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Rat Anti-DYNLL1 Recombinant Antibody (10D6) (CBMAB-D2005-YC)

Provided herein is a Rat monoclonal antibody, which binds to Dynein Light Chain LC8-Type 1 (DYNLL1). The antibody can be used for immunoassay techniques, such as FC, WB.
See all DYNLL1 antibodies

Summary

Host Animal
Rat
Specificity
Human, Mouse
Clone
10D6
Antibody Isotype
IgM
Application
FC, WB

Basic Information

Immunogen
Recombinant mouse DLC1 [LC8, PIN]
Specificity
Human, Mouse
Antibody Isotype
IgM
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!]

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
dynein, light chain, LC8-type 1
Introduction
DYNLL1 is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of DYNLL1 destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity.
Entrez Gene ID
Human8655
Mouse56455
UniProt ID
HumanP63167
MouseP63168
Alternative Names
DYNLL1 is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of DYNLL1 destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity.
Research Area
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.

Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.

Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.

Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.
Biological Process
Apoptotic process Source: UniProtKB-KW
Cilium assembly Source: GO_Central
Microtubule-based process Source: InterPro
Negative regulation of nitric oxide biosynthetic process Source: Ensembl
Negative regulation of phosphorylation Source: UniProtKB
Positive regulation of ATP-dependent microtubule motor activity, plus-end-directed Source: GO_Central
Positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
Spermatid development Source: Ensembl
Substantia nigra development Source: UniProtKB
Cellular Location
Mitochondrion; Centrosome; Cytoskeleton; Nucleus. Upon induction of apoptosis translocates together with BCL2L11 to mitochondria.
PTM
Phosphorylation at Ser-88 appears to control the dimer-monomer transition. According to PubMed:15193260, it is phosphorylated at Ser-88 by PAK1, however, according to PubMed:18650427, the DYNLL1 dimer is not accessible for PAK1 and the phosphorylation could not be demonstrated in vitro.

Li, Q., Zhang, Z., Jiang, H., Hou, J., Chai, Y., Nan, H., ... & Wang, L. (2022). DLEU1 promotes cell survival by preventing DYNLL1 degradation in esophageal squamous cell carcinoma. Journal of translational medicine, 20(1), 1-15.

Berkel, C., & Cacan, E. (2021). Involvement of ATMIN-DYNLL1-MRN axis in the progression and aggressiveness of serous ovarian cancer. Biochemical and Biophysical Research Communications, 570, 74-81.

Liu, R., King, A., Tarlinton, D., & Heierhorst, J. (2021). The ASCIZ-DYNLL1 Axis Is Essential for TLR4-Mediated Antibody Responses and NF-κB Pathway Activation. Molecular and Cellular Biology, 41(12), e00251-21.

Berkel, C., & Cacan, E. (2020). DYNLL1 is hypomethylated and upregulated in a tumor stage-and grade-dependent manner and associated with increased mortality in hepatocellular carcinoma. Experimental and Molecular Pathology, 117, 104567.

Berkel, C., & Cacan, E. (2020). In silico analysis of DYNLL1 expression in ovarian cancer chemoresistance. Cell Biology International, 44(8), 1598-1605.

He, Y. J., Meghani, K., Caron, M. C., Yang, C., Ronato, D. A., Bian, J., ... & Chowdhury, D. (2019). Abstract GMM-027: DYNLL1 INHIBITS DNA END RESECTION IN BRCA1-DEFICIENT CELLS AND REGULATES PARP INHIBITOR SENSITIVITY. Clinical Cancer Research, 25(22_Supplement), GMM-027.

West, K. L., Kelliher, J. L., Xu, Z., An, L., Reed, M. R., Eoff, R. L., ... & Leung, J. W. (2019). LC8/DYNLL1 is a 53BP1 effector and regulates checkpoint activation. Nucleic acids research, 47(12), 6236-6249.

Becker, J. R., Cuella-Martin, R., Barazas, M., Liu, R., Oliveira, C., Oliver, A. W., ... & Chapman, J. R. (2018). The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity. Nature communications, 9(1), 1-12.

He, Y. J., Meghani, K., Caron, M. C., Yang, C., Ronato, D. A., Bian, J., ... & Chowdhury, D. (2018). DYNLL1 binds to MRE11 to limit DNA end resection in BRCA1-deficient cells. Nature, 563(7732), 522-526.

Myllykoski, M., Eichel, M. A., Jung, R. B., Kelm, S., Werner, H. B., & Kursula, P. (2018). High‐affinity heterotetramer formation between the large myelin‐associated glycoprotein and the dynein light chain DYNLL 1. Journal of neurochemistry, 147(6), 764-783.

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

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