Recombinant Human Rho Guanine Nucleotide Exchange Factor 12 (ARHGEF12) Protein (His)

Name: Recombinant Human Rho Guanine Nucleotide Exchange Factor 12 (ARHGEF12) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01779P
Price: 240.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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100ug

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Product Overview

Description	Recombinant Human Rho Guanine Nucleotide Exchange Factor 12 (ARHGEF12) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9NZN5
Target Symbol	ARHGEF12
Synonyms	Leukemia-associated RhoGEF
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	GQCSCFQSIELLKSRPAHLAVFLHHVVSQFDPATLLCYLYSDLYKHTNSKETRRIFLEFHQFFLDRSAHLKVSVPDEMSADLEKRRPELIPEDLHRHYIQTMQERVHPEVQRHLEDFRQKRSMGLTLAESELTKLDAERDKDRLTLEKERTCAEQIVAKIEEVLMTAQAVEEDKSSTMQYVILMYMKHLGVK
Expression Range	367-558aa
Protein Length	Partial
Mol. Weight	28.7 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	May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13.
Subcellular Location	Cytoplasm. Membrane.
Database References	HGNC: 14193 OMIM: 604763 KEGG: hsa:23365 STRING: 9606.ENSP00000380942 UniGene: PMID: 29279389 We studied the function of LARG in murine and human megakaryocytes and platelets with Larg knockout (KO), shRNA-mediated knockdown and small molecule-mediated inhibition. We found that LARG is important for human, but not murine, megakaryocyte maturation. PMID: 27345948 that leukemia-associated Rho guanine-nucleotide exchange factor can be directly phosphorylated by cyclin-dependent kinase 1 PMID: 26483157 Two related guanine nucleotide exchange factors (GEFs), PDZ-RhoGEF and leukemia-associated RhoGEF (LARG), use their PDZ domains to bind class B plexins and play critical roles in signaling. PMID: 26627240 this study identified a novel association between IOP and ARHGEF12. PMID: 25637523 TGF-beta regulates LARG and GEF-H1 during epithelial-mesenchymal transition to affect stiffening response to force and cell invasion. PMID: 25143398 LARG is a novel and temporally distinct Rho Guanine Nucleotide Exchange Factor required for completion of abscission. PMID: 23885121 Data indicate that ICAM-1 signaling activates leukemia-associated Rho guanine nucleotide exchange factor (LARG), also known as Rho GEF 12 (ARHGEF12). PMID: 24585879 Agonist-induced Ca2+ sensitization in smooth muscle: redundancy of Rho guanine nucleotide exchange factors (RhoGEFs) and response kinetics, a caged compound study. PMID: 24106280 RhoGEF activity of p210 BCR/ABL directly contributes to transforming activity, and may account for the difference in disease outcome associated with p190 BCR/ABL and p210 BCR/ABL. PMID: 23207522 NIS enhanced cell migration and invasion by binding to leukemia-associated RhoA guanine exchange factor PMID: 22962269 The PDZ domain of LARG is required HRH1-mediated activation of the strictly Rho-dependent transcriptional activity of serum response factor and can be mimicked by activated Galpha(q)(Q209L). PMID: 22100544 Mechanistic insights into specificity, activity, and regulatory elements of the regulator of G-protein signaling (RGS)-containing Rho-specific guanine nucleotide exchange factors (GEFs) p115, PDZ-RhoGEF (PRG), and leukemia-associated RhoGEF (LARG). PMID: 21454492 a novel physical and functional interaction between ABCA1 and PDZ-RhoGEF/LARG, which activates RhoA, resulting in ABCA1 stabilization and cholesterol efflux activity. PMID: 20348106 Regulation of G protein-linked guanine nucleotide exchange factors for Rho, PDZ-RhoGEF, and LARG by tyrosine phosphorylation: evidence of a role for focal adhesion kinase PMID: 11799111 Plexin B regulates Rho through the guanine nucleotide exchange factors leukemia-associated protein and PDZ-RhoGEF. PMID: 12183458 LARG plays a critical role in plexin-B1 signaling to stimulate Rho activation and cytoskeletal reorganization. PMID: 12196628 Rho activation through Galpha12 and the regulation of RhoGEFs by heterotrimeric G proteins G1213 is further modulated by tyrosine phosphorylated leukemia-associated RhoGEF. PMID: 12515866 Data show that different rho guanine nucleotide exchange factors (rhoGEFs; p115rhoGEF, LARG and PDZrhoGEF) mediate downstream rho signaling by the thrombin and lysophosphatidic acid receptors. PMID: 15143072 analysis of LARG RhoA binding and nucleotide exchange structure PMID: 15331592 CD44 interaction with LARG and EGFR plays a pivotal role in Rho/Ras co-activation, PLC epsilon-Ca2+ signaling, and Raf/ERK up-regulation required for CaMKII-mediated cytoskeleton function and in head and neck squamous cell carcinoma progression PMID: 16565089 Tyr1306Cys substitution in LARG, through its differential activation of RhoA, increases insulin sensitivity in nondiabetic Pima Indians. PMID: 16644711 There is no evidence in the Caucasian KORA study that variants of the LARG gene confer susceptibility for type 2 diabetes, insulin sensitivity, or the metabolic syndrome PMID: 17766704 Analysis of the (15)N relaxation data using reduced spectral density mapping shows that the apo LARG PDZ is flexible and exhibits internal motions on both picosecond to nanosecond and microsecond to millisecond timescales PMID: 18411422 Moreover, leukemia-associated guanine nucleotide exchange factor (LARG) associates with Unc5B to transduce the RhoA signal. PMID: 19273616 mutations in the hydrophobic patch do not have a significant effect on in vitro activity, but abolished the ability of LARG to activate RhoA and to induce stress fiber formation in cultured cells. PMID: 19560536 LARG at chromosome 11q23 has functional characteristics of a tumor suppressor in human breast and colorectal cancer PMID: 19734946

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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.