GLRX3 Antibody - #DF13041
製品説明
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
引用形式: Affinity Biosciences Cat# DF13041, RRID:AB_2846002.
折りたたみ／展開
glrx3; GLRX3_HUMAN; GLRX4; Glutaredoxin 3; Glutaredoxin 4; Glutaredoxin-3; GRX3; GRX4; PICOT; PKC interacting cousin of thioredoxin; PKC theta interacting protein; PKC-interacting cousin of thioredoxin; PKC-theta-interacting protein; PKCq interacting protein; PKCq-interacting protein; Thioredoxin like protein 2; Thioredoxin-like protein 2; TXNL2; TXNL3;
免疫原
Expressed in heart, spleen, testis and, to a lower extent, in thymus and peripheral blood leukocytes. Weakly expressed in lung, placenta, colon and small intestine.
- O76003 GLRX3_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MAAGAAEAAVAAVEEVGSAGQFEELLRLKAKSLLVVHFWAPWAPQCAQMNEVMAELAKELPQVSFVKLEAEGVPEVSEKYEISSVPTFLFFKNSQKIDRLDGAHAPELTKKVQRHASSGSFLPSANEHLKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKAYSSWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIVKELKENGELLPILRGEN
種類予測
Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.
High(score>80) Medium(80>score>50) Low(score<50) No confidence
PTMs - O76003 基板として
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| A2 | Acetylation | Uniprot | |
| S32 | Phosphorylation | Uniprot | |
| K67 | Sumoylation | Uniprot | |
| K67 | Ubiquitination | Uniprot | |
| K79 | Ubiquitination | Uniprot | |
| K92 | Ubiquitination | Uniprot | |
| K96 | Ubiquitination | Uniprot | |
| T109 | Phosphorylation | Uniprot | |
| K110 | Acetylation | Uniprot | |
| K110 | Ubiquitination | Uniprot | |
| S117 | Phosphorylation | Uniprot | |
| S118 | Phosphorylation | Uniprot | |
| S120 | Phosphorylation | Uniprot | |
| S124 | Phosphorylation | Uniprot | |
| K130 | Ubiquitination | Uniprot | |
| K139 | Ubiquitination | Uniprot | |
| C146 | S-Nitrosylation | Uniprot | |
| K151 | Ubiquitination | Uniprot | |
| T153 | Phosphorylation | Uniprot | |
| K163 | Ubiquitination | Uniprot | |
| S183 | Phosphorylation | Uniprot | |
| S196 | Phosphorylation | Uniprot | |
| Y200 | Phosphorylation | Uniprot | |
| K231 | Ubiquitination | Uniprot | |
| K234 | Ubiquitination | Uniprot | |
| K240 | Ubiquitination | Uniprot | |
| T301 | Phosphorylation | Uniprot | |
| K319 | Ubiquitination | Uniprot | |
| K322 | Ubiquitination | Uniprot |
研究背景
Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Required for hemoglobin maturation. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity.
Cytoplasm>Cytosol. Cytoplasm>Cell cortex. Cytoplasm>Myofibril>Sarcomere>Z line.
Note: Under the plasma membrane (By similarity). After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area (By similarity). In the Z line, found associated with CSRP3 (By similarity).
Expressed in heart, spleen, testis and, to a lower extent, in thymus and peripheral blood leukocytes. Weakly expressed in lung, placenta, colon and small intestine.
Homodimer; the homodimer is independent of 2Fe-2S clusters. Heterotrimer; forms a heterotrimeric complex composed by two BOLA2 molecules and one GLRX3 molecule; linked by [2Fe-2S] clusters. Interacts (via N-terminus) with PRKCQ/PKC-theta. Interacts (via C-terminus) with CSRP3 (By similarity). Interacts with CSRP2 (By similarity).
The thioredoxin domain lacks the two redox-active cysteines. This strongly suggests that it lacks thioredoxin activity.
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