Recombinant Human RhoD Protein

Name: Recombinant Human RhoD Protein
Brand: Beta LifeScience
SKU: BL-0173SG
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	BC001338
Synonym	Rho; RHOHP1; RHOM
Background	RhoD is a member of the Rho gene family that interacts with protein kinases and serves as a target of activated GTPase. Rho binds GTP and plays a critical role in muscle differentiation by regulating the expression of myogenin and MEF2 genes. Furthermore, Rho is involved in endosome dynamics and reorganization of the actin cytoskeleton and plays a role in coordinating membrane transport (1). mDia and ROCK are downstream effectors of Rho mediating Rho action on the actin cytoskeleton; mDia produces actin filaments by nucleation and polymerization and ROCK activate myosin to cross-link them for induction of actomyosin bundles and contractility (2).
Description	Recombinant human RhoD (1-207) was produced in E. coli, fused with a His tag at N-terminus.
Source	E.coli
AA Sequence	1-207a.a.
Molecular Weight	~23 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human RhoD Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Involved in endosome dynamics. May coordinate membrane transport with the function of the cytoskeleton. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Participates in the reorganization of actin cytoskeleton; the function seems to involve WHAMM and includes regulation of filopodia formation and actin filament bundling. Can modulate the effect of DAPK3 in reorganization of actin cytoskeleton and focal adhesion dissolution.
Subcellular Location	Cell membrane; Lipid-anchor; Cytoplasmic side. Early endosome.
Protein Families	Small GTPase superfamily, Rho family
Database References	HGNC: 670 OMIM: 605781 KEGG: hsa:29984 STRING: 9606.ENSP00000308576 UniGene: Hs.15114
Tissue Specificity	Heart, placenta, liver, skeletal muscle, and pancreas and, with weaker intensity, in several other tissues.

Gene Functions References

The GTPase deficient atypical Rho GTPases, which have a stalled GTPase activity, RhoD has an elevated intrinsic GDP/GTP exchange activity, rendering the protein constitutively active. PMID: 29776664
RhoD recruits Pak6 to the plasma membrane to antagonize RhoC signaling during cell contraction and blebbing PMID: 28486133
RhoD silencing leads to increased actin filament-containing structures and disruption of cell migration and proliferation. PMID: 28196728
A novel signaling pathway involving RhoD and its binding partner WHAMM, regulate Golgi dynamics. PMID: 25746724
Activated p42/44-MAP kinase, Rho GTPase. PMID: 24706358
Fetal RHD detection in early pregnancy using a single-exon assay in a routine clinical setting is feasible and accurate after its implementation in an unselected pregnant population. PMID: 22776962
It regulates relaxation of vascular smooth muscle. PMID: 24717605
Data from differentiating cultured erythroid precursor cells suggest that RhAG (Rh-associated glycoprotein) knockdown abolishes Rh blood group expression (RhoD; ICAM4 [intercellular adhesion molecule 4]; CD47 Rh-related antigen) in erythroid cells. PMID: 23417980
RhoD interacts with ZIPK in a GTP-dependent manner and modulates stress fiber and focal adhesion reorganization. PMID: 23454120
A GTPase-deficient mutant of RhoD, RhoDG26V, causes hyperplasia and perturbed differentiation of the epidermis. PMID: 22665057
Overexpression of RhoD is associated with multiple myeloma. PMID: 20528248
The expression of RhoA/Rho kinase mRNA and protein and function in the RA were significantly stronger than in the IMA, suggesting that RhoA/Rho kinase pathway may be one mechanism by which RA is more susceptible to spasm than IMA. PMID: 19682162
These results suggest a critical role for the CS amplitude and the balance between Rac and Rho in mechanochemical regulation of lung EC barrier. PMID: 16651639
Methylophiopogonanone B appears to induce Rho activation, resulting in actin cytoskeletal reorganization, including dendrite retraction and stress fiber formation. PMID: 17029007
The data suggest that Rho-kinase dependent cell contractility contributes to global and local matrix remodeling, whereas Rho dependent activation of mDia and/or other downstream effectors regulates the structure and number of cell processes. PMID: 17342762
the the increased expression of p120 isoform 1 during tumor progression contributes to the invasive phenotype of cadherin-deficient carcinomas and that the N-terminal domain of p120 is a valid therapeutic target PMID: 18407999
strongly activated in HTLV-1 infected T cell lines derived from HAM/TSP patients. PMID: 18552504
A previously unknown function of Brk in regulating both RhoA and Ras by phosphorylating p190 and a crucial role of this Brk-elicited signaling pathway in promoting breast malignancy. PMID: 18829532
Rho mediates various phenotypes of malignant transformation by Ras and Src through its effectors, ROCK and mDia [review] PMID: 19160018
Data suggest that mammalian cells have two potential steps that require active Rho for the stabilization of midzone microtubules during mitosis and cytokinesis. PMID: 19576212
estrogen receptor-alpha transcriptional activity is repressed by the Rho/megakaryoblastic leukemia 1 signaling pathway PMID: 19826002

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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.

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