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Mouse Anti-MARK2 Recombinant Antibody (3C5) (CBMAB-A5307-LY)

The product is antibody recognizes MARK2. The antibody 3C5 immunoassay techniques such as: WB, ELISA.
See all MARK2 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
3C5
Antibody Isotype
IgG2a, κ
Application
WB, ELISA

Basic Information

Immunogen
MARK2 (AAH08771, 401 a.a. ~ 500 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, κ
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!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
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
Microtubule Affinity Regulating Kinase 2
Introduction
This gene encodes a member of the Par-1 family of serine/threonine protein kinases. The protein is an important regulator of cell polarity in epithelial and neuronal cells, and also controls the stability of microtubules through phosphorylation and inactivation of several microtubule-associating proteins. The protein localizes to cell membranes. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq]
Entrez Gene ID
UniProt ID
Alternative Names
EMK1; MGC99619; PAR-1; Par1b
Function
Serine/threonine-protein kinase (PubMed:23666762).

Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762).

Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells.
Biological Process
Activation of protein kinase activity Source: ParkinsonsUK-UCL
Autophagy of mitochondrion Source: ParkinsonsUK-UCL
Axon development Source: ARUK-UCL
Establishment of cell polarity Source: UniProtKB
Establishment or maintenance of cell polarity regulating cell shape Source: ARUK-UCL
Establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
Intracellular signal transduction Source: UniProtKB
Microtubule cytoskeleton organization Source: GO_Central
Mitochondrion localization Source: ParkinsonsUK-UCL
Neuron migration Source: UniProtKB
Peptidyl-serine phosphorylation Source: ARUK-UCL
Peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
Positive regulation of neuron projection development Source: UniProtKB
Protein autophosphorylation Source: UniProtKB
Protein phosphorylation Source: UniProtKB
Regulation of axonogenesis Source: UniProtKB
Regulation of cytoskeleton organization Source: UniProtKB
Regulation of microtubule binding Source: ARUK-UCL
Regulation of microtubule cytoskeleton organization Source: ARUK-UCL
Wnt signaling pathway Source: UniProtKB-KW
Cellular Location
Plasma membrane
Cell membrane
Lateral cell membrane
Cytoskeleton
Cytoplasm and Cytosol
Cytoplasm
Other locations
dendrite
Note: Phosphorylation at Thr-596 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm.
PTM
Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-212 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation by CaMK1 promotes activity and is required to promote neurite outgrowth. Phosphorylation at Thr-596 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity and promotes binding to 14-3-3 protein YWHAZ, leading to relocation from cell membrane to cytoplasm.

Ponnusamy, L., Natarajan, S. R., & Manoharan, R. (2022). MARK2 potentiate aerobic glycolysis‐mediated cell growth in breast cancer through regulating mTOR/HIF‐1α and p53 pathways. Journal of Cellular Biochemistry, 123(4), 759-771.

Pasapera, A. M., Heissler, S. M., Eto, M., Nishimura, Y., Fischer, R. S., Thiam, H. R., & Waterman, C. M. (2022). MARK2 regulates directed cell migration through modulation of myosin II contractility and focal adhesion organization. Current Biology, 32(12), 2704-2718.

Natarajan, S. R., Ponnusamy, L., & Manoharan, R. (2022). MARK2/4 promotes Warburg effect and cell growth in non-small cell lung carcinoma through the AMPKα1/mTOR/HIF-1α signaling pathway. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1869(7), 119242.

Zeng, Y., Yin, L., Zhou, J., Zeng, R., Xiao, Y., Black, A. R., ... & Dong, J. (2022). MARK2 regulates chemotherapeutic responses through class IIa HDAC-YAP axis in pancreatic cancer. Oncogene, 41(31), 3859-3875.

Lu, Y. N., Kavianpour, S., Zhang, T., Zhang, X., Nguyen, D., Thombre, R., ... & Wang, J. (2021). MARK2 phosphorylates eIF2α in response to proteotoxic stress. PLoS biology, 19(3), e3001096.

Wei, X., Xu, L., Jeddo, S. F., Li, K., Li, X., & Li, J. (2020). MARK2 enhances cisplatin resistance via PI3K/AKT/NF-κB signaling pathway in osteosarcoma cells. American journal of translational research, 12(5), 1807.

Xu, L., Sun, Z., Wei, X., Tan, H., Kong, P., Li, Z., ... & Li, J. (2020). The inhibition of MARK2 suppresses cisplatin resistance of osteosarcoma stem cells by regulating DNA damage and repair. Journal of Bone Oncology, 23, 100290.

Drange, O. K., Smeland, O. B., Shadrin, A. A., Finseth, P. I., Witoelar, A., Frei, O., ... & Andreassen, O. A. (2019). Genetic overlap between Alzheimer’s disease and bipolar disorder implicates the MARK2 and VAC14 genes. Frontiers in neuroscience, 13, 220.

Ichinose, S., Ogawa, T., Jiang, X., & Hirokawa, N. (2019). The spatiotemporal construction of the axon initial segment via KIF3/KAP3/TRIM46 transport under MARK2 signaling. Cell Reports, 28(9), 2413-2426.

DiBona, V. L., Zhu, W., Shah, M. K., Rafalia, A., Ben Cheikh, H., Crockett, D. P., & Zhang, H. (2019). Loss of Par1b/MARK2 primes microglia during brain development and enhances their sensitivity to injury. Journal of neuroinflammation, 16, 1-15.

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

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