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16815
Redox Homeostasis and Signaling Antibody Sampler Kit
Primary Antibodies
Antibody Sampler Kit

Redox Homeostasis and Signaling Antibody Sampler Kit #16815

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Redox Homeostasis and Signaling Antibody Sampler Kit: Image 1
Western blot analysis of extracts from A-431 cells, untreated or treated with EGF (50 ng/ml, 15 min), λ phosphatase (13333 Unit/ml, overnight) using Phospho-Prdx1 (Tyr194) (D1T9C) Rabbit mAb (upper) and Prdx1 (D5G12) Rabbit mAb #8499 (lower).
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 2
Western blot analysis of extracts from various cell lines using TXNIP (D5F3E) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 3
Western blot analysis of extracts from various cell lines using Thioredoxin 2 (D1C9L) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 4
Western blot analysis of extracts from various cell lines and tissues using TRXR1 (D1T3D) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 5
Western blot analysis of extracts from various cell types using Thioredoxin 1 (C63C6) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 6
Western blot analysis of extracts from 293 and THP-1 cells using GPX1 (C8C4) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 7
Western blot analysis of extracts from various cell lines using GPX4 Antibody.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 8
After the primary antibody is bound to the target protein, a complex with HRP-linked secondary antibody is formed. The LumiGLO® is added and emits light during enzyme catalyzed decomposition.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 9
Western blot analysis of extracts from HeLa and MCF7 cells using Prdx1 (D5G12) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 10
Immunoprecipitation of Phospho-Prdx1 (Tyr194) protein from A-431 cells treated with EGF (50 ng/ml, 15 min), using Rabbit (DA1E) mAb XP® Isotype control #3900 (lane 2) or Phospho-Prdx1 (Tyr194) (D1T9C) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using Phospho-Prdx1 (Tyr194) (D1T9C) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 11
Immunoprecipitation of TXNIP from RL cell extracts using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or TXNIP (D5F3E) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using TXNIP (D5F3E) Rabbit mAb. Mouse Anti-rabbit IgG (Light-Chain Specific) (L57A3) mAb #3677 was used as the secondary antibody.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 12
Western blot analysis of extracts from 293 cells, mock transfected (-) or transfected with a construct expressing Myc-tagged full-length human thioredoxin 2 protein (hTRX2-Myc; +), using Thioredoxin 2 (D1C9L) Rabbit mAb (upper), Myc-Tag (71D10) Rabbit mAb #2278 (middle), and β-Actin (D6A8) Rabbit mAb #8457 (lower).
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 13
Western blot analysis of Caco-2 cells, untreated (-) or treated (+) for 48 hr with R-sulforaphane (SFN; 10 μM) and sodium selenite (100 nM), using TRXR1 (D1T3D) Rabbit mAb (upper) and GAPDH (D16H11) XP® Rabbit mAb #5174 (lower).
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 14
Immunohistochemical analysis of paraffin-embedded human lung carcinoma using Thioredoxin 1 (C63C6) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 15
Western blot analysis of extracts from mouse testis using GPX4 Antibody.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 16
Immunohistochemical analysis of paraffin-embedded human lung carcinoma using TRXR1 (D1T3D) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 17
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Thioredoxin 1 (C63C6) Rabbit mAb in the presence of control peptide (left) or Thioredoxin Blocking Peptide #1057 (right).
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 18
Immunohistochemical analysis of paraffin-embedded human ovarian carcinoma using TRXR1 (D1T3D) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 19
Immunohistochemical analysis of paraffin-embedded Caco-2 cells, untreated (left) and R-sulforaphane (SFN) and sodium selenite-treated (right), using TRXR1 (D1T3D) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 20
Immunohistochemical analysis of paraffin-embedded human prostate carcinoma using TRXR1 (D1T3D) Rabbit mAb.
Redox Homeostasis and Signaling Antibody Sampler Kit: Image 21
Immunohistochemical analysis of paraffin-embedded human testis using TRXR1 (D1T3D) Rabbit mAb.
To Purchase # 16815T
Product # Size Price
16815T
1 Kit  (8 x 20 microliters) $ 570

