Recombinant Mouse Sialidase-1 (Neu1)

Code CSB-YP015717MO
Size $436
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 85% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
Neu1; Neu; Sialidase-1; EC; G9 sialidase; Lysosomal sialidase; N-acetyl-alpha-neuraminidase 1
Mus musculus (Mouse)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Tris-based buffer,50% glycerol
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

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.
Gene References into Functions
  1. The NEU1 exists on the cell surface of mouse thymocytes and CD5 is a natural substrate for it. PMID: 29897583
  2. Neu1 inhibits lipolysis induced by beta-adrenergic stimulation in adipocytes via interactions with Plin1 on lipid drops. PMID: 28429532
  3. Neu1 is the only lysosomal multienzyme complex gene underexpressed in mucopolysaccharidosis type I mice. PMID: 27720939
  4. Neu1 desialylation is a mechanism of Fc-independent platelet clearance in immune thrombocytopenia. PMID: 26185093
  5. Data indicate a role for neuraminidase 1 (Neu1) in regulating Siglec E protein-toll-like receptor 4 (TLR4) interaction and endotoxemia. PMID: 25187624
  6. elastin-derived peptides as an enhancer of atherogenesis and defines the Neuraminidase 1/PI3Kgamma signalling pathway as a key mediator PMID: 24357053
  7. 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
  8. NEU1 deficiency has a role in determining amyloid precursor protein levels and amyloid-beta secretion via deregulated lysosomal exocytosis PMID: 24225533
  9. 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
  10. these studies identify Neu1 as a novel component of the signaling pathways of energy metabolism and glucose uptake. PMID: 23520133
  11. 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
  12. Data indicate that sialidases Neu1 and Neu3 are present on sperm, and their activity is required for capacitation and zona pellucida binding. PMID: 22989879
  13. Neuraminidase 1 as a modulator of cell receptors. (Review) PMID: 21928149
  14. The deficiency of lysosomal neuraminidase may result in a serious hearing loss and morphological alterations of ear. PMID: 16408748
  15. desialylation of both IR and IGF-1R by Neu1 controls the net proliferative response of skeletal myoblasts to insulin PMID: 20100694
  16. 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
  17. A potential role of NEU1 in cell proliferation and extracellular matrix remodeling. PMID: 20388541
  18. 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
  19. 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
  20. 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
  21. Neu1 is a negative regulator of lysosomal exocytosis. PMID: 18606142
  22. in vivo histopathological effects of neuraminidase-1 (Neu1) deficiency on elastin assembly in the lungs and aorta of mice PMID: 18689602
  23. A regulatory mutation, (-519G-->A) within the neu1 promoter generates a consensus binding site for Nkx3 family transcription repressors. PMID: 19217813
  24. 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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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
Tissue Specificity
Highly expressed in kidney, epididymis, followed by brain, spinal cord and weakly expressed in adrenal, heart, liver, lung and spleen.
Database Links
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