Browse our anti-SRC (SRC) Antibodies

Mouse (Murine) V-Src Sarcoma (Schmidt-Ruppin A-2) Viral Oncogene Homolog (Avian) (SRC) interaction partners

1. findings suggest that HBc promotes tumorigenesis of hepatoma cells by enhancing the expression of total Src and the active form of the kinase and subsequently activates Src/PI3K/Akt signaling pathway, revealing novel insights into the underlying mechanisms of HBV-associated hepatocarcinogenesis.

2. Src kinase activation by nitric oxide promotes resistance to anoikis in tumor cell lines.

3. RANKL and Src has an unrecognized role in osteocyte survival.

4. These interactions are required for SRC-induced activation of VAV and the subsequent engagement of a JIP1-tethered JNK signaling module.

5. Elevated retinoic acid-inducible gene 1 (RIG-I) modulated the interaction of activated proto-oncogene c-Src (Src) and STAT3 by competitive binding to STAT3.

6. Cbl, Cbl-b, and Cbl-c have a role in protecting mammary epithelial cellsfrom proteotoxic stress-induced cell death by promoting turnover of active c-Src

7. unlike c-fos-/- mice, c-src-/- mice demonstrated activated, mature osteoblasts, and parallel layers of cement lines in the superficial bone matrix, indicating the new bones were piled up to older bone.

8. TM, especially TME45, maintains vascular integrity, at least in part, via Src signaling.

9. We conclude that pp60(Src) can directly inhibit DDAH II and this is involved in the increased ADMA levels that enhance eNOS uncoupling during the development of acute lung injury (ALI).

10. Ambra1 binds to both FAK and Src in cancer cells. When FAK is present, Ambra1 is recruited to focal adhesions, promoting FAK-regulated cancer cell direction-sensing and invasion. However, when Ambra1 cannot bind to FAK, abnormally high levels of phospho-Src and phospho-FAK accumulate at focal adhesions, positively regulating adhesion and invasive migration.

11. Thus we propose that Cx43 might enhance the activation of Nrf2/ARE pathway by means of inhibiting c-Src activity to hinder the nuclear export of Nrf2, and then reduce expression of FN, ICAM-1 and TGF-b1, ultimately attenuating renal fibrosis in diabetes.

12. Osteoprotegerin may induce podosome reassembly and peripheral adhesive structure detachment by modulating phosphorylation of Pyk2 and Src and their intracellular distribution in osteoclasts.

13. BMP2 also requires Src for filamentous actin polymerization in Tgfbr3(-/-) epicardial cells.

14. v-Src prevents nuclear exclusion of YAP through a decrease in the phosphorylation of YAP at Ser127 in multinucleated cells.

15. These results revealed that vascular sprouting and permeability are both controlled through the VEGFR2-TSAd-c-Src signaling pathway in a subset of tissues, which may be useful in developing strategies to control tissue-specific pathological angiogenesis.

16. The TBK1 Y179A mutant failed to rescue type I IFN production by virally infected RAW264.7 macrophages deficient in TBK1.

17. identified both Syk and Src signaling pathways as ones that participate in Borrelia burgdorferi phagocytosis and the resulting cytokine activation.

18. results indicate that SRC likely plays a central role in regulating multiple unique signaling pathways activated by MTB infection

19. c-Src tyrosine kinase mediates high glucose-induced endothelin-1 expression

20. PTPN2 is a positive regulator of lipopolysaccharide-induced inflammatory response by enhancing the activity of Src through targeting the inhibitory phosphor-tyrosine527 of Src.

Fruit Fly (Drosophila melanogaster) V-Src Sarcoma (Schmidt-Ruppin A-2) Viral Oncogene Homolog (Avian) (SRC) interaction partners

1. Src overexpression alone activated the Jun N-terminal Kinase (JNK) signalling pathway to promote actin cytoskeletal and cell polarity defects and drive apoptosis in in a whole epithelial tissue context in the Drosophila eye, whereas, in cooperation with RasACT, JNK led to a loss of differentiation and an invasive phenotype.

