NEU1
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Official Full Name
sialidase 1 (lysosomal sialidase)
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Overview
The protein encoded by this gene is a lysosomal enzyme that cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter is also referred to as protective protein). Mutations in this gene can lead to sialidosis, a lysosomal storage disease that can be type 1 (cherry red spot-myoclonus syndrome or normosomatic type), which is late-onset, or type 2 (the dysmorphic type), which occurs at an earlier age with increased severity. [provided by RefSeq, Jul 2008] -
Synonyms
NEU1; sialidase 1 (lysosomal sialidase); NEU; NANH; SIAL1; sialidase-1; G9 sialidase; exo-alpha-sialidase; lysosomal sialidase; acetylneuraminyl hydrolase; N-acetyl-alpha-neuraminidase 1;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Rhesus Macaque
- Zebrafish
- E. coli
- E.coli
- HEK293
- HEK293T
- Mammalian Cell
- Mammalian cells
- Yeast
- C
- His
- Flag
- His (Fc)
- Avi
- Myc
- DDK
- N/A
- N
- Involved Pathway
- Protein Function
- Interacting Protein
- NEU1 Related Articles
- NEU1 Related Research Area
NEU1 involved in several pathways and played different roles in them. We selected most pathways NEU1 participated on our site, such as Other glycan degradation, Sphingolipid metabolism, Lysosome, which may be useful for your reference. Also, other proteins which involved in the same pathway with NEU1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Other glycan degradation | NEU3;NEU3.2;NEU2;MAN2B1;HEXDC;AGA;FUCA1.2;NEU4;HEXB |
Sphingolipid metabolism | ARSE;PPM1L;VAPB;SPTLC3;CERS4A;GLTPA;CERS1;DEGS1;ARSF |
Lysosome | SUMF1;ATP6V0CB;AP1S3;CTSG;ENTPD4;ASAH1;AP3D1;ABCB9;CTSSB.2 |
NEU1 has several biochemical functions, for example, exo-alpha-(2->3)-sialidase activity, exo-alpha-(2->6)-sialidase activity, exo-alpha-(2->8)-sialidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by NEU1 itself. We selected most functions NEU1 had, and list some proteins which have the same functions with NEU1. You can find most of the proteins on our site.
Function | Related Protein |
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exo-alpha-(2->3)-sialidase activity | NEU3;NEU2;NEU4;NEU1 |
exo-alpha-(2->6)-sialidase activity | NEU2;NEU1;NEU3;NEU4 |
exo-alpha-(2->8)-sialidase activity | NEU3;NEU4;NEU1;NEU2 |
exo-alpha-sialidase activity | NEU3.1;NEU3.4;NEU3.2;NEU4;NEU3;ST3GAL5L;NEU1;NEU3.5;NEU3.3 |
NEU1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with NEU1 here. Most of them are supplied by our site. Hope this information will be useful for your research of NEU1.
GLB1; JUNB; EEF1A1; tktA; pi3p; ELN; Rcc1; VAPA
- Q&As
- Reviews
Q&As (5)
Ask a questionYes, there is ongoing research aimed at understanding the molecular mechanisms of NEU1 and developing potential therapeutic interventions for associated disorders.
NEU1 deficiency can lead to a group of rare genetic disorders known as sialidosis, which can cause a range of symptoms including intellectual disabilities, muscle weakness, and skeletal abnormalities.
NEU1 protein has also been implicated in certain types of cancer and neurodegenerative diseases.
Yes, NEU1 deficiency can lead to additional complications such as hepatosplenomegaly (enlargement of the liver and spleen), seizures, and difficulty swallowing.
Currently, there are no specific cures for NEU1 deficiency or sialidosis. Treatment is generally supportive and aims to manage the symptoms.
Customer Reviews (3)
Write a reviewIts purity and reliability ensure reliable and reproducible results in a variety of research applications.
The protein's reliability and reproducibility in WB ensure accurate analysis of target proteins, while its suitability for electron microscopy structure analysis enables detailed examination of molecular structures.
The NEU1 protein exhibits outstanding performance in enzyme-linked immunosorbent assays (ELISA).
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