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Mouse Anti-DYNLL1 Recombinant Antibody (4/PIN) (CBMAB-P0287-YC)

Provided herein is a Mouse monoclonal antibody against Human Dynein Light Chain LC8-Type 1. The antibody can be used for immunoassay techniques, such as WB, IF.
See all DYNLL1 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Rat
Clone
4/PIN
Antibody Isotype
IgG1
Application
WB, IF

Basic Information

Immunogen
Rat PIN, AA 1-89
Specificity
Human, Rat
Antibody Isotype
IgG1
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
Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record 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 this protein 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
Rat58945
UniProt ID
HumanP63167
RatP63170
Alternative Names
LC8a; PIN; Pin; 8kDLC; Dnclc1; LC8; hdlc1; DLC8; DNCLC1; DLC1; DNCL1; Dlc8
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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