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Rabbit Anti-LARP1 Recombinant Antibody (CBYJL-1191) (CBMAB-L0695-YJ)

Provided herein is a Rabbit monoclonal antibody, which binds to La Ribonucleoprotein Domain Family Member 1 (LARP1). The antibody can be used for immunoassay techniques, such as WB, IP.
See all LARP1 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Monkey
Clone
CBYJL-1191
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Specificity
Human, Monkey
Antibody Isotype
IgG
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
La ribonucleoprotein domain family, member 1
Introduction
Among its related pathways are Translational Control. Gene Ontology (GO) annotations related to LARP1 include translation initiation factor binding. An important paralog of LARP1 is LARP1B. LARP1 is a RNA-binding protein that promotes translation of specific classes of mRNAs downstream of the mTORC1 complex. Associates with the mRNA 5cap in an MTOR-dependent manner and associates with mRNAs containing a 5 terminal oligopyrimidine (5TOP) motif, which is present in mRNAs encoding for ribosomal proteins and several components of the translation machinery. Associates with actively translating ribosomes via interaction with PABPC1/PABP and stimulates translation of mRNAs containing a 5TOP, thereby regulating cell growth and proliferation. Positively regulates the replication of dengue virus (DENV).
Entrez Gene ID
Human23367
Monkey714714
UniProt ID
HumanQ6PKG0
MonkeyG7P8S4
Alternative Names
LARP
Function
RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (PubMed:20430826, PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797, PubMed:28673543, PubMed:29244122).
Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (PubMed:23711370, PubMed:25940091, PubMed:28650797, PubMed:29244122, PubMed:26206669, PubMed:28379136).
The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 (PubMed:25940091, PubMed:28650797, PubMed:29244122, PubMed:28379136).
When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (PubMed:25940091, PubMed:28650797).
Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif (PubMed:28379136).
Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543).
Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (PubMed:23711370, PubMed:28650797).
Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (PubMed:20430826, PubMed:24532714).
Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826, PubMed:23711370, PubMed:25940091, PubMed:28673543).
(Microbial infection) Positively regulates the replication of dengue virus (DENV).
Biological Process
Cell population proliferationManual Assertion Based On ExperimentIMP:UniProtKB
Cellular response to rapamycinManual Assertion Based On ExperimentIMP:UniProtKB
mRNA stabilizationManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of translationManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of translational initiationManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of macroautophagyManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of translationManual Assertion Based On ExperimentIBA:GO_Central
Positive regulation of translational initiationManual Assertion Based On ExperimentIMP:CACAO
Positive regulation of viral genome replicationManual Assertion Based On ExperimentIMP:UniProtKB
Posttranscriptional regulation of gene expressionManual Assertion Based On ExperimentIDA:FlyBase
Response to amino acid starvationManual Assertion Based On ExperimentIMP:UniProtKB
TOR signalingManual Assertion Based On ExperimentIMP:UniProtKB
TORC1 signalingManual Assertion Based On ExperimentIMP:UniProtKB
Translational initiationManual Assertion Based On ExperimentIMP:UniProtKB
Cellular Location
Cytoplasm
Cytoplasmic granule
Colocalizes with RPTOR and PABPC1 in cytoplasmic granules that resemble stress granules.
PTM
Phosphorylated on multiple Ser and Thr residues in response to active mTORC1. Phosphorylation is important for interaction with RPTOR and the mTORC1 complex. Phosphorylation promotes dissociation from the 5'UTR of mRNA molecules with a 5'TOP motif.

Ogami, K., Oishi, Y., Sakamoto, K., Okumura, M., Yamagishi, R., Inoue, T., ... & Hoshino, S. I. (2022). mTOR-and LARP1-dependent regulation of TOP mRNA poly (A) tail and ribosome loading. Cell reports, 41(4).

Mattijssen, S., Kozlov, G., Fonseca, B. D., Gehring, K., & Maraia, R. J. (2021). LARP1 and LARP4: up close with PABP for mRNA 3’poly (A) protection and stabilization. RNA biology, 18(2), 259-274.

Jia, J. J., Lahr, R. M., Solgaard, M. T., Moraes, B. J., Pointet, R., Yang, A. D., ... & Fonseca, B. D. (2021). mTORC1 promotes TOP mRNA translation through site-specific phosphorylation of LARP1. Nucleic acids research, 49(6), 3461-3489.

Wu, M., Kong, C., Cai, M., Huang, W., Chen, Y., Wang, B., & Liu, X. (2021). Hsa_circRNA_002144 promotes growth and metastasis of colorectal cancer through regulating miR-615-5p/LARP1/mTOR pathway. Carcinogenesis, 42(4), 601-610.

Al-Ashtal, H. A., Rubottom, C. M., Leeper, T. C., & Berman, A. J. (2021). The LARP1 La-Module recognizes both ends of TOP mRNAs. RNA biology, 18(2), 248-258.

Smith, E. M., Benbahouche, N. E. H., Morris, K., Wilczynska, A., Gillen, S., Schmidt, T., ... & Bushell, M. (2021). The mTOR regulated RNA-binding protein LARP1 requires PABPC1 for guided mRNA interaction. Nucleic acids research, 49(1), 458-478.

Philippe, L., van den Elzen, A. M., Watson, M. J., & Thoreen, C. C. (2020). Global analysis of LARP1 translation targets reveals tunable and dynamic features of 5′ TOP motifs. Proceedings of the National Academy of Sciences, 117(10), 5319-5328.

Han, J., Zhao, G., Ma, X., Dong, Q., Zhang, H., Wang, Y., & Cui, J. (2018). CircRNA circ-BANP-mediated miR-503/LARP1 signaling contributes to lung cancer progression. Biochemical and Biophysical Research Communications, 503(4), 2429-2435.

Fonseca, B. D., Lahr, R. M., Damgaard, C. K., Alain, T., & Berman, A. J. (2018). LARP1 on TOP of ribosome production. Wiley Interdisciplinary Reviews: RNA, 9(5), e1480.

Philippe, L., Vasseur, J. J., Debart, F., & Thoreen, C. C. (2018). La-related protein 1 (LARP1) repression of TOP mRNA translation is mediated through its cap-binding domain and controlled by an adjacent regulatory region. Nucleic acids research, 46(3), 1457-1469.

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

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