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Mouse Anti-FKBP8 (AA 58-382) Recombinant Antibody (CBXF-2646) (CBMAB-F3066-CQ)

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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBXF-2646
Antibody Isotype
IgG2b
Application
WB

Basic Information

Immunogen
E. coli-derived recombinant human FKBP38, Met58-Gly382, Accession # Q14318
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b
Clonality
Monoclonal
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
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with trehalose
Concentration
LYOPH
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 58-382

Target

Full Name
FK506 Binding Protein 8
Introduction
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. Unlike the other members of the family, this encoded protein does not seem to have PPIase/rotamase activity. It may have a role in neurons associated with memory function.
Entrez Gene ID
Human23770
Mouse14232
Rat290652
UniProt ID
HumanQ14318
MouseO35465
RatQ3B7U9
Alternative Names
FK506 Binding Protein 8; FK506-Binding Protein 8 (38kD); FK506 Binding Protein 8, 38kDa; 38 KDa FK506-Binding Protein; PPIase FKBP8; 38 KDa FKBP; Rotamase; FKBPr38;
Function
Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.
Biological Process
Apoptotic process Source: UniProtKB-KW
Camera-type eye development Source: Ensembl
Cell fate specification Source: Ensembl
Dorsal/ventral neural tube patterning Source: Ensembl
Intracellular signal transduction Source: ProtInc
Multicellular organism growth Source: Ensembl
Negative regulation of apoptotic process Source: Ensembl
Negative regulation of protein phosphorylation Source: CAFA
Positive regulation of BMP signaling pathway Source: Ensembl
Protein folding Source: MGI
Regulation of gene expression Source: Ensembl
Smoothened signaling pathway Source: Ensembl
Cellular Location
Mitochondrion; Mitochondrion membrane
Isoform 1: Mitochondrion membrane
Isoform 3: Mitochondrion membrane
Topology
Helical: 390-410
PTM
Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
More Infomation

Zuo, L., Kuo, W. T., Cao, F., Chanez-Paredes, S. D., Zeve, D., Mannam, P., ... & Turner, J. R. (2022). Tacrolimus-binding protein FKBP8 directs myosin light chain kinase-dependent barrier regulation and is a potential therapeutic target in Crohn’s disease. Gut.

Aguilera, M. O., Robledo, E., Melani, M., Wappner, P., & Colombo, M. I. (2022). FKBP8 is a novel molecule that participates in the regulation of the autophagic pathway. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1869(5), 119212.

Lv, S., Zhao, X., Zhang, E., Yan, Y., Ma, X., Li, N., ... & Song, T. (2022). Lysine demethylase KDM1A promotes cell growth via FKBP8–BCL2 axis in hepatocellular carcinoma. Journal of Biological Chemistry, 298(9).

Zhang, J., Yin, Y., Wang, J., Zhang, J., Liu, H., Feng, W., ... & Xu, Y. (2021). Prohibitin regulates mTOR pathway via interaction with FKBP8. Frontiers of Medicine, 15, 448-459.

Yoo, S. M., Yamashita, S. I., Kim, H., Na, D., Lee, H., Kim, S. J., ... & Jung, Y. K. (2020). FKBP8 LIRL‐dependent mitochondrial fragmentation facilitates mitophagy under stress conditions. The FASEB Journal, 34(2), 2944-2957.

Tian, T., Cao, X., Kim, S. E., Lin, Y. L., Steele, J. W., Cabrera, R. M., ... & Lei, Y. (2020). FKBP8 variants are risk factors for spina bifida. Human molecular genetics, 29(18), 3132-3144.

Hsu, F. F., Chou, Y. T., Chiang, M. T., Li, F. A., Yeh, C. T., Lee, W. H., & Chau, L. Y. (2019). Signal peptide peptidase promotes tumor progression via facilitating FKBP8 degradation. Oncogene, 38(10), 1688-1701.

Xu, S. S., Xu, L. G., Yuan, C., Li, S. N., Chen, T., Wang, W., ... & Rao, H. (2019). FKBP8 inhibits virus‐induced RLR‐VISA signaling. Journal of Medical Virology, 91(3), 482-492.

Peng, Y. J., Lee, Y. C., Fu, S. J., Chien, Y. C., Liao, Y. F., Chen, T. Y., ... & Tang, C. Y. (2018). FKBP8 enhances protein stability of the CLC-1 chloride channel at the plasma membrane. International journal of molecular sciences, 19(12), 3783.

Misaka, T., Murakawa, T., Nishida, K., Omori, Y., Taneike, M., Omiya, S., ... & Otsu, K. (2018). FKBP8 protects the heart from hemodynamic stress by preventing the accumulation of misfolded proteins and endoplasmic reticulum-associated apoptosis in mice. Journal of Molecular and Cellular Cardiology, 114, 93-104.

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

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