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Mouse Anti-AJUBA Recombinant Antibody (V2-180369) (CBMAB-A1839-YC)

Provided herein is a Mouse monoclonal antibody against Human Ajuba LIM Protein. The antibody can be used for immunoassay techniques, such as IP, WB.
See all AJUBA antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-180369
Antibody Isotype
IgG1
Application
IP, WB

Basic Information

Immunogen
Full length Human Ajuba fused to maltose binding protein.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100

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

Format
Liquid
Buffer
PBS
Preservative
0.1% sodium azide
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.

Target

Full Name
Ajuba LIM Protein
Introduction
Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adh
Entrez Gene ID
84962
UniProt ID
Q96IF1
Alternative Names
Ajuba LIM Protein; JUB; Jub, Ajuba Homolog (Xenopus Laevis); LIM Domain-Containing Protein Ajuba; Jub, Ajuba Homolog;
Function
Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adhesion, cell differentiation, proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell-cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1.
Biological Process
Calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: Ensembl
Cellular protein localization Source: Ensembl
Cytoskeleton organization Source: GO_Central
Focal adhesion assembly Source: Ensembl
G2/M transition of mitotic cell cycle Source: Reactome
Gene silencing by miRNA Source: MGI
Glycerophospholipid biosynthetic process Source: Ensembl
Lamellipodium assembly Source: Ensembl
Negative regulation of hippo signaling Source: UniProtKB
Negative regulation of kinase activity Source: Ensembl
Negative regulation of transcription by RNA polymerase II Source: Ensembl
Positive regulation of cellular biosynthetic process Source: Ensembl
Positive regulation of gene silencing by miRNA Source: UniProtKB
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
Positive regulation of MAP kinase activity Source: Ensembl
Positive regulation of protein-containing complex assembly Source: MGI
Regulation of cell migration Source: Ensembl
Regulation of cellular response to hypoxia Source: UniProtKB
Regulation of GTPase activity Source: Ensembl
Regulation of transcription, DNA-templated Source: GO_Central
Response to hypoxia Source: UniProtKB
Wound healing, spreading of epidermal cells Source: Ensembl
Cellular Location
Cell membrane; Cytoskeleton; Centrosome; Nucleus; Cell junction; P-body. Shuttles between the cytoplasm and the nucleus. Localizes on centrosomes during G2-M phase. Preferentially co- localizes with cadherin-adhesive complexes at sites of cell-cell contacts. Colocalizes with GFI1 in the nucleus.
PTM
Phosphorylated by LATS2 during mitosis. Phosphorylated by AURKA.

Wu, Z., Zou, X., Xu, Y., Zhou, F., Kuai, R., Li, J., ... & Peng, H. (2021). Ajuba transactivates N‐cadherin expression in colorectal cancer cells through interaction with Twist. Journal of Cellular and Molecular Medicine.

Dommann, N., Sánchez-Taltavull, D., Eggs, L., Birrer, F., Brodie, T., Salm, L., ... & Stroka, D. (2020). The LIM Protein Ajuba Augments Tumor Metastasis in Colon Cancer. Cancers, 12(7), 1913.

Zhang, C., Wei, S., Sun, W. P., Teng, K., Dai, M. M., Wang, F. W., ... & Xie, D. (2020). Super-enhancer-driven AJUBA is activated by TCF4 and involved in epithelial-mesenchymal transition in the progression of hepatocellular carcinoma. Theranostics, 10(20), 9066.

Xu, B., Li, Q., Chen, N., Zhu, C., Meng, Q., Ayyanathan, K., ... & Hou, Z. (2019). The LIM protein Ajuba recruits DBC1 and CBP/p300 to acetylate ERα and enhances ERα target gene expression in breast cancer cells. Nucleic acids research, 47(5), 2322-2335.

Bi, L., Ma, F., Tian, R., Zhou, Y., Lan, W., Song, Q., & Cheng, X. (2018). AJUBA increases the cisplatin resistance through hippo pathway in cervical cancer. Gene, 644, 148-154.

Fowler, S., Maguin, P., Kalan, S., & Loayza, D. (2018). LIM Protein Ajuba associates with the RPA complex through direct cell cycle-dependent interaction with the RPA70 subunit. Scientific reports, 8(1), 1-13.

Jia, H., Song, L., Cong, Q., Wang, J., Xu, H., Chu, Y., ... & Hou, Z. (2017). The LIM protein AJUBA promotes colorectal cancer cell survival through suppression of JAK1/STAT1/IFIT2 network. Oncogene, 36(19), 2655-2666.

Zhang, M., Singh, R., Peng, S., Mazumdar, T., Sambandam, V., Shen, L., ... & Johnson, F. M. (2017). Mutations of the LIM protein AJUBA mediate sensitivity of head and neck squamous cell carcinoma to treatment with cell-cycle inhibitors. Cancer letters, 392, 71-82.

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

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