Product Includes Quantity Applications Reactivity MW(kDa) Isotype
GPX1 (C8C4) Rabbit mAb 3286 20 µl
  • WB
H 22 Rabbit IgG
GPX4 Antibody 52455 20 µl
  • WB
H M Mk 20, 22 Rabbit 
Thioredoxin 1 (C63C6) Rabbit mAb 2429 20 µl
  • WB
  • IHC
H M R 12 Rabbit IgG
Thioredoxin 2 (D1C9L) Rabbit mAb 14907 20 µl
  • WB
H M R Hm Mk 13 Rabbit IgG
TRXR1 (D1T3D) Rabbit mAb 15140 20 µl
  • WB
  • IHC
H M R Hm Mk 55 Rabbit IgG
TXNIP (D5F3E) Rabbit mAb 14715 20 µl
  • WB
  • IP
H M R Mk 55 Rabbit IgG
Prdx1 (D5G12) Rabbit mAb 8499 20 µl
  • WB
H M R Mk 21 Rabbit IgG
Phospho-Prdx1 (Tyr194) (D1T9C) Rabbit mAb 14041 20 µl
  • WB
  • IP
H 21 Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
  • WB
Goat 

Product Description

The Redox Homeostasis and Signaling Antibody Sampler Kit provides an economical means of detecting select components involved in redox homeostasis and signaling. The kit contains enough primary antibodies to perform at least two western blot experiments per antibody.

Specificity / Sensitivity

Each antibody in this kit recognizes endogenous levels of its specific target protein. Prdx1 (D5G12) Rabbit mAb does not cross-react with Prdx2 protein. Phospho-Prdx1 (Tyr194) (D1T9C) Rabbit mAb recognizes endogenous levels of Prdx1 protein only when phosphorylated at Tyr194. Phospho-Prdx1 (Tyr194) (D1T9C) Rabbit mAb may cross-react with other activated receptor tyrosine kinases including EGFR.

Source / Purification

GPX4 Antibody is produced by immunizing a rabbit with a synthetic peptide corresponding to residues near the carboxy terminus of human GPX4 protein. The antibody is purified by peptide affinity chromatography. Monoclonal antibodies are produced by immunizing rabbits with synthetic peptides corresponding to residues of human GPX1 protein, residues surrounding Ala9 of human thioredoxin 1 protein, Leu100 of human thioredoxin 2 protein, Gly412 of human TRXR1 protein, Val337 of human TXNIP protein, and Arg110 of human Prdx1 protein. Phospho-Prdx1 (Tyr194) (D1T9C) Rabbit mAb is produced by immunizing a rabbit with a synthetic phosphopeptide corresponding to residues surrounding Tyr194 of human Prdx1 protein.

