Recombinant Human Rho-Related Gtp-Binding Protein Rhod (RHOD) Protein (His&Myc)

Name: Recombinant Human Rho-Related Gtp-Binding Protein Rhod (RHOD) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01849P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Rho-Related Gtp-Binding Protein Rhod (RHOD) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O00212
Target Symbol	RHOD
Synonyms	Rho-related protein HP1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MTAAQAAGEEAPPGVRSVKVVLVGDGGCGKTSLLMVFADGAFPESYTPTVFERYMVNLQVKGKPVHLHIWDTAGQDDYDRLRPLFYPDASVLLLCFDVTSPNSFDNIFNRWYPEVNHFCKKVPIIVVGCKTDLCKDKSLVNKLRRNGLEPVTYHRGQEMARSVGAVAYLECSARLHDNVHAVFQEAAEVALSSRGRNFWRRITQGFC
Expression Range	1-207aa
Protein Length	Full Length of Mature Protein
Mol. Weight	30.6 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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

FAQs

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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.