2. Src64 controls actin dynamics to mediate proper ring canal formation during incomplete cytokinesis during germline cyst development in vivo

3. that Brat represses the translation of src64B, an upstream regulator of a conserved Rho-dependent pathway previously shown to promote axon retraction

4. Results show that Src42a and Src64b are required for the normal division capacity of Drosophila intestinal progenitor cells, and that these genes as well as Ack cause progenitor overproliferation in the intestine via core cell cycle activation.

5. a novel essential role for Src in intestinal stem/progenitor cell proliferation and tumourigenesis initiation in vivo.

6. Data show that the actin-Capping Protein (CP) alphabeta heterodimer, which regulates actin filament (F-actin) polymerization, limits Src-induced apoptosis or tissue overgrowth by restricting JNK activation.

7. Dumbfounded/Neph1, a key diaphragm constituent, is a target of the Src kinase Src64B. Loss of Src64B activity leads to a reduction in the number of diaphragms, and this effect is in part mediated by loss of Dumbfounded/Neph1 tyrosine phosphorylation.

8. Homodimerization of the Wnt receptor DERAILED recruits the Src family kinase SRC64B in the developing embryonic central nervous system.

9. E4orf4 has a role in inducing PP2A- and Src-dependent cell death while inhibiting classic apoptosis pathways in Drosophila melanogaster

10. Mutations in a Drosophila src gene, src64, that alter the three HRD amino acids, were identified.

11. Maternal src64 regulates microfilament contraction throughout cellularization, but that zygotic src64 makes a small, but normally nonessential, contribution during late cellularization.

12. Src64B overexpression induced the formation of specialized haemocytes (lamellocytes), but had no effect on circulating plasmatocyte concentration. Src64B overexpression induced F-actin formation and Jun kinase activation in plasmatocytes.

13. Src64 acts in a cell-autonomous fashion and is likely to interact with the previously-identified linotte/derailed receptor tyrosine kinase in mushroom body development

14. In the absence of its PH domain, Tec29 constitutively localizes to ring canals, but still requires Src64 for full activation

15. Src, Jun N-terminal kinase, and STAT pathways are inhibited by Drosophila C-terminal Src kinase, which negatively regulates organ growth and cell proliferation

16. Src64 is involved in fusome development and karyosome formation during Drosophila oogenesis.

17. Results demonstrate that regulation of Src64 by Drosophila C-terminal-Src Kinase (Csk) contributes to the packaging of germline cysts by overlying somatic follicle cells during egg chamber formation.

18. Study shows that in Drosophila epithelia in situ, levels of Src signaling determine the cellular outcome of Src activation; apoptotic cell death was triggered at high Src levels; lower levels directed antiapoptotic signals while promoting proliferation.

19. Src64B is required for tracheal development and to increase the rate of adherens junction turnover.

Human V-Src Sarcoma (Schmidt-Ruppin A-2) Viral Oncogene Homolog (Avian) (SRC) interaction partners

1. X-ray irradiation induced the aggregation of lipid rafts and the clustering of c-Met and c-Src to lipid rafts through both lipid raft-dependent and lipid raft-independent mechanisms. The lipid raft-dependent activation of c-Met and its downstream pathways played an important role in the development of radiation resistance in non-small cell lung cancer cells mediated by c-Met.

2. Mutation in c-Src phosphorylation site of either HK1 or HK2 remarkably abrogates the stimulating effects of c-Src on glycolysis, cell proliferation, migration, invasion, tumorigenesis and metastasis

3. results showed that CAV-1 could promote anchorage-independent growth and anoikis resistance in detached SGC-7901 cells, which was associated with the activation of Src-dependent epidermal growth factor receptor-integrin beta signaling as well as the phosphorylation of PI3K/Akt and MEK/ERK signaling pathways

4. This study shows that Leu33Pro polymorphism of integrin beta 3 modulates platelet Src pY418 and focal adhesion kinase pY397 phosphorylation in response to abnormally high shear stress. Whereas physiological shear stress does not affect platelet signaling, abnormally high-shear stress considerably elevates Src and FAK phosphorylation in both Pro33 and Leu33 platelets.

