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Mouse Anti-HSD17B4 Recombinant Antibody (CBFYH-2010) (CBMAB-H3022-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-2010
Antibody Isotype
IgG1
Application
IF, IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
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
Buffer
PBS, PH 7.3, 1% BSA, 50% glycerol
Preservative
0.02% Sodium azide
Concentration
1 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
hydroxysteroid (17-beta) dehydrogenase 4
Introduction
The protein encoded by this gene is a bifunctional enzyme that is involved in the peroxisomal beta-oxidation pathway for fatty acids. It also acts as a catalyst for the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids. Defects in this gene that affect the peroxisomal fatty acid beta-oxidation activity are a cause of D-bifunctional protein deficiency (DBPD). An apparent pseudogene of this gene is present on chromosome 8. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Entrez Gene ID
3295
UniProt ID
P51659
Alternative Names
Hydroxysteroid 17-Beta Dehydrogenase 4; 17-Beta-Hydroxysteroid Dehydrogenase 4; 3-Alpha,7-Alpha,12-Alpha-Trihydroxy-5-Beta-Cholest-24-Enoyl-CoA Hydratase; Short Chain Dehydrogenase/Reductase Family 8C Member 1; 17beta-Estradiol Dehydrogenase Type IV; Peroxisomal Multifunctional Protein 2; D-Bifunctional Protein, Peroxisomal; D-3-Hydroxyacyl-CoA Dehydratase; Beta-Hydroxyacyl Dehydrogenase; Multifunctional Protein 2; Beta-Keto-Reductase; 17-Beta-HSD IV; 17-Beta-HSD 4
Function
Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from straight-chain, 2-methyl-branched-chain fatty acids bile acid intermediates. With EHHADH, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (PubMed:10671535).
Biological Process
Androgen metabolic process Source: UniProtKB
Estrogen metabolic process Source: UniProtKB
Fatty acid beta-oxidation Source: UniProtKB
Medium-chain fatty-acyl-CoA metabolic process Source: UniProtKB
Osteoblast differentiation Source: UniProtKB
Sertoli cell development Source: Ensembl
Very long-chain fatty acid metabolic process Source: Ensembl
Very long-chain fatty-acyl-CoA metabolic process Source: UniProtKB
Cellular Location
Peroxisome
Involvement in disease
D-bifunctional protein deficiency (DBPD):
Disorder of peroxisomal fatty acid beta-oxidation.
Perrault syndrome 1 (PRLTS1):
A sex-influenced disorder characterized by sensorineural deafness in both males and females and ovarian dysgenesis in females. Some patients also have neurologic manifestations, including mild mental retardation and cerebellar and peripheral nervous system involvement.
More Infomation

Arai, N., Hattori, N., Yamashita, S., Liu, Y. Y., Ebata, T., Takeuchi, C., ... & Ushijima, T. (2023). HSD17B4 methylation enhances glucose dependence of BT-474 breast cancer cells and increases lapatinib sensitivity. Breast Cancer Research and Treatment, 1-12.

Chen, S., Du, L., Lei, Y., Lin, Y., Chen, S., & Liu, Y. (2021). Two novel HSD17B4 heterozygous mutations in association with D-Bifunctional protein deficiency: a case report and literature review. Frontiers in Pediatrics, 9, 679597.

Lee, S. A., Lee, J., Kim, K., Moon, H., Min, C., Moon, B., ... & Park, D. (2021). The peroxisomal localization of Hsd17b4 is regulated by its interaction with phosphatidylserine. Molecules and Cells, 44(4), 214.

Yamashita, S., Hattori, N., Fujii, S., Yamaguchi, T., Takahashi, M., Hozumi, Y., ... & Mukai, H. (2020). Multi-omics analyses identify HSD17B4 methylation-silencing as a predictive and response marker of HER2-positive breast cancer to HER2-directed therapy. Scientific Reports, 10(1), 15530.

Huang, H., Liu, R., Huang, Y., Feng, Y., Fu, Y., Chen, L., ... & Chen, Y. (2020). Acetylation-mediated degradation of HSD17B4 regulates the progression of prostate cancer. Aging (Albany NY), 12(14), 14699.

Zhang, X., Yang, H., Zhang, J., Gao, F., & Dai, L. (2020). HSD17B4, ACAA1, and PXMP4 in peroxisome pathway are down-regulated and have clinical significance in non-small cell lung cancer. Frontiers in Genetics, 11, 273.

Matsuda, Y., Morino, H., Miyamoto, R., Kurashige, T., Kume, K., Mizuno, N., ... & Kawakami, H. (2020). Biallelic mutation of HSD17B4 induces middle age–onset spinocerebellar ataxia. Neurology Genetics, 6(1).

Violante, S., Achetib, N., van Roermund, C. W., Hagen, J., Dodatko, T., Vaz, F. M., ... & Houten, S. M. (2019). Peroxisomes can oxidize medium-and long-chain fatty acids through a pathway involving ABCD3 and HSD17B4. The FASEB Journal, 33(3), 4355.

Pan, L. C., Xiao, H. Y., Yin, W. J., & Lin, Z. (2018). Correlation between HSD17B4 expression in rat liver cancer tissues and inflammation or proliferation. Eur Rev Med Pharmacol Sci, 22(11), 3386-3393.

Ko, H. K., Berk, M., Chung, Y. M., Willard, B., Bareja, R., Rubin, M., ... & Sharifi, N. (2018). Loss of an androgen-inactivating and isoform-specific HSD17B4 splice form enables emergence of castration-resistant prostate cancer. Cell reports, 22(3), 809-819.

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

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