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C57BL/6JCya-Reep2em1flox/Cya
Common Name:
Reep2-flox
Product ID:
S-CKO-06827
Background:
C57BL/6JCya
Product Type
Age
Genotype
Sex
Quantity
Price:
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Basic Information
Strain Name
Reep2-flox
Strain ID
CKOCMP-225362-Reep2-B6J-VA
Gene Name
Reep2
Product ID
S-CKO-06827
Gene Alias
--
Background
C57BL/6JCya
NCBI ID
225362
Modification
Conditional knockout
Chromosome
18
Phenotype
MGI:2385070
Document
Click here to download >>
Application
--
More
Rare Disease Data Center >>
Note
Note: When using this mouse strain in a publication, please cite “C57BL/6JCya-Reep2em1flox/Cya mice (Catalog S-CKO-06827) were purchased from Cyagen.”
Strain Description
Ensembl Number
ENSMUST00000043484
NCBI RefSeq
NM_144865
Target Region
Exon 4~8
Size of Effective Region
~3.0 kb
Detailed Document
Click here to download >>
Overview of Gene Research
Reep2, a member of the Receptor Expression-enhancing proteins (REEPs) family, is pivotal to the structure and function of the endoplasmic reticulum (ER) [1]. The REEP family is involved in many physiological and pathological processes such as ER morphogenesis, microtubule cytoskeleton regulation, and G protein-coupled receptor (GPCR) trafficking and expression [1]. Reep2 has been found to be preferentially expressed in neuronal and neuronal-like exocytotic tissues including brain, spinal cord, testes, pituitary, and adrenal gland [8].

Mutations in Reep2 have been identified as a cause of "pure" hereditary spastic paraplegias (HSPs), SPG72, with both autosomal dominant and autosomal recessive inheritance [2,5,7]. In a Nepalese family with early-onset pure-type HSP, a heterozygous Reep2 missense mutation (c.119T>G, p.Met40Arg) was found, with the proband presenting a slow and spastic gait from age 2 years [2]. Another study reported a de novo missense mutation (c.119T > G, p.Met40Arg) in a patient with pure hereditary spastic paraplegia [5]. Also, three mutations in Reep2 were identified in two families with HSP, where one missense variant (c.107T>A [p.Val36Glu]) had a dominant-negative effect in the autosomal-dominant family, inhibiting the normal binding of wild-type Reep2 to membranes, and a missense change (c.215T>A [p.Phe72Tyr]) in the recessive family decreased the affinity of the mutant protein for membranes [7]. Additionally, in nasopharyngeal carcinoma, Reep2 was upregulated compared to non-tumor samples, and high expression of Reep2 was associated with poor survival in patients [3]. Moreover, Reep2 enhances sweet receptor function by recruiting them into lipid raft microdomains near the taste cell's apical region, improving G-protein-coupled receptor signaling [4]. Chidamide suppresses adipogenic differentiation of bone marrow-derived mesenchymal stem cells via increasing Reep2 expression, indicating Reep2 is a negative regulator of adipogenic differentiation [6].

In conclusion, Reep2 plays essential roles in multiple biological processes. Its involvement in diseases such as hereditary spastic paraplegias and nasopharyngeal carcinoma, as well as its functions in taste receptor regulation and adipogenic differentiation, are revealed through genetic studies. Understanding Reep2's functions helps in comprehending the pathophysiological mechanisms of related diseases and may provide potential therapeutic targets.

References:
1. Fan, Sisi, Liu, Huimei, Li, Lanfang. 2022. The REEP family of proteins: Molecular targets and role in pathophysiology. In Pharmacological research, 185, 106477. doi:10.1016/j.phrs.2022.106477. https://pubmed.ncbi.nlm.nih.gov/36191880/
2. Nan, Haitian, Takaki, Ryusuke, Hata, Takanori, Koh, Kishin, Takiyama, Yoshihisa. 2021. A Nepalese family with an REEP2 mutation: clinical and genetic study. In Journal of human genetics, 66, 749-752. doi:10.1038/s10038-020-00882-x. https://pubmed.ncbi.nlm.nih.gov/33526816/
3. Wang, Yong, Peng, Lisha, Wang, Feng. 2024. M6A-mediated molecular patterns and tumor microenvironment infiltration characterization in nasopharyngeal carcinoma. In Cancer biology & therapy, 25, 2333590. doi:10.1080/15384047.2024.2333590. https://pubmed.ncbi.nlm.nih.gov/38532632/
4. Ilegems, Erwin, Iwatsuki, Ken, Kokrashvili, Zaza, Ninomiya, Yuzo, Margolskee, Robert F. . REEP2 enhances sweet receptor function by recruitment to lipid rafts. In The Journal of neuroscience : the official journal of the Society for Neuroscience, 30, 13774-83. doi:10.1523/JNEUROSCI.0091-10.2010. https://pubmed.ncbi.nlm.nih.gov/20943918/
5. Roda, Ricardo H, Schindler, Alice B, Blackstone, Craig. 2017. De novo REEP2 missense mutation in pure hereditary spastic paraplegia. In Annals of clinical and translational neurology, 4, 347-350. doi:10.1002/acn3.404. https://pubmed.ncbi.nlm.nih.gov/28491902/
6. Zhang, Xianning, Liu, Lulu, Liu, Xin, Zhang, Hao, Chen, Mingtai. 2023. Chidamide suppresses adipogenic differentiation of bone marrow derived mesenchymal stem cells via increasing REEP2 expression. In iScience, 26, 106221. doi:10.1016/j.isci.2023.106221. https://pubmed.ncbi.nlm.nih.gov/36879811/
7. Esteves, Typhaine, Durr, Alexandra, Mundwiller, Emeline, Stevanin, Giovanni, Darios, Frédéric. 2014. Loss of association of REEP2 with membranes leads to hereditary spastic paraplegia. In American journal of human genetics, 94, 268-77. doi:10.1016/j.ajhg.2013.12.005. https://pubmed.ncbi.nlm.nih.gov/24388663/
8. Hurt, Carl M, Björk, Susann, Ho, Vincent K, Hein, Lutz, Angelotti, Timothy. 2013. REEP1 and REEP2 proteins are preferentially expressed in neuronal and neuronal-like exocytotic tissues. In Brain research, 1545, 12-22. doi:10.1016/j.brainres.2013.12.008. https://pubmed.ncbi.nlm.nih.gov/24355597/
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
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