Recombinant Human LATS1 Protein

Name: Recombinant Human LATS1 Protein
Brand: Beta LifeScience
SKU: BL-0538SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_004690
Synonym	WARTS; wts
Background	LATS1 is a putative serine/threonine kinase that localizes to the mitotic apparatus and complexes with cell cycle controller CDC2 kinase in early mitosis which is phosphorylated in a cell-cycle dependent manner. The N-terminal region of the protein binds CDC2 to form a complex showing reduced H1 histone kinase activity which indicating a role as a negative regulator of CDC2/cyclin A and the C-terminal kinase domain binds to its own N-terminal region, suggesting potential negative regulation through interference with complex formation via intramolecular binding (1). LATS1 act as a tumor suppressor and play an important role in the development of soft-tissue sarcomas, ovarian stromal cell tumors and a high sensitivity to carcinogenic treatments (2).
Description	Recombinant human LATS1 (589-end) was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	589a.a.-end
Molecular Weight	~95 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human LATS1 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDK1 kinase activity. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. May also play a role in endocrine function. Plays a role in mammary gland epithelial cell differentiation, both through the Hippo signaling pathway and the intracellular estrogen receptor signaling pathway by promoting the degradation of ESR1.
Subcellular Location	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Midbody. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Protein Families	Protein kinase superfamily, AGC Ser/Thr protein kinase family
Database References	HGNC: 6514 OMIM: 603473 KEGG: hsa:9113 STRING: 9606.ENSP00000253339 UniGene: PMID: 29438698 Knockdown of Lats1/2 prevented the cytoplasmic delocalization of Yap1/Taz proteins in response to AICAR. PMID: 29730476 Results provide evidence that LATS1 undergoes intronic premature polyadenylation (pPA) following large internal exons, and that N(6)-methyladenosine levels in this exon are reduced in pPA-activated breast cancer cells. PMID: 29362392 TNFAIP8 regulates Hippo pathway through interacting with LATS1 to promote cell proliferation. PMID: 28926138 The TAZ WW domain exhibits a binding preference for the second of the two PPxY motifs of LATS1 in vitro. We modelled the structure of the domain in complex with LATS1 PPxY2 peptide and, through molecular dynamics simulations, show that WW domain-PPxY2 complex is stable with some flexibility in the peptide region. PMID: 29787761 These results suggest that LMO3 promotes hepatocellular carcinoma (HCC) cell invasion and anoikis inhibition by interacting with LATS1 and suppressing Hippo signaling. LMO3 may serve as a potential therapeutic target for HCC in future. PMID: 30219064 FOXP4-AS1 is overexpressed in osteosarcoma (OS), and is the independent risk factor in OS prognosis. Upregulated FOXP4-AS1 promotes the proliferation, migration and cell cycle, but inhibits apoptosis of OS cells. Furthermore, FOXP4-AS1 participates in the development and progression of OS by downregulating LATS1 via binding to LSD1 and EZH2. PMID: 29859193 Results confirmed that S100A1 interacted with LATS1. LATS1 depletion significantly reduced the effects of S100A1 on cell growth rate and apoptosis, and there was a positive correlation between phosphorylated LATS1 and S100A1 in hepatocellular carcinoma (HCC) clinical samples, indicating that LATS1 was responsible for the S100A1-induced changes in cancer cell growth and Hippo signaling. PMID: 29901195 Knockdown of LATS1 attenuated the suppression of FUS overexpression on hepatocellular carcinoma progression, and LATS1 expression was positively correlated with FUS expression in hepatocellular carcinoma tissues. PMID: 30308519 YAP1 and LATS1 can be considered as new prognostic factors in clear cell renal cell carcinoma. PMID: 29850494 lncARSR interacts with Yes-associated protein (YAP) to block its phosphorylation by LATS1, facilitating YAP nuclear translocation. PMID: 27886176 LATS1 is an independent prognostic factor and may play an important role in non-Small Cell Lung Cancer progression and may serve as a novel therapeutic target of non-Small Cell Lung Cancer. PMID: 28434174 Increased miR-424 expression or decreased LATS1 expression was associated with pathological stage and unfavorable prognosis of GC patients. PMID: 28893265 Deregulation of LATS1 and YAP1 expression is associated with clear cell renal cell carcinoma progression and poor patient survival. PMID: 28504812 In the present study, we investigated the expression of activated core Hippo pathway kinases (pMST1/2 and pLATS1/2) in a series of 57 HER2-positve and triple-negative breast cancer patients who received neoadjuvant therapy . PMID: 28387539 LATS1/2 signaling via the Hippo pathway regulates human megakaryocytic differentiation. PMID: 27786336 Our findings suggest that LATS1 is a potential candidate tumor suppressor and inhibits the growth and metastasis of gastric carcinoma cells via downregulation of the YAP signaling. PMID: 