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Mouse Anti-LITAF Recombinant Antibody (CBYJL-1791) (CBMAB-L1727-YJ)

Provided herein is a Mouse monoclonal antibody, which binds to Lipopolysaccharide Induced Tnf Factor (LITAF). The antibody can be used for immunoassay techniques, such as FC, ELISA, WB.
See all LITAF antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYJL-1791
Antibody Isotype
IgG2b
Application
FC, ELISA, WB

Basic Information

Specificity
Human
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!]

Buffer
PBS, pH 7.4
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
LITAF
Introduction
Lipopolysaccharide is a potent stimulator of monocytes and macrophages, causing secretion of tumor necrosis factor-alpha (TNF-alpha) and other inflammatory mediators. This gene encodes lipopolysaccharide-induced TNF-alpha factor, which is a DNA-binding protein and can mediate the TNF-alpha expression by direct binding to the promoter region of the TNF-alpha gene. The transcription of this gene is induced by tumor suppressor p53 and has been implicated in the p53-induced apoptotic pathway. Mutations in this gene cause Charcot-Marie-Tooth disease type 1C (CMT1C) and may be involved in the carcinogenesis of extramammary Paget's disease (EMPD). Multiple alternatively spliced transcript variants have been found for this gene. Diseases associated with LITAF include Charcot-Marie-Tooth Disease, Demyelinating, Type 1C and Tooth Disease. Among its related pathways are Lysosome and NF-kappaB Signaling.
Entrez Gene ID
9516
UniProt ID
Q99732
Alternative Names
PIG7; SIMPLE; TP53I7
Function
Plays a role in endosomal protein trafficking and in targeting proteins for lysosomal degradation (PubMed:23166352).
Plays a role in targeting endocytosed EGFR and ERGG3 for lysosomal degradation, and thereby helps down-regulate downstream signaling cascades (PubMed:23166352).
Helps recruit the ESCRT complex components TSG101, HGS and STAM to cytoplasmic membranes (PubMed:23166352).
Probably plays a role in regulating protein degradation via its interaction with NEDD4 (PubMed:15776429).
May also contribute to the regulation of gene expression in the nucleus (PubMed:10200294, PubMed:15793005).
Binds DNA (in vitro) and may play a synergistic role with STAT6 in the nucleus in regulating the expression of various cytokines (PubMed:15793005).
May regulate the expression of numerous cytokines, such as TNF, CCL2, CCL5, CXCL1, IL1A and IL10 (PubMed:10200294, PubMed:15793005).
Biological Process
Cellular response to lipopolysaccharideIEA:Ensembl
Negative regulation of NIK/NF-kappaB signalingIEA:Ensembl
Positive regulation of I-kappaB kinase/NF-kappaB signalingManual Assertion Based On ExperimentHMP:UniProtKB
Positive regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIMP:NTNU_SB
Regulation of cytokine productionManual Assertion Based On ExperimentIBA:GO_Central
Cellular Location
Cytoplasm
Nucleus
Lysosome membrane
Early endosome membrane
Late endosome membrane
Endosome membrane
Cell membrane
Golgi apparatus membrane
Associated with membranes of lysosomes, early and late endosomes (PubMed:11274176, PubMed:27927196, PubMed:27582497).
Can translocate from the cytoplasm into the nucleus (PubMed:15793005).
Detected at Schmidt-Lanterman incisures and in nodal regions of myelinating Schwann cells (By similarity).
Involvement in disease
Charcot-Marie-Tooth disease 1C (CMT1C):
A dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet.
Defects in LITAF may be involved in extramammary Paget disease (EMPD) carcinogenesis. EMPD is a cancerous disease representing about 8% of all malignant skin cancers; it usually appears in the anogenital area and can be fatal by metastasizing to internal organs when left untreated for a long time. The clinical features are usually those of eczematous eruptions with weeping and crust formation.
PTM
Phosphorylated on tyrosine residues in response to EGF.

Avinery, L., Gahramanov, V., Hesin, A., & Sherman, M. Y. (2022). Hsp70–Bag3 Module Regulates Macrophage Motility and Tumor Infiltration via Transcription Factor LITAF and CSF1. Cancers, 14(17), 4168.

Chen, K., Tian, J., Wang, J., Jia, Z., Zhang, Q., Huang, W., ... & Zou, J. (2021). Lipopolysaccharide-induced TNFα factor (LITAF) promotes inflammatory responses and activates apoptosis in zebrafish Danio rerio. Gene, 780, 145487.

Chi, Z., Gao, Q., Sun, Y., Zhou, F., Wang, H., Shu, X., & Zhang, M. (2021). LINC00473 downregulation facilitates trophoblast cell migration and invasion via the miR‐15a‐5p/LITAF axis in pre‐eclampsia. Environmental toxicology, 36(8), 1618-1627.

Wang, Q., Sun, Q., Wang, J., Qiu, X., Qi, R., & Huang, J. (2021). Lactobacillus plantarum 299v changes miRNA expression in the intestines of piglets and leads to downregulation of LITAF by regulating ssc-miR-450a. Probiotics and Antimicrobial Proteins, 13(4), 1093-1105.

Liu, J., Zuo, Z., Sastalla, I., Liu, C., Jang, J. Y., Sekine, Y., ... & Liu, S. (2020). Sequential CRISPR-based screens identify LITAF and CDIP1 as the Bacillus cereus hemolysin BL toxin host receptors. Cell host & microbe, 28(3), 402-410.

Turan, N. N., Moshal, K. S., Roder, K., Baggett, B. C., Kabakov, A. Y., Dhakal, S., ... & Koren, G. (2020). The endosomal trafficking regulator LITAF controls the cardiac Nav1. 5 channel via the ubiquitin ligase NEDD4-2. Journal of Biological Chemistry, 295(52), 18148-18159.

Huang, C., Chen, D., Zhu, H., Lv, S., Li, Q., & Li, G. (2019). LITAF enhances radiosensitivity of human glioma cells via the FoxO1 pathway. Cellular and Molecular Neurobiology, 39, 871-882.

Li, R., Wang, N., Xue, M., Long, W., Cheng, C., Mi, C., & Gao, Z. (2019). A potential regulatory network among WDR86-AS1, miR-10b-3p, and LITAF is possibly involved in preeclampsia pathogenesis. Cellular Signalling, 55, 40-52.

Zhou, Y., Huang, J., Yu, X., Jiang, X., Shi, Y., Weng, Y., ... & Lu, C. (2018). LITAF is a potential tumor suppressor in pancreatic cancer. Oncotarget, 9(3), 3131.

Hoey, C., Ray, J., Jeon, J., Huang, X., Taeb, S., Ylanko, J., ... & Liu, S. K. (2018). mi RNA‐106a and prostate cancer radioresistance: a novel role for LITAF in ATM regulation. Molecular oncology, 12(8), 1324-1341.

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

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