Recombinant Human Guanine Nucleotide-Binding Protein Subunit Alpha-13 (GNA13) Protein (His)

Name: Recombinant Human Guanine Nucleotide-Binding Protein Subunit Alpha-13 (GNA13) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08878P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Guanine Nucleotide-Binding Protein Subunit Alpha-13 (GNA13) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q14344
Target Symbol	GNA13
Synonyms	G alpha 13; G alpha-13; G-protein subunit alpha-13; GNA13; GNA13_HUMAN; Guanine nucleotide binding protein (G protein) alpha 13; Guanine nucleotide binding protein alpha 13 subunit; Guanine nucleotide-binding protein subunit alpha-13
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MADFLPSRSVLSVCFPGCLLTSGEAEQQRKSKEIDKCLSREKTYVKRLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKGMRVLVDAREKLHIPWGDNSNQQHGDKMMSFDTRAPMAAQGMVETRVFLQYLPAIRALWADSGIQNAYDRRREFQLGESVKYFLDNLDKLGEPDYIPSQQDILLARRPTKGIHEYDFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEFDQVLMEDRLTNRLTESLNIFETIVNNRVFSNVSIILFLNKTDLLEEKVQIVSIKDYFLEFEGDPHCLRDVQKFLVECFRNKRRDQQQKPLYHHFTTAINTENIRLVFRDVKDTILHDNLKQLMLQ
Expression Range	1-377aa
Protein Length	Full Length
Mol. Weight	48.0 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	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG). GNA13-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway. Inhibits CDH1-mediated cell adhesion in process independent from Rho activation.
Subcellular Location	Cell membrane; Lipid-anchor. Melanosome. Cytoplasm. Nucleus.
Protein Families	G-alpha family, G(12) subfamily
Database References	HGNC: 4381 OMIM: 604406 KEGG: hsa:10672 STRING: 9606.ENSP00000400717 UniGene: PMID: 27883022 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 the selective expression of FZD10 in brain vascular endothelial cells points at a potential role of FZD10-Galpha13 signalling in central nervous system angiogenesis. PMID: 28126591 The protein profile indicates attenuation of "GNA13-ERK signaling" in schizophrenia brain. In particular, EIF4G2 and CYFIP1, which are located downstream of the GNA13-ERK network, were decreased, suggesting that the attenuation of this signal network may cause impairment of axon formation and synapse plasticity in the brain of schizophrenia patients. PMID: 28214564 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 Data (including data from studies using transgenic mice) suggest that R7BP-RGS7 heterotrimers interact with Galpha13 to augment signaling pathways in neurons that regulate neurite morphogenesis. (R7BP = RGS7 family binding protein; RGS7 = regulator of G-protein signaling 7 protein; Galpha13 = GTP-binding protein alpha subunit 13) PMID: 28432124 Upregulation of GNA13 expression increased the proliferation and tumorigenicity of gastric cancer. PMID: 26735177 Knockdown DDR1 reversed the effects of Galpha13 knockdown on cell-cell adhesion and proteolytic invasion in three-dimensional collagen. PMID: 26589794 RGS22 acts as a tumor suppressor, repressing human pancreatic adenocarcinoma cell migration by coupling to GNA12/13. PMID: 26323264 Galpha13 Switch Region 2 Binds to the Talin Head Domain and Activates alphaIIbbeta3 Integrin in Human Platelets PMID: 26292217 GNA13 expression in breast cancer cells is regulated by post-transcriptional mechanisms involving miR-31. PMID: 25889182 Data show that N-linked glycosylation of protease-activated receptor-1 (PAR1) at extracellular loop 2 (ECL2) controls G12/13 versus Gq G-proteins coupling specificity in response to thrombin stimulation. PMID: 26100877 Our findings highlight the important role of miR-29c in regulating CRC EMT via GSK-3b/b-catenin signaling by targeting GNA13 and PTP4A and provide new insights into the metastatic basis of colorectal cancer PMID: 25193986 These results place Blk upstream of the p190RhoGAP-RhoA pathway in Galpha13-activated cells, overall representing an opposing signaling module during CXCL12-triggered invasion. PMID: 25025568 findings identify a Galpha13-dependent pathway that exerts dual actions in suppressing growth and blocking dissemination of germinal centre B cells that is frequently disrupted in germinal centre B-cell-derived lymphoma PMID: 25274307 Findings indicate lysophosphatidic acid (LPA)-lysophosphatidic acid receptor-Galpha13 signaling node as a therapeutic target for pancreatic cancer treatment and control. PMID: 23508014 Mutation in the Galpha13 gene is associated with diffuse large B-cell lymphoma. PMID: 23699601 Itk enhances Galpha13 mediated activation of serum response factor (SRF) transcriptional activity dependent on its ability to interact with Galpha13, but its kinase activity is not required to enhance SRF activity. PMID: 23454662 GNA13 is an important mediator of prostate cancer cell invasion, and