Mouse Anti-NAAA Recombinant Antibody (CBWJN-1148) (CBMAB-N1017-WJ)

Name: Mouse Anti-NAAA Recombinant Antibody (CBWJN-1148)
SKU: CBMAB-N1017-WJ
Rating: 5 (1 reviews)

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Datasheet

SDS

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Basic Information

Host Animal

Mouse

Clone

CBWJN-1148

Application

ELISA, IP, WB

Specificity

Human

Antibody Isotype

IgG1

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

Lyophilized

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

N-acylethanolamine acid amidase

Introduction

This gene encodes an N-acylethanolamine-hydrolyzing enzyme which is highly similar to acid ceramidase. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Entrez Gene ID

27163

UniProt ID

Q02083

Alternative Names

N-Acylethanolamine Acid Amidase; Acid Ceramidase-Like Protein; ASAH-Like Protein; ASAHL; PLT; N-Acylsphingosine Amidohydrolase (Acid Ceramidase)-Like; N-Acylethanolamine-Hydrolyzing Acid Amidase; N-Acylsphingosine Amidohydrolase-Like; EC 3.5.1.-;

Function

Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine> N-myristoylethanolamine> N-lauroylethanolamine = N-stearoylethanolamine> N-arachidonoylethanolamine> N-oleoylethanolamine (PubMed:15655246, PubMed:17980170, PubMed:18793752, PubMed:30301806, PubMed:22825852).

Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine (PubMed:15655246).

Biological Process

Fatty acid metabolic process Source: UniProtKB
Lipid catabolic process Source: UniProtKB-KW
N-acylethanolamine metabolic process Source: UniProtKB
N-acylphosphatidylethanolamine metabolic process Source: UniProtKB
Sphingosine metabolic process Source: UniProtKB

Cellular Location

Lysosome
Other locations
Membrane

PTM

N-glycosylated (PubMed:17980170, PubMed:18793752, PubMed:30301806). Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine.
A disulfide bond is seen in the crystal structure of the human protein, but the Cys residues are not conserved in rodents.
Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and beta subunit (PubMed:15655246, PubMed:22040171, PubMed:17980170, PubMed:18793752, PubMed:30301806). Cleavage gives rise to a conformation change that activates the enzyme (PubMed:17980170, PubMed:18793752, PubMed:30301806, PubMed:22040171). The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates (PubMed:17980170, PubMed:18793752) (Probable).

Romano, B., Pagano, E., Iannotti, F. A., Piscitelli, F., Brancaleone, V., Lucariello, G., ... & Izzo, A. A. (2022). N‐Acylethanolamine acid amidase (NAAA) is dysregulated in colorectal cancer patients and its inhibition reduces experimental cancer growth. British Journal of Pharmacology, 179(8), 1679-1694.

Li, Y., Li, Y., Xu, S., Chen, Y., Zhou, P., Hu, T., ... & Lu, C. (2022). N-Acylethanolamine acid amidase (NAAA) exacerbates psoriasis inflammation by enhancing dendritic cell (DCs) maturation. Pharmacological Research, 185, 106491.

Malamas, M. S., Farah, S. I., Lamani, M., Pelekoudas, D. N., Perry, N. T., Rajarshi, G., ... & Makriyannis, A. (2020). Design and synthesis of cyanamides as potent and selective N-acylethanolamine acid amidase inhibitors. Bioorganic & Medicinal Chemistry, 28(1), 115195.

Piomelli, D., Scalvini, L., Fotio, Y., Lodola, A., Spadoni, G., Tarzia, G., & Mor, M. (2020). N-acylethanolamine acid amidase (NAAA): structure, function, and inhibition. Journal of Medicinal Chemistry, 63(14), 7475-7490.

Pontis, S., Palese, F., Summa, M., Realini, N., Lanfranco, M., De Mei, C., & Piomelli, D. (2020). N-Acylethanolamine Acid Amidase contributes to disease progression in a mouse model of multiple sclerosis. Pharmacological Research, 160, 105064.

Zhou, P., Xiang, L., Yang, Y., Wu, Y., Hu, T., Liu, X., ... & Li, Y. (2019). N-Acylethanolamine acid amidase (NAAA) inhibitor F215 as a novel therapeutic agent for osteoarthritis. Pharmacological Research, 145, 104264.

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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

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

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