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Rabbit Anti-ELOVL2 Recombinant Antibody (EG1095) (CBMAB-EN1291-LY)


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Summary

Host Animal
Rabbit
Specificity
Human
Clone
EG1095
Antibody Isotype
IgG
Application
IHC: 1:50~1:100 ELISA: 1:10000

Basic Information

Immunogen
The antibody was produced against synthesized peptide derived from internal of human ELOVL2.
Specificity
Human
Antibody Isotype
IgG
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
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
ELOVL Fatty Acid Elongase 2
Introduction
ELOVL2 (ELOVL Fatty Acid Elongase 2) is a Protein Coding gene. Diseases associated with ELOVL2 include Melanoma, Cutaneous Malignant 1. Among its related pathways are Fatty Acyl-CoA Biosynthesis and Ectoderm Differentiation. Gene Ontology (GO) annotations related to this gene include transferase activity, transferring acyl groups other than amino-acyl groups and fatty acid elongase activity. An important paralog of this gene is ELOVL5.
Entrez Gene ID
54898
UniProt ID
Q9NXB9
Alternative Names
ELOVL Fatty Acid Elongase 2; Elongation Of Very Long Chain Fatty Acids (FEN1/Elo2, SUR4/Elo3, Yeast)-Like 2; Very Long Chain 3-Ketoacyl-CoA Synthase 2; Very Long Chain 3-Oxoacyl-CoA Synthase 2; 3-Keto Acyl-CoA Synthase ELOVL2; ELOVL FA Elongase 2; SSC2; Elongation Of Very Long Chain Fatty Acids Protein 2; EC 2.3.1.199;
Research Area
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA), acting specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Biological Process
Alpha-linolenic acid metabolic process Source: Reactome
Fatty acid elongation, monounsaturated fatty acid Source: GO_Central
Fatty acid elongation, polyunsaturated fatty acid Source: UniProtKB
Fatty acid elongation, saturated fatty acid Source: GO_Central
Linoleic acid metabolic process Source: Reactome
Long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
Sphingolipid biosynthetic process Source: GO_Central
Unsaturated fatty acid biosynthetic process Source: UniProtKB-UniPathway
Very long-chain fatty acid biosynthetic process Source: UniProtKB
Cellular Location
Endoplasmic reticulum membrane
More Infomation

Tanaka, K., Kandori, S., Sakka, S., Nitta, S., Tanuma, K., Shiga, M., ... & Nishiyama, H. (2022). ELOVL2 promotes cancer progression by inhibiting cell apoptosis in renal cell carcinoma. Oncology reports, 47(2), 1-11.

Jeong, D., Ham, J., Kim, H. W., Kim, H., Ji, H. W., Yun, S. H., ... & Kim, S. J. (2021). ELOVL2: a novel tumor suppressor attenuating tamoxifen resistance in breast cancer. American Journal of Cancer Research, 11(6), 2568.

Osada, H., Toda, E., Homma, K., Guzman, N. A., Nagai, N., Ogawa, M., ... & Ozawa, Y. (2021). ADIPOR1 deficiency-induced suppression of retinal ELOVL2 and docosahexaenoic acid levels during photoreceptor degeneration and visual loss. Cell death & disease, 12(5), 1-13.

Maguolo, A., Zusi, C., Giontella, A., Miraglia Del Giudice, E., Tagetti, A., Fava, C., ... & Maffeis, C. (2021). Influence of genetic variants in FADS2 and ELOVL2 genes on BMI and PUFAs homeostasis in children and adolescents with obesity. International Journal of Obesity, 45(1), 56-65.

Sun, S., Ren, T., Li, X., Cao, X., & Gao, J. (2020). Polyunsaturated fatty acids synthesized by freshwater fish: A new insight to the roles of elovl2 and elovl5 in vivo. Biochemical and Biophysical Research Communications, 532(3), 414-419.

Chen, D., Chao, D. L., Rocha, L., Kolar, M., Nguyen Huu, V. A., Krawczyk, M., ... & Skowronska‐Krawczyk, D. (2020). The lipid elongation enzyme ELOVL2 is a molecular regulator of aging in the retina. Aging cell, 19(2), e13100.

Jung, S. E., Lim, S. M., Hong, S. R., Lee, E. H., Shin, K. J., & Lee, H. Y. (2019). DNA methylation of the ELOVL2, FHL2, KLF14, C1orf132/MIR29B2C, and TRIM59 genes for age prediction from blood, saliva, and buccal swab samples. Forensic Science International: Genetics, 38, 1-8.

Datsomor, A. K., Zic, N., Li, K., Olsen, R. E., Jin, Y., Vik, J. O., ... & Winge, P. (2019). CRISPR/Cas9-mediated ablation of elovl2 in Atlantic salmon (Salmo salar L.) inhibits elongation of polyunsaturated fatty acids and induces Srebp-1 and target genes. Scientific reports, 9(1), 1-13.

Slieker, R. C., Relton, C. L., Gaunt, T. R., Slagboom, P. E., & Heijmans, B. T. (2018). Age-related DNA methylation changes are tissue-specific with ELOVL2 promoter methylation as exception. Epigenetics & chromatin, 11(1), 1-11.

Bellini, L., Campana, M., Rouch, C., Chacinska, M., Bugliani, M., Meneyrol, K., ... & Le Stunff, H. (2018). Protective role of the ELOVL2/docosahexaenoic acid axis in glucolipotoxicity-induced apoptosis in rodent beta cells and human islets. Diabetologia, 61(8), 1780-1793.

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

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