C57BL/6JCya-Prkd2em1/Cya
Common Name:
Prkd2-KO
Product ID:
S-KO-18191
Background:
C57BL/6JCya
Product Type
Age
Genotype
Sex
Quantity
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Basic Information
Strain Name
Prkd2-KO
Strain ID
KOCMP-101540-Prkd2-B6J-VB
Gene Name
Product ID
S-KO-18191
Gene Alias
PKD2
Background
C57BL/6JCya
NCBI ID
Modification
Conventional knockout
Chromosome
7
Phenotype
Document
Application
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Note: When using this mouse strain in a publication, please cite “C57BL/6JCya-Prkd2em1/Cya mice (Catalog S-KO-18191) were purchased from Cyagen.”
Strain Description
Ensembl Number
ENSMUST00000086104
NCBI RefSeq
NM_178900
Target Region
Exon 2~3
Size of Effective Region
~2.6 kb
Detailed Document
Overview of Gene Research
Prkd2, encoding the serine/threonine kinase protein kinase D2, is involved in multiple biological processes. It has been implicated in pathways such as Notch1, TP53/CDKN1A, and is crucial for the regulation of cell survival, proliferation, and differentiation. It also plays a role in processes like angiogenesis, insulin secretion, and T follicular helper cell differentiation [1,2,3,4,5,6]. Genetic models, especially knockout (KO) mouse models, have been valuable in studying Prkd2's functions.
In AML, knockdown of Prkd2 induced apoptosis and increased chemosensitivity, indicating it promotes AML cell proliferation and chemoresistance via the Notch1 pathway [1]. In cervical cancer, Prkd2 knockdown increased chemotherapy sensitivity through the TP53/CDKN1A pathway [2]. In mice, Prkd2 deficiency led to polyclonal hypergammaglobulinemia due to excessive T follicular helper cell development as Prkd2 and Bcl6 form a mutually inhibitory loop [3]. PRKD2 -KO rhesus monkeys and mice showed hyperinsulinemia, suggesting its role in insulin-related metabolic disorders [4].
In conclusion, Prkd2 is essential for various biological functions including cell growth, immune cell regulation, and metabolism. Studies using KO mouse models have revealed its significance in diseases such as AML, cervical cancer, and metabolic disorders, providing potential therapeutic targets for these conditions.
References:
1. Liu, Qian, Li, Wei, Zhou, Ying, Ji, Min, Ji, Chunyan. 2019. PRKD2 Promotes Progression and Chemoresistance of AML via Regulating Notch1 Pathway. In OncoTargets and therapy, 12, 10931-10941. doi:10.2147/OTT.S233234. https://pubmed.ncbi.nlm.nih.gov/31849496/
2. Feng, Ruijing, Wang, Xin, Chen, Hongwei, Ma, Ji, Gong, Danni. . Knockdown of PRKD2 Enhances Chemotherapy Sensitivity in Cervical Cancer via the TP53/CDKN1A Pathway. In Current cancer drug targets, 23, 159-170. doi:10.2174/1568009622666220822191039. https://pubmed.ncbi.nlm.nih.gov/36017858/
3. Misawa, Takuma, SoRelle, Jeffrey A, Choi, Jin Huk, Moresco, Eva Marie Y, Beutler, Bruce. . Mutual inhibition between Prkd2 and Bcl6 controls T follicular helper cell differentiation. In Science immunology, 5, . doi:10.1126/sciimmunol.aaz0085. https://pubmed.ncbi.nlm.nih.gov/31980486/
4. Xiao, Yao, Wang, Can, Chen, Jia-Yu, Li, Chuan-Yun, Zhang, Xiuqin. 2018. Deficiency of PRKD2 triggers hyperinsulinemia and metabolic disorders. In Nature communications, 9, 2015. doi:10.1038/s41467-018-04352-z. https://pubmed.ncbi.nlm.nih.gov/29789568/
5. Azoitei, Ninel, Fröhling, Stefan, Scholl, Claudia, Seufferlein, Thomas. 2015. PRKD2: A two-pronged kinase crucial for the tumor-supporting activity of HSP90. In Molecular & cellular oncology, 2, e981444. doi:10.4161/23723556.2014.981444. https://pubmed.ncbi.nlm.nih.gov/27308444/
6. Azoitei, Ninel, Diepold, Kristina, Brunner, Cornelia, Scholl, Claudia, Seufferlein, Thomas. 2014. HSP90 supports tumor growth and angiogenesis through PRKD2 protein stabilization. In Cancer research, 74, 7125-36. doi:10.1158/0008-5472.CAN-14-1017. https://pubmed.ncbi.nlm.nih.gov/25297628/
Quality Control Standard
Sperm Test
Pre-cryopreservation: Measurement of sperm concentration, determination of sperm viability.
Post-cryopreservation: A vial of cryopreserved sperms is selected for in-vitro fertilization from each batch.
Environmental Standards:SPF
Available Region:Global
Source:Cyagen