
  • significant increases in Col1a1, serine/threonine-protein kinase 1, Ctnnb1, CSRNP1, Ddit4, Cyp2e1, and Krit1 expressions and great decreases inreceptor D2, Neu1, and Dhcr7 expressions following long-term exposure to TiO2 NPs PMID: 23533084
  • NEU1 deficiency has a role in determining amyloid precursor protein levels and amyloid-beta secretion via deregulated lysosomal exocytosis PMID: 24225533
  • The activity of NEU1 was preferentially higher in epididymal fat and lower in the livers of two strains of obese and diabetic mice. PMID: 23727924
  • these studies identify Neu1 as a novel component of the signaling pathways of energy metabolism and glucose uptake. PMID: 23520133
  • The rescue of sialidase activity in hypomorphic sialidase mice using helper-dependent adenovirus resulted in increased VLDL production and an increase in MTP levels. PMID: 22984145
  • Data indicate that sialidases Neu1 and Neu3 are present on sperm, and their activity is required for capacitation and zona pellucida binding. PMID: 22989879
  • Neuraminidase 1 as a modulator of cell receptors. (Review) PMID: 21928149
  • The deficiency of lysosomal neuraminidase may result in a serious hearing loss and morphological alterations of ear. PMID: 16408748
  • desialylation of both IR and IGF-1R by Neu1 controls the net proliferative response of skeletal myoblasts to insulin PMID: 20100694
  • Hyaluronan receptor activity of CD44 and acute asthmatic reactions, including Th2-mediated airway inflammation and airway hyperresponsiveness, are dependent upon Neu1 enzymatic activity. PMID: 20491786
  • A potential role of NEU1 in cell proliferation and extracellular matrix remodeling. PMID: 20388541
  • The neuraminidase-1 (Neu1) knockout mouse model is a phenocopy of the lysosomal storage disease sialidosis, characterized by neuropathic symptoms, including hearing loss. PMID: 19857571
  • A membrane controlling mechanism that is initiated by ligand binding to TLR-2, -3 and-4 to induce Neu1 sialidase activity within minutes in live primary bone marrow (BM) macrophage cells and macrophage and dendritic cell lines, is showed. PMID: 19430901
  • The cell surface Neu1 activates the phagocytosis in macrophages and dendritic cells through desialylation of surface receptors, thus, contributing to their functional integrity. PMID: 19889639
  • Neu1 is a negative regulator of lysosomal exocytosis. PMID: 18606142
  • in vivo histopathological effects of neuraminidase-1 (Neu1) deficiency on elastin assembly in the lungs and aorta of mice PMID: 18689602
  • A regulatory mutation, (-519G-->A) within the neu1 promoter generates a consensus binding site for Nkx3 family transcription repressors. PMID: 19217813
  • The N-terminal N-glycan of NEU1 is indispensable for its function, whereas the C-terminal N-glycan appears to be non-essential. The omission of the second N-glycan can be compensated for by upregulating the expression of protective protein/cathepsin A. PMID: 19714866

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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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