5. High SRC expression is associated with lung adenocarcinoma.

6. While activation in c-Src is strictly controlled by ATP-binding and phosphorylation, the authors find that activating conformational transitions are spontaneously sampled in Hsp90-dependent Src mutants.

7. High SRC expression is associated with gastric cancer cell migration.

8. Src kinase mediates UV-induced TRPV1 trafficking into cell membrane in HaCaT keratinocytes.

9. Src kinase activation by nitric oxide promotes resistance to anoikis in tumor cell lines.

10. Src and Aurora-A interact upon Golgi ribbon fragmentation; Src phosphorylates Aurora-A at tyrosine 148 and this specific phosphorylation is required for Aurora-A localization at the centrosomes.

11. Study demonstrated that c-Src contributed to hypoxic microenvironment-rendered paclitaxel resistance in human epithelial ovarian cancer cells by G2/M phase arrest deterioration, and through c-Src suppression, FV-429 was capable of reversing the resistance by blocking c-Src/Stat3/HIF-1alpha pathway.

12. Data demonstrated that the Src/Fn14/NF-kappaB axis plays a critical role in NSCLC metastasis.

13. Results suggest that Src promotes EGF-stimulated EMT and migration by upregulation of ZEB1 and ZEB2 through AKT signaling pathway in gastric cancer cells.

14. Combined targeting of AKT and SRC resulted in a synergistic efficacy against human pancreatic cancer growth and metastasis.

15. important roles for c-Src tyrosine kinase in phosphorylation and activation of SLC11A1 in macrophages

16. Our data suggest that targeting Src signaling may be an effective approach to the treatment of ALK-non-small cell lung cancer (NSCLC) with acquired resistance to ALK inhibitors.

17. Src kinase in chemo-naive human primary osteosarcoma cells is differentially activated.

18. This study demonstrates that simultaneous inhibition of c-Met and Src signaling in MD-MSCs triggers apoptosis and reveals vulnerable pathways that could be exploited to develop NF2 therapies.

19. Syntenin mediates SRC function in exosomal cell-to-cell communication.

20. Endothelial cell-derived matrix promotes the metabolic functional maturation of hepatocyte via integrin-Src signaling.

Cow (Bovine) V-Src Sarcoma (Schmidt-Ruppin A-2) Viral Oncogene Homolog (Avian) (SRC) interaction partners

1. RhoA and membrane fluidity mediates the spatially polarized Src/FAK activation in response to shear stress.

2. AngII activates PKD via a mechanism involving Src family kinases and PKC, to underlie increased aldosterone production.

3. The Src gene possibly contributed to conducting association analysis and can be recognized as genetic marker in milk production traits and other performance for animal breeding and genetics.

4. src has a role in activation of 5'-AMP-activated kinase during hypoxia-reoxygenation of bovine aortic endothelial cells

5. results indicate that integrin engagement disrupts VE-cadherin-containing adherens junctions via the activation of Src, but not Ras, possibly as a result of modulation of the actin network

6. These results suggest that TGF-beta1-induced monolayer permeability involves focal adhesion and cytoskeletal rearrangement through both FAK/Src-dependent and -independent pathways.

Pig (Porcine) V-Src Sarcoma (Schmidt-Ruppin A-2) Viral Oncogene Homolog (Avian) (SRC) interaction partners

1. The findings are consistent with previous studies that indicate a link between Na,K-ATPase activity and SFK signaling.

2. Src kinase mediates hypoxia-induced caspase-1 activation in the cerebral cortex of newborn piglets

3. Expression of mutant alpha1 Na/K-ATPase defective in conformational transition attenuates Src-mediated signal transduction

4. 20-HETE activates the Raf/MEK/ERK pathway in renal epithelial cells through an EGFR- and c-Src-dependent mechanism.