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Mouse Anti-CDKN1B Recombinant Antibody (0.N.491) (CBMAB-P0188-YC)


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Summary

Host Animal
Mouse
Specificity
Human, Dog, Mouse, Rat
Clone
0.N.491
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, IHC-P

Basic Information

Immunogen
Full length p27 Kip1 of mouse.
Host Species
Mouse
Specificity
Human, Dog, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
IHC-P1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
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
Cyclin Dependent Kinase Inhibitor 1B
Introduction
CDKN1B is a cyclin-dependent kinase inhibitor, which shares a limited similarity with CDK inhibitor CDKN1A/p21. The encoded protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and thus controls the cell cycle progression at G1. The degradation of this protein, which is triggered by its CDK dependent phosphorylation and subsequent ubiquitination by SCF complexes, is required for the cellular transition from quiescence to the proliferative state.
Entrez Gene ID
Human1027
Mouse12576
Rat83571
Dog403429
UniProt ID
HumanP46527
MouseP46414
RatO08769
DogF1PGU6
Alternative Names
Cyclin Dependent Kinase Inhibitor 1B; Cyclin-Dependent Kinase Inhibitor 1B (P27, Kip1); P27KIP1; KIP1; Cyclin-Dependent Kinase Inhibitor P27; Cyclin-Dependent Kinase Inhibitor 1B; CDKN4; MEN1B; MEN4;
Function
Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (PubMed:28666995).
Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry.
Biological Process
Autophagic cell death Source: BHF-UCL
Cell cycle arrest Source: HGNC-UCL
Cellular response to lithium ion Source: MGI
Cytokine-mediated signaling pathway Source: Reactome
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
G1/S transition of mitotic cell cycle Source: BHF-UCL
Heart development Source: BHF-UCL
Mitotic cell cycle arrest Source: UniProtKB
Negative regulation of cardiac muscle tissue regeneration Source: BHF-UCL
Negative regulation of cell cycle Source: UniProtKB
Negative regulation of cell growth Source: BHF-UCL
Negative regulation of cell population proliferation Source: UniProtKB
Negative regulation of cyclin-dependent protein kinase activity Source: CAFA
Negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
Negative regulation of kinase activity Source: UniProtKB
Negative regulation of mitotic cell cycle Source: UniProtKB
Negative regulation of phosphorylation Source: BHF-UCL
Negative regulation of transcription, DNA-templated Source: UniProtKB
Negative regulation of vascular associated smooth muscle cell proliferation Source: BHF-UCL
Positive regulation of cell cycle Source: Reactome
Positive regulation of cell death Source: UniProtKB
Positive regulation of protein catabolic process Source: MGI
Regulation of cell cycle G1/S phase transition Source: GO_Central
Regulation of cyclin-dependent protein serine/threonine kinase activity Source: GO_Central
Cellular Location
Endosome; Nucleus; Cytoplasm. Nuclear and cytoplasmic in quiescent cells. AKT- or RSK-mediated phosphorylation on Thr-198, binds 14-3-3, translocates to the cytoplasm and promotes cell cycle progression. Mitogen-activated UHMK1 phosphorylation on Ser-10 also results in translocation to the cytoplasm and cell cycle progression. Phosphorylation on Ser-10 facilitates nuclear export. Translocates to the nucleus on phosphorylation of Tyr-88 and Tyr-89. Colocalizes at the endosome with SNX6; this leads to lysosomal degradation (By similarity).
Involvement in disease
Multiple endocrine neoplasia 4 (MEN4): Multiple endocrine neoplasia (MEN) syndromes are inherited cancer syndromes of the thyroid. MEN4 is a MEN-like syndrome with a phenotypic overlap of both MEN1 and MEN2.
PTM
Phosphorylated; phosphorylation occurs on serine, threonine and tyrosine residues. Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G0-G1 phase and leads to protein stability. Phosphorylation on other sites is greatly enhanced by mitogens, growth factors, cMYC and in certain cancer cell lines. The phosphorylated form found in the cytoplasm is inactivate. Phosphorylation on Thr-198 is required for interaction with 14-3-3 proteins. Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation. Tyrosine phosphorylation promotes this process. Phosphorylation by PKB/AKT1 can be suppressed by LY294002, an inhibitor of the catalytic subunit of PI3K. Phosphorylation on Tyr-88 and Tyr-89 has no effect on binding CDK2, but is required for binding CDK4. Dephosphorylated on tyrosine residues by G-CSF.
Ubiquitinated; in the cytoplasm by the KPC complex (composed of RNF123/KPC1 and UBAC1/KPC2) and, in the nucleus, by SCF(SKP2). The latter requires prior phosphorylation on Thr-187. Ubiquitinated; by a TRIM21-containing SCF(SKP2)-like complex; leads to its degradation.
Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation (By similarity).
More Infomation

Yang, H., Zhang, L., & Wang, Q. (2021). MicroRNA-221-3p alleviates cell apoptosis and inflammatory response by targeting cyclin dependent kinase inhibitor 1B in chronic obstructive pulmonary disease. Bioengineered, 12(1), 5705-5715.

Guo, H., Luo, X., Sun, L., Li, J., & Cui, S. (2021). Cyclin-dependent kinase inhibitor 1B acts as a novel molecule to mediate testosterone synthesis and secretion in mouse Leydig cells by luteinizing hormone (LH) signaling pathway. In Vitro Cellular & Developmental Biology-Animal, 57(7), 742-752.

Li, C., Liu, Z., Zhou, J., Meng, X., Liu, S., Li, W., ... & Liu, H. (2020). Insulin-like growth factor-I prevents hypoxia-inducible factor-1 alpha-dependent G1/S arrest by activating cyclin E/cyclin-dependent kinase2 via the phoshatidylinositol-3 kinase/AKT/forkhead box O1/Cdkn1b pathway in porcine granulosa cells. Biology of reproduction, 102(1), 116-132.

Hu, X. H., Zhao, Z. X., Dai, J., Geng, D. C., & Xu, Y. Z. (2019). MicroRNA‐221 regulates osteosarcoma cell proliferation, apoptosis, migration, and invasion by targeting CDKN1B/p27. Journal of cellular biochemistry, 120(3), 4665-4674.

Wang, Z., Zhu, H., Shi, H., Zhao, H., Gao, R., Weng, X., ... & Ge, J. (2019). Exosomes derived from M1 macrophages aggravate neointimal hyperplasia following carotid artery injuries in mice through miR-222/CDKN1B/CDKN1C pathway. Cell death & disease, 10(6), 1-15.

Stevenson, M., Olinger, E., Debaix, H., Vogt, B., Devuyst, O., & Thakker, R. (2019, November). A cyclin dependent kinase inhibitor 1B missense mutation (Pro69Leu) is associated with familial hypomagnesaemia, but not multiple endocrine neoplasia type 4 (MEN4). In Society for Endocrinology BES 2019 (Vol. 65). BioScientifica.

Liu, J., Yu, J., Jiang, W., He, M., & Zhao, J. (2019). Targeting of CDKN 1B by miR‐222‐3p may contribute to the development of intervertebral disc degeneration. FEBS open bio, 9(4), 728-735.

Ale-Agha, N., Goy, C., Jakobs, P., Spyridopoulos, I., Gonnissen, S., Dyballa-Rukes, N., ... & Haendeler, J. (2018). CDKN1B/p27 is localized in mitochondria and improves respiration-dependent processes in the cardiovascular system—New mode of action for caffeine. PLoS biology, 16(6), e2004408.

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

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