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Rabbit Anti-CLK2 Recombinant Antibody (EG732) (CBMAB-EN886-LY)

The product is antibody recognizes CLK2. The antibody EG732 immunoassay techniques such as: WB: 1:500~1:1000 ELISA: 1:20000.
See all CLK2 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat
Clone
EG732
Antibody Isotype
IgG
Application
WB: 1:500~1:1000 ELISA: 1:20000

Basic Information

Immunogen
The antibody was produced against synthesized peptide derived from internal of human CLK2.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
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!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
CDC Like Kinase 2
Introduction
This gene encodes a dual specificity protein kinase that phosphorylates serine/threonine and tyrosine-containing substrates. Activity of this protein regulates serine- and arginine-rich (SR) proteins of the spliceosomal complex, thereby influencing alternative transcript splicing. Chromosomal translocations have been characterized between this locus and the PAFAH1B3 (platelet-activating factor acetylhydrolase 1b, catalytic subunit 3 (29kDa)) gene on chromosome 19, resulting in the production of a fusion protein. Note that this gene is distinct from the TELO2 gene (GeneID:9894), which shares the CLK2 alias, but encodes a protein that is involved in telomere length regulation. There is a pseudogene for this gene on chromosome 7. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2014]
Entrez Gene ID
Human1196
Mouse12748
Rat365842
UniProt ID
HumanP49760
MouseO35491
RatQ5XI98
Alternative Names
CDC Like Kinase 2; CDC-Like Kinase 2; EC 2.7.12.1;
Function
Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Phosphorylates PAGE4 at several serine and threonine residues and this phosphorylation attenuates the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (PubMed:28289210).
Biological Process
Negative regulation of gluconeogenesis Source: UniProtKB
Protein autophosphorylation Source: UniProtKB
Protein phosphorylation Source: UniProtKB
Regulation of RNA splicing Source: UniProtKB
Response to ionizing radiation Source: UniProtKB
Cellular Location
Nucleus
Isoform 1: Nucleus; Nucleus speckle. Inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle.
Isoform 2: Nucleus speckle. Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles.
PTM
Autophosphorylates on all three types of residues. Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin. Phosphorylation plays a critical role in cell proliferation following low dose radiation and prevents cell death following high dose radiation. Phosphorylation at Thr-344 by PKB/AKT2 induces its kinase activity which is required for its stability. The phosphorylation status at Ser-142 influences its subnuclear localization; inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle.

Qin, Z., Qin, L., Feng, X., Li, Z., & Bian, J. (2021). Development of Cdc2-like Kinase 2 Inhibitors: Achievements and Future Directions. Journal of Medicinal Chemistry, 64(18), 13191-13211.

Liu, B., Kong, X., Wang, R., & Xin, C. (2021). CLK2 promotes occurrence and development of non-small cell lung cancer. Journal of BU ON.: Official Journal of the Balkan Union of Oncology, 26(1), 58-64.

Licciardello, M. P., & Workman, P. (2021). A New Chemical Probe Challenges the Broad Cancer Essentiality of CK2. Trends in Pharmacological Sciences.

Yazici, Y., McAlindon, T. E., Gibofsky, A., Lane, N. E., Clauw, D., Jones, M., ... & Hochberg, M. C. (2020). Lorecivivint, a Novel Intraarticular CDC‐like Kinase 2 and Dual‐Specificity Tyrosine Phosphorylation‐Regulated Kinase 1A Inhibitor and Wnt Pathway Modulator for the Treatment of Knee Osteoarthritis: A Phase II Randomized Trial. Arthritis & Rheumatology, 72(10), 1694-1706.

Wu, Z. X., Yang, Y., Wang, G., Wang, J. Q., Teng, Q. X., Sun, L., ... & Zou, C. (2020). Dual TTK/CLK2 inhibitor, CC‐671, selectively antagonizes ABCG2‐mediated multidrug resistance in lung cancer cells. Cancer Science, 111(8), 2872.

Deshmukh, V., O'Green, A. L., Bossard, C., Seo, T., Lamangan, L., Ibanez, M., ... & Yazici, Y. (2019). Modulation of the Wnt pathway through inhibition of CLK2 and DYRK1A by lorecivivint as a novel, potentially disease-modifying approach for knee osteoarthritis treatment. Osteoarthritis and cartilage, 27(9), 1347-1360.

Hatting, M., Rines, A. K., Luo, C., Tabata, M., Sharabi, K., Hall, J. A., ... & Puigserver, P. (2017). Adipose tissue CLK2 promotes energy expenditure during high-fat diet intermittent fasting. Cell metabolism, 25(2), 428-437.

Quaresma, P. G. F., Weissmann, L., Zanotto, T. M., Santos, A. C., De Matos, A. H. B., Furigo, I. C., ... & Prada, P. O. (2017). Cdc2-like kinase 2 in the hypothalamus is necessary to maintain energy homeostasis. International Journal of Obesity, 41(2), 268-278.

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

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