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Rabbit Anti-FNIP1 Recombinant Antibody (CBXF-1070) (CBMAB-F0933-CQ)

This product is a rabbit antibody that recognizes FNIP1. The antibody CBXF-1070 can be used for immunoassay techniques such as: WB, IHC-P, IF.
See all FNIP1 antibodies

Summary

Host Animal
Rabbit
Specificity
Human
Clone
CBXF-1070
Antibody Isotype
IgG
Application
WB, IHC-P, IF

Basic Information

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!]

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
Folliculin Interacting Protein 1
Introduction
This gene encodes a protein that binds to the tumor suppressor protein folliculin and to AMP-activated protein kinase (AMPK). The encoded protein participates in the regulation of cellular metabolism and nutrient sensing by modulating the AMPK and target of rapamycin signaling pathways. This gene has a closely related paralog that encodes a protein with similar binding activities. Both related proteins also associate with the molecular chaperone heat shock protein-90 (Hsp90) and negatively regulate its ATPase activity and facilitate its association with folliculin.
Entrez Gene ID
96459
UniProt ID
Q8TF40
Alternative Names
Folliculin Interacting Protein 1; KIAA1961;
Function
Binding partner of the GTPase-activating protein FLCN: involved in the cellular response to amino acid availability by regulating the mTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3 (PubMed:17028174, PubMed:18663353, PubMed:24081491).

In low-amino acid conditions, component of the lysosomal folliculin complex (LFC) on the membrane of lysosomes, which inhibits the GTPase-activating activity of FLCN, thereby inactivating mTORC1 and promoting nuclear translocation of TFEB and TFE3 (By similarity).

Upon amino acid restimulation, disassembly of the LFC complex liberates the GTPase-activating activity of FLCN, leading to activation of mTORC1 and subsequent cytoplasmic retention of TFEB and TFE3 (By similarity).

Required to promote FLCN recruitment to lysosomes and interaction with Rag GTPases (PubMed:24081491).

Together with FLCN, regulates autophagy: following phosphorylation by ULK1, interacts with GABARAP and promotes autophagy (PubMed:25126726).

In addition to its role in mTORC1 signaling, also acts as a co-chaperone of HSP90AA1/Hsp90: following gradual phosphorylation by CK2, inhibits the ATPase activity of HSP90AA1/Hsp90, leading to activate both kinase and non-kinase client proteins of HSP90AA1/Hsp90 (PubMed:27353360, PubMed:30699359).

Acts as a scaffold to load client protein FLCN onto HSP90AA1/Hsp90 (PubMed:27353360).

Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360).

Also acts as a core component of the reductive stress response by inhibiting activation of mitochondria in normal conditions: in response to reductive stress, the conserved Cys degron is reduced, leading to recognition and polyubiquitylation by the CRL2(FEM1B) complex, followed by proteasomal (By similarity).

Required for B-cell development (By similarity).
Biological Process
Cellular response to starvation Source: UniProtKB
Immature B cell differentiation Source: UniProtKB
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Negative regulation of TOR signaling Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of B cell apoptotic process Source: UniProtKB
Positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
Positive regulation of protein-containing complex assembly Source: ParkinsonsUK-UCL
Positive regulation of protein phosphorylation Source: UniProtKB
Positive regulation of TOR signaling Source: UniProtKB
Regulation of pro-B cell differentiation Source: UniProtKB
Regulation of protein phosphorylation Source: UniProtKB
TOR signaling Source: UniProtKB
Cellular Location
Lysosome membrane; Cytosol. Localizes to lysosome membrane in amino acid-depleted conditions and relocalizes to the cytosol upon refeeding (PubMed:29848618). Colocalizes with FLCN in the cytoplasm (PubMed:18663353).
PTM
Sequential phosphorylation by CK2 promotes its gradual interaction with HSP90AA1/Hsp90 (PubMed:30699359). Priming phosphorylation at Ser-938 is followed by relay phosphorylation at Ser-939, Ser-941, Ser-946 and Ser-948, promoting its gradual interaction with HSP90AA1/Hsp90 (PubMed:30699359). This leads to incremental inhibition of HSP90AA1/Hsp90 ATPase activity and gradual activation of both kinase and non-kinase clients (PubMed:30699359). Dephosphorylated by protein phosphatase 5 (PP5), promoting glycosylation by OGT (PubMed:30699359). Phosphorylated by AMPK (PubMed:17028174).
GlcNAcylation at Ser-938 by OGT following dephosphorylation by protein phosphatase 5 (PP5) promotes ubiquitination and degradation by the proteasome.
Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties at Lys-1119 following glycosylation by OGT, leading to its degradation by the proteasome (PubMed:30699359). Ubiquitinated by the CRL2(FEM1B) complex in response to reductive stress: reductive stress causes reduction of the conserved Cys degron in FNIP1, leading to recognition by the CRL2(FEM1B), subsequent FNIP1 degradation, and activation of mitochondria to recalibrate reactive oxygen species (ROS) (By similarity).
Oxidation of the Cys degron in normal conditions promotes its stabilization by preventing recognition and ubiquitination by the CRL2(FEM1B) complex.

van de Beek, I., Glykofridis, I. E., Tanck, M. W., Luijten, M. N., Starink, T. M., Balk, J. A., ... & Waisfisz, Q. (2023). Familial multiple discoid fibromas is linked to a locus on chromosome 5 including the FNIP1 gene. Journal of human genetics, 1-7.

Yin, Y., Xu, D., Mao, Y., Xiao, L., Sun, Z., Liu, J., ... & Gan, Z. (2022). FNIP1 regulates adipocyte browning and systemic glucose homeostasis in mice by shaping intracellular calcium dynamics. Journal of Experimental Medicine, 219(5), e20212491.

Yin, Y., Xu, D., Mao, Y., & Gan, Z. (2022). Comments on ‘FNIP1 regulates adipocyte browning and systemic glucose homeostasis in mice by shaping intracellular calcium dynamics’. Journal of Molecular Cell Biology, 14(5), mjac033.

Xiao, L., Liu, J., Sun, Z., Yin, Y., Mao, Y., Xu, D., ... & Gan, Z. (2021). AMPK-dependent and-independent coordination of mitochondrial function and muscle fiber type by FNIP1. PLoS Genetics, 17(3), e1009488.

Glykofridis, I. E., Knol, J. C., Balk, J. A., Westland, D., Pham, T. V., Piersma, S. R., ... & Wolthuis, R. M. (2021). Loss of FLCN-FNIP1/2 induces a non-canonical interferon response in human renal tubular epithelial cells. elife, 10, e61630.

Niehues, T., Özgür, T. T., Bickes, M., Waldmann, R., Schöning, J., Bräsen, J., ... & Viemann, D. (2020). Mutations of the gene FNIP1 associated with a syndromic autosomal recessive immunodeficiency with cardiomyopathy and pre‐excitation syndrome. European journal of immunology, 50(7), 1078-1080.

Sager, R. A., Woodford, M. R., Backe, S. J., Makedon, A. M., Baker-Williams, A. J., DiGregorio, B. T., ... & Mollapour, M. (2019). Post-translational regulation of FNIP1 creates a rheostat for the molecular chaperone Hsp90. Cell reports, 26(5), 1344-1356.

Centini, R., Tsang, M., Iwata, T., Park, H., Delrow, J., Margineantu, D., ... & Iritani, B. M. (2018). Loss of Fnip1 alters kidney developmental transcriptional program and synergizes with TSC1 loss to promote mTORC1 activation and renal cyst formation. PLoS One, 13(6), e0197973.

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

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