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Mouse Anti-LACC1 (AA 1-430) Recombinant Antibody (CBXF-2741) (CBMAB-F3458-CQ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-2741
Antibody Isotype
IgG
Application
ELISA, WB

Basic Information

Immunogen
FLJ38725 (AAH35749, 1aa-430aa) full-length recombinant protein with GST tag
Specificity
Human
Antibody Isotype
IgG
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
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 1-430

Target

Full Name
LACCASE DOMAIN CONTAINING 1
Entrez Gene ID
144811
UniProt ID
Q8IV20
Alternative Names
C13orf31; FAMIN
Function
Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine, guanosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine, guanine and hypoxanthine (PubMed:31978345).
Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (PubMed:31978345).
Also has adenosine deaminase activity (PubMed:31978345).
Acts as a regulator of innate immunity in macrophages by modulating the purine nucleotide metabolism, thereby regulating the metabolic function and bioenergetic state of macrophages (PubMed:31978345).
Enables a purine nucleotide cycle between adenosine and inosine monophosphate and adenylosuccinate that prevents cytoplasmic acidification and balances the cytoplasmic-mitochondrial redox interface (PubMed:31978345).
The purine nucleotide cycle consumes aspartate and releases fumarate in a manner involving fatty acid oxidation and ATP-citrate lyase activity (PubMed:31978345).
Participates in pattern recognition receptor (PRR)-induced cytokines in macrophages: associates with the NOD2-signaling complex and promotes optimal NOD2-induced signaling, cytokine secretion and bacterial clearance (PubMed:28593945, PubMed:31875558).
Localizes to the endoplasmic reticulum upon PRR stimulation of macrophages and associates with endoplasmic reticulum-stress sensors, promoting the endoplasmic reticulum unfolded protein response (UPR) (PubMed:31875558).
Does not show laccase activity (PubMed:27959965, PubMed:31978345).
Biological Process
Inflammatory responseIEA:UniProtKB-KW
Innate immune responseIEA:UniProtKB-KW
Nucleotide-binding oligomerization domain containing 2 signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Pattern recognition receptor signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of cytokine production involved in immune responseManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of cellular pHManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of inflammatory responseISS:UniProtKB
Regulation of purine nucleotide metabolic processISS:UniProtKB
Cellular Location
Cytoplasm
Nucleus
Endoplasmic reticulum
Peroxisome
Upon stimulation of the pattern-recognition receptor (PRR) NOD2, localizes to the endoplasmic reticulum.
Involvement in disease
Juvenile arthritis (JUVAR):
A rare, familial form of juvenile arthritis characterized by autosomal recessive inheritance and onset in early childhood of symmetric, chronic joint inflammation. It causes joint swelling, pain, stiffness and restricted joint movement. JUVAR has high clinical variability. Some patients exhibit systemic symptoms, including quotidian fever, erythematous rash, generalized lymphadenopathy, hepatomegaly, and/or splenomegaly. Others display polyarthritis without systemic inflammation.
PTM
Phosphorylated on tyrosine residues.
More Infomation

Wei, Z., Oh, J., Flavell, R. A., & Crawford, J. M. (2022). LACC1 bridges NOS2 and polyamine metabolism in inflammatory macrophages. Nature, 609(7926), 348-353.

Omarjee, O., Mathieu, A. L., Quiniou, G., Moreews, M., Ainouze, M., Frachette, C., ... & Belot, A. (2021). LACC1 deficiency links juvenile arthritis with autophagy and metabolism in macrophages. Journal of Experimental Medicine, 218(3), e20201006.

Al-Mayouf, S. M., Yateem, M., Al-Dusery, H., Monies, D., Wakil, S., AlShiakh, M., ... & Meyer, B. (2021). New or vanishing frontiers: LACC1-associated juvenile arthritis. International Journal of Pediatrics and Adolescent Medicine, 8(1), 44-47.

Kang, J. W., Yan, J., Ranjan, K., Zhang, X., Turner, J. R., & Abraham, C. (2020). Myeloid cell expression of LACC1 is required for bacterial clearance and control of intestinal inflammation. Gastroenterology, 159(3), 1051-1067.

Rabionet, R., Remesal, A., Mensa-Vilaró, A., Murías, S., Alcobendas, R., González-Roca, E., ... & Arostegui, J. I. (2019). Biallelic loss-of-function LACC1/FAMIN mutations presenting as rheumatoid factor-negative polyarticular juvenile idiopathic arthritis. Scientific Reports, 9(1), 4579.

Skon-Hegg, C., Zhang, J., Wu, X., Sagolla, M., Ota, N., Wuster, A., ... & Behrens, T. W. (2019). LACC1 regulates TNF and IL-17 in mouse models of arthritis and inflammation. The Journal of Immunology, 202(1), 183-193.

Huang, C., Hedl, M., Ranjan, K., & Abraham, C. (2019). LACC1 required for NOD2-induced, ER stress-mediated innate immune outcomes in human macrophages and LACC1 risk variants modulate these outcomes. Cell reports, 29(13), 4525-4539.

Szymanski, A. M., & Ombrello, M. J. (2018). Using genes to triangulate the pathophysiology of granulomatous autoinflammatory disease: NOD2, PLCG2 and LACC1. International Immunology, 30(5), 205-213.

Wang, D., Fan, Y., Malhi, M., Bi, R., Wu, Y., Xu, M., ... & Yao, Y. G. (2018). Missense variants in HIF1A and LACC1 contribute to leprosy risk in Han Chinese. The American Journal of Human Genetics, 102(5), 794-805.

Karacan, I., Uğurlu, S., Şahin, S., Everest, E., Kasapçopur, Ö., Tolun, A., ... & Turanli, E. T. (2018). LACC1 gene defects in familial form of juvenile arthritis. The Journal of Rheumatology, 45(5), 726-728.

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

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