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Mouse Anti-GSTP1 Recombinant Antibody (CBFYH-0523) (CBMAB-H1401-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-0523
Antibody Isotype
IgG1
Application
ELISA, IHC-Fr, IHC-P, WB

Basic Information

Immunogen
Recombinant human GSTP1
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 7.4
Preservative
0.03% 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
Glutathione S-Transferase Pi 1
Introduction
Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into 4 main classes: alpha, mu, pi, and theta. This GST family member is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.
Entrez Gene ID
2950
UniProt ID
P09211
Alternative Names
Glutathione S-Transferase Pi 1; GST Class-Pi; EC 2.5.1.18; GSTP1-1; FAEES3; GST3; Fatty Acid Ethyl Ester Synthase III; Epididymis Secretory Protein Li 22
Function
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911).

Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276).

Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.
Biological Process
Cellular response to lipopolysaccharide Source: BHF-UCL
Central nervous system development Source: ProtInc
Common myeloid progenitor cell proliferation Source: BHF-UCL
Glutathione derivative biosynthetic process Source: UniProtKB
Glutathione metabolic process Source: UniProtKB
Hepoxilin biosynthetic process Source: UniProtKB
Linoleic acid metabolic process Source: BHF-UCL
Negative regulation of acute inflammatory response Source: BHF-UCL
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of biosynthetic process Source: BHF-UCL
Negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
Negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
Negative regulation of fibroblast proliferation Source: BHF-UCL
Negative regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
Negative regulation of interleukin-1 beta production Source: BHF-UCL
Negative regulation of JUN kinase activity Source: BHF-UCL
Negative regulation of leukocyte proliferation Source: BHF-UCL
Negative regulation of MAPK cascade Source: BHF-UCL
Negative regulation of MAP kinase activity Source: BHF-UCL
Negative regulation of monocyte chemotactic protein-1 production Source: BHF-UCL
Negative regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
Negative regulation of protein kinase activity Source: BHF-UCL
Negative regulation of stress-activated MAPK cascade Source: BHF-UCL
Negative regulation of tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
Negative regulation of tumor necrosis factor production Source: BHF-UCL
Nitric oxide storage Source: BHF-UCL
Positive regulation of superoxide anion generation Source: BHF-UCL
Prostaglandin metabolic process Source: UniProtKB
Regulation of ERK1 and ERK2 cascade Source: BHF-UCL
Regulation of stress-activated MAPK cascade Source: BHF-UCL
Response to reactive oxygen species Source: BHF-UCL
Xenobiotic metabolic process Source: UniProtKB
Cellular Location
Cytoplasm; Nucleus; Mitochondrion. The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.
More Infomation

Lei, X., Du, L., Yu, W., Wang, Y., Ma, N., & Qu, B. (2021). GSTP1 as a novel target in radiation induced lung injury. Journal of Translational Medicine, 19, 1-5.

Feng, Q., Li, X., Sun, W., Sun, M., Li, Z., Sheng, H., ... & Shan, C. (2020). Targeting G6PD reverses paclitaxel resistance in ovarian cancer by suppressing GSTP1. Biochemical Pharmacology, 178, 114092.

Cui, J., Li, G., Yin, J., Li, L., Tan, Y., Wei, H., ... & Yi, L. (2020). GSTP1 and cancer: Expression, methylation, polymorphisms and signaling. International Journal of Oncology, 56(4), 867-878.

Santric, V., Djokic, M., Suvakov, S., Pljesa-Ercegovac, M., Nikitovic, M., Radic, T., ... & Savic-Radojevic, A. (2020). GSTP1 rs1138272 polymorphism affects prostate cancer risk. Medicina, 56(3), 128.

Lei, K., Gu, X., Alvarado, A. G., Du, Y., Luo, S., Ahn, E. H., ... & Ye, K. (2020). Discovery of a dual inhibitor of NQO1 and GSTP1 for treating glioblastoma. Journal of hematology & oncology, 13, 1-21.

Farmohammadi, A., Arab-Yarmohammadi, V., & Ramzanpour, R. (2020). Association analysis of rs1695 and rs1138272 variations in GSTP1 gene and breast cancer susceptibility. Asian Pacific Journal of Cancer Prevention: APJCP, 21(4), 1167.

Du, Y., Zhang, H., Xu, Y., Ding, Y., Chen, X., Mei, Z., ... & Jie, Z. (2019). Association among genetic polymorphisms of GSTP1, HO-1, and SOD-3 and chronic obstructive pulmonary disease susceptibility. International Journal of Chronic Obstructive Pulmonary Disease, 2081-2088.

Gurioli, G., Martignano, F., Salvi, S., Costantini, M., Gunelli, R., & Casadio, V. (2018). GSTP1 methylation in cancer: a liquid biopsy biomarker?. Clinical Chemistry and Laboratory Medicine (CCLM), 56(5), 702-717.

Checa-Rojas, A., Delgadillo-Silva, L. F., del Castillo Velasco-Herrera, M., Andrade-Domínguez, A., Gil, J., Santillán, O., ... & Encarnación-Guevara, S. (2018). GSTM3 and GSTP1: novel players driving tumor progression in cervical cancer. Oncotarget, 9(31), 21696.

Lin, C., Xie, L., Lu, Y., Hu, Z., & Chang, J. (2018). miR-133b reverses cisplatin resistance by targeting GSTP1 in cisplatin-resistant lung cancer cells. International Journal of Molecular Medicine, 41(4), 2050-2058.

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

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