miR-182 and miR-200 family members regulate its expression post-transcriptionally PMID: 23329838 Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain. PMID: 22661716 signaling-selective inhibition of the CXCR4-Galpha(13)-Rho axis prevents the metastatic spread of basal-like breast cancer cells. PMID: 21934106 alpha subunit of the G protein G13 regulates activity of one or more Gli transcription factors independently of smoothened PMID: 21757753 Negative regulation of Gq-mediated pathways in platelets by G(12/13) pathways through Fyn kinase PMID: 21592972 Galpha(12/13) regulate AP-1-dependent CYR61 induction in vascular smooth muscle, promoting migration, and they are upregulated with CYR61 in arteriosclerotic lesions. PMID: 21212405 A new role is described for Galpha13 as a mediator of chemokine receptor CXCR4 endosomal trafficking in human T cells. PMID: 21148034 Galpha(12) binds to p120(ctn) and modulates its phosphorylation status through a Rho-independent mechanism. Galpha(12) emerges as an important regulator of p120(ctn) function PMID: 20974127 Galpha12/13 upregulate matrix metalloproteinase-2 via p53 promoting human breast cell invasion. PMID: 20044778 G(alpha)(12) and G(alpha)13) exert a complex pattern of nonredundant effects in small cell lung cancer cells PMID: 20160064 This review gives an overview of Galpha12/13 signaling of G protein-coupled receptors with a focus on RhoGTPase nucleotide exchange factor (RhoGEF) proteins as the immediate mediators of G12/13 activation. PMID: 19226283 The studies highlighted in this review provide compelling evidence that Galpha12 and Galpha13 play pivotal roles in many aspects of cancer invasion and metastasis. PMID: 19422395 study demonstrates not only a function of integrin alphaIIbbeta3 as a noncanonical Galpha13-coupled receptor but also a new concept of Galpha13-dependent dynamic regulation of RhoA PMID: 20075254 Galpha12 and Galpha13 negatively regulate the adhesive functions of cadherin PMID: 11976333 Galpha13 is not associated with lipid rafts PMID: 12117999 Galpha13 can induce ppET-1 gene expression through a JNK-mediated pathway. PMID: 12135322 co-stimulation of G(12/13) and G(i) pathways is sufficient to activate GPIIb/IIIa in human platelets in a mechanism that involves intracellular calcium PMID: 12297512 These results suggest that protein kinase A blocks Rho activation by phosphorylation of Galpha(13) Thr(203). PMID: 12399457 Selective activation of Galpha(12) and Galpha(13) by thrombin and LPA, respectively, is determined by the N-terminal short sequences of alpha subunits. PMID: 12594220 Several features of a typical alpha/RGS interaction are preserved in the alpha(13)/p115RhoGEF interaction. PMID: 15735747 Galpha13-induced VASP phosphorylation that involves activation of RhoA and MEKK1, phosphorylation and degradation of IkappaB, release of PKA catalytic subunit from the complex with IkappaB and NF-kappaB, and subsequent phosphorylation of VASP PMID: 16046415 analysis of the molecular mechanism of how the human TXA2 receptor interacts with G alpha 13 to activate intracellular signaling PMID: 16212421 Estrogen receptor alpha interacts with Galpha13 to drive actin remodeling and endothelial cell migration. PMID: 16601072 Results identify the G12 family proteins Galpha12 and 13 as important regulators of prostate cancer invasion and suggest that these proteins may be targeted to limit invasion- and metastasis-induced prostate cancer patient mortality. PMID: 16787920 Galpha13-Rho signaling axis is required for SDF-1-induced migration through CXCR4 PMID: 17056591 Distinct regions of Galpha13 participate in its regulatory interactions with RGS homology domain-containing RhoGEFs. PMID: 17449226 analysis of a novel cross-talk exerted from the LPA/Galpha(13)/p115RhoGEF/RhoA pathway to the beta(2)-adrenergic receptor/Galpha(s)/adenylyl cyclase pathway PMID: 17493936 G alpha(12/13) regulate basal p53 levels via mdm4, which constitutes a cell signaling pathway distinct from p53 phosphorylations elicited by genotoxic stress. PMID: 17510313 role in regulating ASK1 expression levels PMID: 17595347 provides first examination of Galpha12 and Galpha13 in the human heart, demonstrating selective activation of human atrial Galpha12 and Galpha13 by endothelin and angiotensin receptors, respectively PMID: 17878759 A pronounced and rapid translocation of p115-RhoGEF from the cytosol to the plasma membrane was observed upon activation of several G(12/13)-coupled receptors in a cell type-independent fashion. PMID: 18320579 AC7 is a specific downstream effector of the G(12/13) pathway PMID: 18541530

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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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