26921249 Low LATS1 expression is associated with breast cancer. PMID: 28754671 Loss of LATS1 expression is associated with pancreatic cancer. PMID: 28720576 TNFAIP8 regulates Hippo (MST1/2) signaling through its interaction with LATS1. PMID: 28152516 Lats1 SUMOylation at K751 suppresses its kinase activity and subsequently attenuates its tumor-suppressor functions in HepG2 cells. PMID: 27847303 High LATS1 expression is associated with Colorectal Tumorigenesis and Metastasis. PMID: 27325643 A group of miRNAs have been demonstrated to directly target components of the Hippo signaling pathway, such as YAP, TAZ and LATS1/2 in oncogenesis. (Review) PMID: 27973704 findings reveal a non-canonical (that is, YAP/TAZ-independent) effect of LATS in the regulation of human breast cell fate PMID: 28068668 AGO2 immunoprecipitation revealed LATS1 as a novel proapoptotic target of miR-21 in T cells. PMID: 28075055 LATS1 was downregulated in cervical cancer and may suppress cell growth and invasion through regulating the expression of cyclin E, p27, MMP9 and YAP. PMID: 28259899 PARD3 promotes interaction between PP1A and LATS1 to induce LATS1 dephosphorylation and inactivation,leading to dephosphorylation and activation of TAZ PMID: 26116754 Loss of LATS1 expression is associated with breast neoplasms. PMID: 25772246 Phosphorylation of CHO1 at S716 by Lats1 regulate its centrosomal localization, and that phosphorylated CHO1 interacts with and activates LIMK1 during early mitosis. PMID: 25786116 LATS1 phosphorylates the Thr7 residue of the APC/C component CDC26 directly PMID: 25723520 These results demonstrated that as an inhibitor of YAP, LATS1 was decreased via downregulation of YAP using RNAi. This therefore indicated that the change in YAP levels in hepatocellular carcinoma cells may regulate LATS1 in a feedback manner. PMID: 25625370 LATS1 promoter hypermethylation is associated with oral squamous cell carcinomas. PMID: 25743838 results reported here further support that LATS1/2 act normally as tumor suppressors and loss of their functions contributes to human cancer development PMID: 25482410 Phosphorylation of S716 NDR/LATS, present only in the longest Kif23 isoform, is required for phosphorylation at S814, revealing phosphorylation at these two sites, and differential regulation of Kif23-14-3-3 interaction for the two Kif23 isoforms. PMID: 25658096 Findings suggest that polyomavirus middle T-antigen (PyMT) activates the Hippo pathway tumor suppressor Lats in a Src-dependent manner. PMID: 25362852 LATS1 and LATS2 kinases play an important role in the regulation of NS5A function through site-specific post-translational modification and that phosphorylation of Ser/Thr71 is essential for optimal viral genome replication. PMID: 25044019 ITCH up-regulation and LATS1 down-regulation were closely associated with tumorigenesis and progression of SCC PMID: 25618271 Both LATS1 and LATS2 were not related with the clinical variables in mucinous and clear cell carcinoma PMID: 25841306 The control of LATS activation by angiotensin II and subsequent YAP localization is important for podocyte homeostasis and survival. PMID: 25393475 both LATS1 demethylation and overexpression of LATS1 downregulated the expression of Yes-associated protein (YAP), inhibited cell proliferation, induced cell apoptosis and cell cycle G1 arrest in 786-O cells PMID: 25270913 ivation of MSH4 in germ cells may have played a role in the acquisition of additional TP53 and LATS1 germline mutations in a Li-Fraumeni family PMID: 25041856 overexpression of Kibra rescues the increased cell migration and aberrant three-dimensional morphogenesis induced by knockdown of PTPN14, and this rescue is mediated through the activation of the upstream LATS1 kinase PMID: 25023289 Data indicate that tumour suppressor RASSF1A triggers large tumor suppressor kinase 1 (LATS)-CDK2 interaction and restricts CDK2 kinase activity towards BRCA2. PMID: 25218637 These results indicate that LATS1 may play an important role in NSCLC, and may serve as a novel therapeutic target of non-small-cell lung cancer (NSCLC). PMID: 24682895 NF2 loss-driven derepressed CRL4(DCAF1) promotes activation of YAP by inhibiting hippo pathwat kinases Lats1 and 2 in the nucleus. PMID: 25026211 LATS1 and LATS2 mutations from cancers can lead to loss or reduction of their growth-inhibitory activity PMID: 24026096 In conclusion, N-terminally truncated Lats1 induced Lats2 downregulation and Yap protein accumulation, leading to chromosomal instability and tumorigenesis. PMID: 23230145 These results collectively suggest that the Hippo pathway negatively regulates the actin-binding activity of Amot family members through direct phosphorylation. PMID: 24225952 Thus AMOT is a direct substrate of Lats1/2 mediating functions of the Hippo pathway in endothelial cell migration and angiogenesis. PMID: 24106267 Decreased expression of LATS1 in CRC is associated with promoter hypermethylation, but not microsatellite instability status PMID: 23885148

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Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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