Recombinant Human RhoA Protein

Beta LifeScience SKU/CAT #: BLA-7789P

Recombinant Human RhoA Protein

Beta LifeScience SKU/CAT #: BLA-7789P
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Product Overview

Host Species Human
Accession P61586
Synonym Aplysia ras related homolog 12 ARH12 ARHA H 12 H12 Oncogene RHO H12 Ras homolog family member A Ras homolog gene family member A Rho A Rho cDNA clone 12 RHO H12 RHO12 RHOA RHOA_HUMAN RHOH12 Small GTP binding protein Rho A Transforming protein Rho A Transforming protein RhoA
Description Recombinant Human RhoA Protein was expressed in E.coli. It is a Full length protein
Source E.coli
AA Sequence MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDG KQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWT PEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANR IGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGC
Purity >85% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity The specific activity of RhoA was 10.9 nmol/min/mg in GPTase-Glo assay.
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis. Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center. May be an activator of PLCE1. In neurons, involved in the inhibiton of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling. Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets.; (Microbial infection) Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague.
Subcellular Location Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex. Midbody. Cell projection, lamellipodium. Cell projection, dendrite.
Protein Families Small GTPase superfamily, Rho family
Database References

Gene Functions References

  1. The results suggest that human parainfluenza virus type 2 (hPIV-2) V protein enhances hPIV2 growth through RhoA-induced F-actin formation, by selectively binding to inactive RhoA. PMID: 30165310
  2. This article summarizes recent progress on the mechanisms that control the expression of the three members of the Rho-like subfamily (RhoA, RhoB, and RhoC) at the level of gene transcription as well as their post-transcriptional regulation by microRNAs. [review] PMID: 29500478
  3. Overexpression of miR133b inhibited the proliferation and promoted apoptosis in a diabetic retinopathy cell model by downregulating RhoA expression. PMID: 29786744
  4. silencing of URG11 altered the expression levels of cell cycleassociated genes, epithelialmesenchymal transitionassociated genes, and RhoA and ROCK1 protein levels. Thus, the results of the present study suggest that URG11 may be a potential therapeutic target, which may be important to inhibit the development and progression of prostatic hyperplasia. PMID: 29749520
  5. Results suggested that the RhoA/ROCK1 pathway activated by excessive ROS is responsible for profilin-1-mediated endothelial damage. PMID: 29849894
  6. We found that lipid radicals govern changes in podocyte homeostasis through redox sensitive RhoA signaling: lipid radicals inhibit migration and cause loss of F-actin fibers. These effects were prevented by mutating the redox sensitive cysteines of RhoA. PMID: 29547847
  7. Data show that p120-catenin interacts with kinesin family member 23 (MKLP1) to regulate focused rhoA GTP-binding protein (RhoA) activity during cytokinesis. PMID: 28004812
  8. Data show that RhoA is upregulated in invasive glioblastoma tissues, and its activation participates in Wnt5a-induced glioblastoma cell invasion. PMID: 29207169
  9. PCGEM1 may be an inducer in epithelial ovarian cancer tumorigenesis and progression by upregulating RhoA and the subsequent expression of YAP, P70S6K, MMP2, and Bcl-xL. PMID: 29949791
  10. This study identified Piezo2 mechanosensitive cationic channel as a transducer of environmental physical cues into mechanobiological responses. PMID: 29432180
  11. High RHOA expression is associated with gastric cancer invasion and metastasis. PMID: 28656284
  12. Results show that RHOA expression level is under the regulation of NORAD to promote EMT in pancreatic neoplasm. PMID: 29121972
  13. Data show that phosphorylation of ribosomal protein S6 kinase 2 (RSK2) at threonine 577 is essential for leukemia-associated RhoGEF (LARG)-dependent Rho GTPase activation. PMID: 29279389
  14. RhoA activated the downstream Wnt/betacatenin signaling pathway and inhibited the expression of apoptotic factors. PMID: 28990085
  15. We identify HGF, acting through the c-Met receptor, as the key polarity-inducing morphogen, which acts to activate b1-integrin-dependent adhesion. HGF and ECM-derived integrin signals co-operate via a c-Src-dependent inhibition of the RhoA-ROCK1 signalling pathway via p190A RhoGAP PMID: 28888686
  16. Extracellular Hsp90alpha mediates house dust mite-induced human bronchial epithelial barrier dysfunction by activating RhoA/MLC signaling, suggesting that eHsp90alpha is a potential therapeutic target for treatment of asthma. PMID: 28558721
  17. This analysis showed a relative increase in the expression of E2F6 in gastric adenocarcinoma with no lymph node metastasis (chi (2), P = 0.04 and OR, P = 0.08), while overexpression of RhoA and SMUG1 was found more often in the diffuse subtype of gastric adenocarcinoma as compared to the intestinal subtype. PMID: 27909884
