Recombinant Human Neuraminidase protein is a Human Full Length protein, in the 48 to 415 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
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Key facts
- Purity
- >85% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE, MS
- Biologically active
- No
Amino acid sequence
M G S S H H H H H H S S G L V P R G S H M G S H M E N D F G L V Q P L V T M E Q L L W V S G R Q I G S V D T F R I P L I T A T P R G T L L A F A E A R K M S S S D E G A K F I A L R R S M D Q G S T W S P T A F I V N D G D V P D G L N L G A V V S D V E T G V V F L F Y S L C A H K A G C Q V A S T M L V W S K D D G V S W S T P R N L S L D I G T E V F A P G P G S G I Q K Q R E P R K G R L I V C G H G T L E R D G V F C L L S D D H G A S W R Y G S G V S G I P Y G Q P K Q E N D F N P D E C Q P Y E L P D G S V V I N A R N Q N N Y H C H C R I V L R S Y D A C D T L R P R D V T F D P E L V D P V V A A G A V V T S S G I V F F S N P A H P E F R V N L T L R W S F S N G T S W R K E T V Q L W P G P S G Y S S L A T L E G S M D G E E Q A P Q L Y V L Y E K G R N H Y T E S I S V A K I S V Y G T L
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Target data
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.
Alternative names
NANH, NEU1, Sialidase-1, Acetylneuraminyl hydrolase, G9 sialidase, Lysosomal sialidase, N-acetyl-alpha-neuraminidase 1
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Recombinant Human Neuraminidase protein is a Human Full Length protein, in the 48 to 415 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
Key facts
- Purity
- >85% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE, MS
- Biologically active
- No
- Accession
- Q99519-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Sequence info
Amino acid sequence
- M G S S H H H H H H S S G L V P R G S H M G S H M E N D F G L V Q P L V T M E Q L L W V S G R Q I G S V D T F R I P L I T A T P R G T L L A F A E A R K M S S S D E G A K F I A L R R S M D Q G S T W S P T A F I V N D G D V P D G L N L G A V V S D V E T G V V F L F Y S L C A H K A G C Q V A S T M L V W S K D D G V S W S T P R N L S L D I G T E V F A P G P G S G I Q K Q R E P R K G R L I V C G H G T L E R D G V F C L L S D D H G A S W R Y G S G V S G I P Y G Q P K Q E N D F N P D E C Q P Y E L P D G S V V I N A R N Q N N Y H C H C R I V L R S Y D A C D T L R P R D V T F D P E L V D P V V A A G A V V T S S G I V F F S N P A H P E F R V N L T L R W S F S N G T S W R K E T V Q L W P G P S G Y S S L A T L E G S M D G E E Q A P Q L Y V L Y E K G R N H Y T E S I S V A K I S V Y G T L
- Accession
- Q99519
- Protein length
- Full Length
- Predicted molecular weight
- 42.9 kDa
- Amino acids
- 48 to 415
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Liquid
- Additional notes
ab131685 was purified using conventional chromatography techniques.
General info
- 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.
- Sequence similarities
Belongs to the glycosyl hydrolase 33 family.
- Post-translational modifications
N-glycosylated.
- Subcellular localisation
- Lysosome membrane, Lysosome lumen, Lysosome
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage duration
- 1-2 weeks
- Appropriate short-term storage conditions
- +4°C
- Appropriate long-term storage conditions
- -20°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Neuraminidase sometimes called sialidase functions as an enzyme that cleaves sialic acid residues from glycoproteins and glycolipids. This process is essential for the maturation and release of progeny viruses from infected cells. Enzymatically active neuraminidase proteins weigh about 60 kilodaltons and localize on the surface of influenza viruses. Researchers identify its expression on the viral envelope playing a pivotal role in the viral life cycle. Neuraminidase activity is an important target for drug development against influenza.
- Biological function summary
Neuraminidase significantly impacts viral virulence and host cell infection. It is part of the functional machinery required for viral particle detachment from the host cell membrane facilitating the spread of infection. Neuraminidase works alongside other viral proteins including hemagglutinin which attaches the virus to the host cell. The neuraminidase function of trimming sialic acids is critical in the ongoing interaction between virus and host.
- Pathways
The influenza lifecycle heavily involves neuraminidase-mediated sialic acid cleavage. This enzyme contributes to pathways by enabling the efficient release of new viral particles enhancing the infectivity of the virus. Neuraminidase operates in concert with hemagglutinin which initially binds the virus to host cells by attaching to the sialic acid residues. This interplay is vital in viral replication pathways which propagate the infection cycle.
- Associated diseases and disorders
Influenza directly relates to neuraminidase as it is a primary means by which the virus spreads within the host. Neuraminidase inhibitors are a class of antiviral drugs that target this protein important for treating and managing influenza infections. Besides influenza research links neuraminidase activity to bacterial infections with some bacterial neuraminidases implicated in the pathogenesis of diseases like pneumonia. The relationship to hemagglutinin in viral influenza highlights the significance of neuraminidase as a target in therapeutic interventions.
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SDS-PAGE - Recombinant Human Neuraminidase protein (ab131685)
15% SDS-PAGE analysis of 3 µg ab131685.
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