Mouse Anti-NEU3 Recombinant Antibody (11B) (CBMAB-N2027-WJ)

Name: Mouse Anti-NEU3 Recombinant Antibody (11B)
SKU: CBMAB-N2027-WJ
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

11B

Application

Specificity

Human

Antibody Isotype

IgG1, κ

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

PBS, pH 7.2, 50% glycerol

Concentration

1 mg/mL

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

neuraminidase 3

Introduction

This gene product belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. It is localized in the plasma membrane, and its activity is specific for gangliosides. It may play a role in modulating the ganglioside content of the lipid bilayer. [provided by RefSeq, Jul 2008]

Entrez Gene ID

10825

UniProt ID

Q9UQ49

Alternative Names

Neuraminidase 3; Sialidase 3 (Membrane Sialidase); N-Acetyl-Alpha-Neuraminidase 3; Ganglioside Sialidase; Membrane Sialidase; EC 3.2.1.18; Neuraminidase 3, Membrane Sialidase; Sialidase-3; SIAL3;

Function

Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3 (PubMed:11298736, PubMed:15847605, PubMed:10861246, PubMed:20511247, PubMed:28646141, PubMed:10405317, PubMed:12011038).

Plays a role in the regulation of transmembrane signaling through the modulation of ganglioside content of the lipid bilayer and by direct interaction with signaling receptors, such as EGFR (PubMed:17334392, PubMed:25922362).

Desialylates EGFR and activates downstream signaling in proliferating cells (PubMed:25922362).

Contributes to clathrin-mediated endocytosis by regulating sorting of endocytosed receptors to early and recycling endosomes (PubMed:26251452).

Biological Process

Carbohydrate metabolic process Source: MGI
Ganglioside catabolic process Source: UniProtKB
Glycosphingolipid metabolic process Source: Reactome
Negative regulation of clathrin-dependent endocytosis Source: UniProtKB
Oligosaccharide catabolic process Source: UniProtKB
Positive regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB

Cellular Location

Endosome
Early endosome membrane
Recycling endosome membrane
Lysosome
Lysosome membrane
Plasma membrane
Cell membrane
Other locations
caveola
Note: Associates with the external leaflet of the plasma membrane (By similarity). S-acylated NEU3 likely spans the lipid bilayer with a portion of C-terminus exposed to the cytosol and the catalytic region facing the extracellular space (PubMed:28646141).

PTM

Palmitoylated; may regulate intracellular trafficking and anchorage to plasma membrane and endomembranes.

Delaveris, C. S., Wang, C. L., Riley, N. M., Li, S., Kulkarni, R. U., & Bertozzi, C. R. (2023). Microglia Mediate Contact-Independent Neuronal Network Remodeling via Secreted Neuraminidase-3 Associated with Extracellular Vesicles. ACS Central Science, 9(11), 2108-2114.

Kirolos, S. A., & Gomer, R. H. (2022). The extracellular sialidase NEU3 induces neutrophil priming. bioRxiv, 2022-02.

Kirolos, S. A., Pilling, D., & Gomer, R. H. (2022). The extracellular sialidase NEU3 primes neutrophils. Journal of Leukocyte Biology, 112(6), 1399-1411.

Miyagi, T., & Yamamoto, K. (2022). Sialidase NEU3 and its pathological significance. Glycoconjugate Journal, 39(5), 677-683.

Tran, H. T. T., Li, C., Chakraberty, R., & Cairo, C. W. (2022). NEU1 and NEU3 enzymes alter CD22 organization on B cells. Biophysical Reports, 2(3).

Yang, W. H., Westman, J. S., Heithoff, D. M., Sperandio, M., Cho, J. W., Mahan, M. J., & Marth, J. D. (2021). Neu3 neuraminidase induction triggers intestinal inflammation and colitis in a model of recurrent human food-poisoning. Proceedings of the National Academy of Sciences, 118(29), e2100937118.

Kim, C. H., & Kim, C. H. (2020). Membrane Ganglioside-Specific Neuraminidase 3 (NEU3) Regulates GM3 Signaling. GM3 Signaling, 49-54.

Howlader, M. A., Li, C., Zou, C., Chakraberty, R., Ebesoh, N., & Cairo, C. W. (2019). Neuraminidase-3 is a negative regulator of LFA-1 adhesion. Frontiers in Chemistry, 7, 791.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

Isotype control

For research use only. Not intended for any clinical use.

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