  18. This is the first study to verify the relationship of the expression of RhoA and Ezrin proteins in vaginal tissue of Postmenopausal atrophic vagina. PMID: 28843271
  19. blockage of RhoA/ROCK repressed the TAK1/NOD2-mediated NF-kappaB pathway in HaCaT cells exposed to UVB. PMID: 28608226
  20. data suggest that TGF-beta stimulated the expression of ChPF and sGAG synthesis in nucleus pulposus cells through Smad3, RhoA/ROCK1 and the three MAPK signaling pathways. PMID: 28608941
  21. a SDF-1/CXCR4-RhoA and RhoC-ROS-cytoskeleton pathway that regulates Jurkat cell migration in response to SDF-1. PMID: 28536953
  22. DIAPH3 overexpression inhibits the migration and invasion of Triple-negative breast cancer by inhibiting RhoA-GTP expression. PMID: 28779705
  23. Tyr42 phosphorylation of RhoA GTPase promotes tumorigenesis through NF-kappaB. PMID: 28712859
  24. NO-induced cGMP signaling modulated RhoA/ROCK signaling in platelets, leading to the disinhibition of MLCP to control the phosphorylation of MLC and remodeling of platelet actin cytoskeleton. PMID: 28509344
  25. Results provide evidence that RhoA is activated by CCNA2 during mitosis. PMID: 27279564
  26. RhoA and COX-2 were upregulated in early gastric cancer tissues, which facilitated the proliferation and migration of gastric cancer cells. PMID: 28624843
  27. Molecular modelling studies of PAK1 with its major interacting partners RHOA and STAT3 revealed potential network gene elements in breast invasive carcinoma. PMID: 27456030
  28. The results identify a significant genotypic association between Primary open-angle glaucoma (POAG) and RHOA gene rs974495 polymorphism. PMID: 27195967
  29. Our findings indicate that NRF2 silencing-mediated reduction of RhoA expression contributes, at least in part, to the poor outcome of breast cancer patients with high NRF2 expression. PMID: 27713154
  30. RHOA, and its oncogenic signaling pathway, represent a strong biomarker-driven therapeutic target for Asian gastric cancer. PMID: 27806312
  31. this study shows that C5a receptor (CD88) promotes motility and invasiveness of gastric cancer by activating RhoA PMID: 27756879
  32. CD44 and RHOA are required for CFL1 phosphorylation and cell migration induced by CD74 in breast cancer cells. PMID: 27626171
  33. Out of multiple members of this family, RhoA and RhoC are important factors. RhoA is supposed to increase tumor proliferation when overexpressed while RhoC is responsible for tumor initiation. PMID: 28508825
  34. These results indicate that aberrant alternative splicing of RHOA results in the loss of its activity and expression in DGC cells. PMID: 29247652
  35. Spatiotemporal analysis of RhoA/RhoB/RhoC activation in primary human endothelial cells has been uncovered. PMID: 27147504
  36. MDA-9 upregulated active levels of known modulators of epithelial mesenchymal transformation, the small GTPases RhoA and Cdc42, via TGFbeta1, promoting lung metastasis of breast cancer cells. PMID: 27863394
  37. Results indicate that miR-126 acts as a tumor suppressor by inactivating RhoA signaling via CXCR4 in colon cancer. PMID: 27517626
  38. RhoA expression patterns in circulating leucocytes is a biomarker for the breast cancer risk assessment. PMID: 27812894
  39. DOCK7 controls neuronal growth via a Rac-dependent pathway, likely by modulating microtubule networks while also regulating F-actin remodeling at the cell rear to promote somal translocation via a previously unrecognized myosin phosphatase-RhoA-interacting protein-dependent pathway. PMID: 29089377
  40. The ability of enhanced GNA13 signaling to suppress KLK gene expression appears at least in part due to the ability of enhanced GNA13 signaling to negatively impact Rho/ROCK-signaling. PMID: 27424208
  41. OB-Rb, RhoA/ROCK, PI3K/AKT, JAK/STAT pathways and NF-kB activation are involved in leptin-induced upA expression. PMID: 28104444
  42. study strongly supported the contribution of the genes ITGA2B, GSN and RHOA and the two pathways "regulation of actin cytoskeleton" and "leukocyte transendothelial migration" to osteoporosis risk. PMID: 27153759
  43. Suggest RHOA mutations useful for diagnosing cutaneous localizations of angioimmunoblastic T-cell lymphomas. PMID: 28945625
  44. TET2 and RhoA mutations cooperatively disrupt T cell homeostasis PMID: 28691928
  45. Genetic variant in RhoA gene is associated with progression of prostate cancer. PMID: 28184030
  46. Downregulation of Cul3 led to a marked increase in RhoA protein expression after 6 days of adipocytes differentiation, suggesting that Cul3 is involved in the regulation of RhoA stability. PMID: 28499918
  47. High RHOA expression is associated with colon cancer cell migration. PMID: 28146427
  48. P311 could accelerate skin wound reepithelialization by promoting the migration of Epidermal Stem Cell through RhoA and Rac1 activation. PMID: 27927130
  49. Findings indicate a tumor suppressive role for G protein subunit alpha 13 (Galpha13) and rhoA GTP-binding protein (RhoA) in Burkitt's lymphoma and diffuse large B-cell lymphoma (DLBCL). PMID: 26616858
  50. RhoA/ROCK and Raf-1/CK2 pathway are responsible for TNF-alpha-mediated endothelial cytotoxicity via regulation of the vimentin cytoskeleton. PMID: 28743511

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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