Active • Host: Insect cells • AA: 2-935 (full length) • MW: 97.7 kDa
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ARMC5 (human, recombinant)

Item No. 45170

Product Insert (PDF)
Technical Information
Synonyms
  • Armadillo Repeat-containing Protein 5
Purity
≥90%
Endotoxin Testing
<1.0 EU per µg of the protein
Source
Active recombinant human ARMC5 expressed in insect cells
Amino Acids
2-935 (full length)
MW
97.7 kDa
50 mM Tris-HCl (pH 7.5), with 200 mM sodium chloride, 20% glycerol, and 1 mM DTT
UniProt Accession №
Q96C12
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Armadillo repeat-containing protein 5 (ARMC5) is a member of the armadillo (ARM) repeat containing family.1 It is composed of an N-terminal ARM repeat domain and C-terminal BTB/POZ domain that each act as scaffolds for protein-protein interactions. ARMC5 is ubiquitously expressed, localizes to the cytoplasm, and undergoes alternative splicing.1,2 It interacts with cullin 3 via the BTB domain to form an E3 ligase complex that ubiquitinates proteins such as sterol regulatory element binding protein (SREBP) and several RNA polymerase II subunits, including DNA-directed RNA polymerase II subunit (RPB1).3,4,5 ARMC5 is involved in T cell proliferation and differentiation, lung morphogenesis, adrenal cortex and neural tube development, and tumor suppression.1,4 Mutations in ARMC5 are associated with primary bilateral macronodular adrenal hyperplasia (PBMAH).6 Cayman’s ARMC5 (human, recombinant) protein can be used for enzyme activity assays and has a calculated molecular weight of 97.7 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Qu, Y., Yang, F., Deng, Y., et alAdvancements in the research of the structure, function, and disease-related roles of ARMC5. Front. Med. 19(2), 185-199 (2025).

    2. Berthon, A., Faucz, F., Bertherat, J., et alAnalysis of ARMC5 expression in human tissues. Mol. Cell. Endocrinol. 441, 140-145 (2017).

    3. Okuno, Y., Fukuhara, A., and Shimomura, I. The role of oxidative stress, glucocorticoid receptor and ARMC5 in lipid metabolism. Endocr. J. 71(12), 1097-1101 (2024).

    4. Luo, H., Lao, L., Au, K.S., et alARMC5 controls the degradation of most Pol II subunits, and ARMC5 mutation increases neural tube defect risks in mice and humans. Genome Biol. 25(1), 19 (2024).

    5. Lao, L., Bourdeau, I., Gagliardi, L., et alARMC5 is part of an RPB1-specific ubiquitin ligase implicated in adrenal hyperplasia. Nucleic Acids Res. 50(11), 6343-6367 (2022).

    6. Yu, L., Zhang, J., Guo, X., et alARMC5 mutations in familial and sporadic primary bilateral macronodular adrenal hyperplasia. PLoS One 13(1), e0191602 (2018).