ULK2 Antibody (YA4362)
(Synonyms: ATG1B; Unc51.2)ULK2 Antibody (YA4362) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to ULK2.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, FC, ELISA
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS with 0.05% sodium azide
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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FC
FC: Flow Cytometry
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|
| Dilution Ratio | 1:500-1:2000 | 1:200-1:400 | 1:10000 |
Product Details
ULK2 Antibody (YA4362) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to ULK2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 113 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 113 kDa
Purified recombinant fragment of human ULK2 (AA: 1-155) expressed in E. Coli.
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS with 0.05% sodium azide
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
ULK2 (unc-51-like kinase 2) is a serine/threonine protein kinase that functions as a core regulator of autophagy, particularly under nutrient-deprived conditions, and acts upstream of the class III phosphatidylinositol 3-kinase machinery that supports autophagosome formation[1][2]. Mechanistically, ULK2 participates in the autophagy-initiation network together with ATG13 and FIP200 and contributes to starvation-induced autophagic signaling through pathways linked to AMPK and mTOR regulation[3][4]. In experimental systems, ULK1 and ULK2 display substantial functional overlap, and nutrient-dependent autophagy is most effectively suppressed when both kinases are absent, demonstrating their cooperative role in autophagy induction[3][2]. Disease-related interest in ULK2 arises from the broad involvement of autophagy in cancer, inflammatory disorders, and other pathologies in which cellular adaptation to metabolic stress is critical. Compared with the closely related isoform ULK1, ULK2 shares major structural and functional characteristics but may exhibit distinct regulatory interactions and biological functions, indicating that the two kinases are not completely redundant[5]. For experimental applications, pharmacological inhibitors targeting ULK1/2 signaling are widely used to investigate autophagy mechanisms; compounds such as MRT68921 inhibit both ULK1 and ULK2 with nanomolar potency and suppress autophagic activity in cellular models[6].
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Subcellular Localization
Cytoplasmic vesicle membrane; Peripheral membrane protein
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Subunit
Interacts with SYNGAP1 (By similarity). Component of a complex consisting of ATG13/KIAA0652, ULK1 and RB1CC1/FIP200. Interacts (via C-terminus) with ATG13/KIAA0652. Associates with the mammalian target of rapamycin complex 1 (mTORC1) through an interaction with RPTOR
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SwissProt ID
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Synonyms
ATG1B; Unc51.2
Documentation
References
[1]. Uniprotkb.
[2]. Lee EJ, et al. The requirement of uncoordinated 51-like kinase 1 (ULK1) and ULK2 in the regulation of autophagy. Autophagy. 2011 Jul;7(7):689-95. [Content Brief]
[3]. Alers S, et al. Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks. Mol Cell Biol. 2012 Jan;32(1):2-11. [Content Brief]
[4]. Ganley IG, et al. ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy. J Biol Chem. 2009 May 1;284(18):12297-305. [Content Brief]
[5]. Demeter A, et al. ULK1 and ULK2 are less redundant than previously thought: computational analysis uncovers distinct regulation and functions of these autophagy induction proteins. Sci Rep. 2020 Jul 2;10(1):10940. [Content Brief]
[6]. Egan DF, et al. Small Molecule Inhibition of the Autophagy Kinase ULK1 and Identification of ULK1 Substrates. Mol Cell. 2015 Jul 16;59(2):285-97. [Content Brief]