Background

Glutathione peroxidase 1 (GPX1) is a cytosolic selenoprotein which reduces hydrogen peroxide to water (1). GPX1 is the most abundant and ubiquitous among the five GPX isoforms identified so far (2). It is an important component in the anti-oxidative defense in cells and is associated with a variety of disease conditions, such as colon cancer (3), coronary artery disease (4), and insulin resistance (1). The selenoprotein glutathione peroxidase 4 (GPX4) is a master regulator of ferroptosis, a form of programmed cell death induced by the iron-dependent lipid peroxidation (5,6). GPX4 converts lipid hydroperoxides to non-toxic lipid alcohols, therefore preventing ferroptosis (6). Research studies show that selenium enhances GPX4 expression and inhibits ferroptotic death to protect neurons (7). In addition, some therapy-resistant cancer cells depend on GPX4 to survive. Loss of GPX4 leads to ferroptosis and thus prevents tumor relapse in mice (8). Furthermore, redox homeostasis mediated by GPX4 is essential for the activation of the cytosolic DNA-sensing cGAS-STING pathway and initiation of the subsequent innate immune response (9). Thioredoxin is a small redox protein found in many eukaryotes and prokaryotes. A pair of cysteines within a highly conserved, active site sequence can be oxidized to form a disulfide bond that is then reduced by thioredoxin reductase (10). Multiple forms of thioredoxin have been identified, including cytosolic thioredoxin 1 (TRX1) and mitochondrial thioredoxin 2 (TRX2). Thioredoxin participates in many cellular processes, including redox signaling, response to oxidative stress, and protein reduction (10). A potential role of thioredoxin in human disorders such as cancer, aging, and heart disease is currently under investigation (11). Thioredoxin can play a key role in cancer progression because it acts as a negative regulator of the proapoptotic kinase ASK1 (12). Changes in thioredoxin expression have been associated with meningococcal septic shock and acute lung injury (13,14). TRXR1 (thioredoxin reductase 1) is a selenocysteine-containing protein that is involved in redox homeostasis (15-20). Its canonical target is thioredoxin, another redox protein (15). Together, they are involved in many functions such as antioxidant regulation (17-20), cell proliferation (16,17,19), DNA replication (16,17), and transcription (17,19). TRXR1 is also capable of reducing a wide array of cellular proteins (15,17). Selenium deficiency, either by diet modification (16,20) or introduction of methylmercury (18), hinders proper expression and function of TRXR1. It is possible that this effect, which results in a higher oxidative state, is a result of the selenocysteine codon (UGA) being read as a STOP codon in the absence of adequate selenium (18). The functions of TRXR1 in cell proliferation and antioxidant defense make it a potential therapeutic target. The ubiquitously expressed thioredoxin-interacting protein (TXNIP) binds and inhibits thioredoxin to regulate cellular redox state (21-23). Research studies demonstrate that hyperglycemia induces TXNIP expression and increases cellular oxidative stress (21). In addition, these studies show that TXNIP reduces glucose uptake directly by binding the glucose transporter Glut1 to stimulate receptor internalization or indirectly by reducing Glut1 mRNA levels (23). Additional studies indicate that TXNIP plays a role in the regulation of insulin mRNA transcription (24). Microarray analyses indicate that TXNIP acts downstream of PPARγ and is a putative tumor suppressor that may control thyroid cancer cell progression (25). In addition, the TXNIP protein may be a potential therapeutic target for the treatment of type 2 diabetes and some disorders related to ER-stress (26). Prdx1 belongs to a family of non-seleno peroxidases that function as H2O2 scavengers. The transient phosphorylation of Prdx1 at Tyr194 leads to inactivation of Prdx1 (27).
  1. McClung, J.P. et al. (2004) Proc Natl Acad Sci U S A 101, 8852-7.
  2. Hamanishi, T. et al. (2004) Diabetes 53, 2455-60.
  3. Drew, J.E. et al. (2005) FEBS Lett 579, 6135-9.
  4. Winter, J.P. et al. (2003) Coron Artery Dis 14, 149-53.
  5. Wenzel, S.E. et al. (2017) Cell 171, 628-641.e26.
  6. Bersuker, K. et al. (2019) Nature 575, 688-92.
  7. Alim, I. et al. (2019) Cell 177, 1262-1279.e25.
  8. Hangauer, M.J. et al. (2017) Nature 551, 247-50.
  9. Jia, M. et al. (2020) Nat Immunol 21, 727-35.
  10. Watson, W.H. et al. (2004) Toxicol Sci 78, 3-14.
  11. Burke-Gaffney, A. et al. (2005) Trends Pharmacol Sci 26, 398-404.
  12. Saitoh, M. et al. (1998) EMBO J 17, 2596-606.
  13. Callister, M.E. et al. (2007) Intensive Care Med 33, 364-7.
  14. Callister, M.E. et al. (2006) Thorax 61, 521-7.
  15. Turanov, A.A. et al. (2010) Biochem J 430, 285-93.
  16. Gasdaska, P.Y. et al. (1995) FEBS Lett 373, 5-9.
  17. Gromer, S. et al. (2004) Med Res Rev 24, 40-89.
  18. Usuki, F. et al. (2011) J Biol Chem 286, 6641-9.
  19. Pappas, A.C. et al. (2008) Comp Biochem Physiol B Biochem Mol Biol 151, 361-72.
  20. Müller, M. et al. (2010) Genes Nutr 5, 297-307.
  21. Schulze, P.C. et al. (2004) J Biol Chem 279, 30369-74.
  22. Saxena, G. et al. (2010) J Biol Chem 285, 3997-4005.
  23. Wu, N. et al. (2013) Mol Cell 49, 1167-75.
  24. Xu, G. et al. (2013) Nat Med 19, 1141-6.
  25. Morrison, J.A. et al. (2014) Mol Cancer 13, 62.
  26. Robinson, K.A. et al. (2013) J Mol Endocrinol 50, 59-71.
  27. Woo, H.A. et al. (2010) Cell 140, 517-28.

Pathways & Proteins

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For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.