Recombinant Human Girdin (CCDC88A) Protein (His)

Name: Recombinant Human Girdin (CCDC88A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06823P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Girdin (CCDC88A) 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	Q3V6T2
Target Symbol	CCDC88A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SLSVSSDFLGKDKPVSCGLARSVSGKTPGDFYDRRTTKPEFLRPGPRKTEDTYFISSAGKPTPGTQGKIKLVKESSLSRQSKDSNPYATLPRASSVISTAEGTTRRTSIHD
Expression Range	1713-1823aa
Protein Length	Partial
Mol. Weight	16.1 kDa
Research Area	Neuroscience
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	Bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. Also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. Essential for cell migration. Interacts in complex with G(i) alpha subunits with the EGFR receptor, retaining EGFR at the cell membrane following ligand stimulation and promoting EGFR signaling which triggers cell migration. Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex which enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB. Phosphorylation of AKT1/PKB induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation. Binds in its tyrosine-phosphorylated form to the phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1 which enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration. Plays a role as a key modulator of the AKT-mTOR signaling pathway, controlling the tempo of the process of newborn neuron integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Inhibition of G(s) subunit alpha GNAS leads to reduced cellular levels of cAMP and suppression of cell proliferation. Essential for the integrity of the actin cytoskeleton. Required for formation of actin stress fibers and lamellipodia. May be involved in membrane sorting in the early endosome. Plays a role in ciliogenesis and cilium morphology and positioning and this may partly be through regulation of the localization of scaffolding protein CROCC/Rootletin.
Subcellular Location	Cell membrane; Peripheral membrane protein. Cytoplasm, cytosol. Cytoplasmic vesicle. Cell projection, lamellipodium. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole.
Protein Families	CCDC88 family
Database References	HGNC: 25523 OMIM: 609736 KEGG: hsa:55704 STRING: 9606.ENSP00000338728 UniGene: PMID: 30194792 Study revealed that the downregulation of the expression of Girdin can inhibit the proliferation, invasion and migration of colorectal cancer cells through decrease in proinflammatory cytokine production and inhibition of JAK/STAT signaling. PMID: 29989653 Girdin may regulate cell processes. PMID: 29901184 The engulfment of platelets assisted in delaying the aging of endothelial cells via girdin and pgirdin, in which the AKT signal was involved. PMID: 29786109 Girdin can regulate glycolysis in hepatocellular carcinoma cells through the PI3K/AKT/HIF-1alpha signaling pathway, which decreases the sensitivity of tumor cells to radiotherapy. PMID: 28810896 Girdin expression may serve as a useful prognostic factor for invasive breast cancer, especially for the HER2 subtype. PMID: 28818465 The present study therefore suggests a role for Girdin as a novel therapeutic target for breast cancer, independent of subtype. PMID: 28713924 GIV is a bifunctional modulator of G proteins; it serves as a guanine nucleotide dissociation inhibitor (GDI) for Galphas using the same motif that allows it to serve as a guanine-nucleotide exchange factor for Galphai PMID: 27621449 GIV (Girdin) expression status predicts recurrence risk in patients with T3 pMMR stage II colon cancer. PMID: 27029492 Results show that high CCDC88A expression in human pancreatic ductal adenocarcinoma (PDAC) tissues is correlated with poor prognosis. Also, the findings suggest that CCDC88A can promote PDAC cell migration and invasion through a signaling pathway that involves phosphorylation/dephosphorylation of many proteins. PMID: 27919290 Here, theauthors identify GIV/Girdin as a novel effector of AMPK, whose phosphorylation at a single site is both necessary and sufficient for strengthening mammalian epithelial tight junctions and preserving cell polarity and barrier function in the face of energetic stress. PMID: 27813479 On the basis of the differential prognostic impact of tGIV/pYGIV within each molecular subtype, we propose a diagnostic algorithm PMID: 27440794 Results show that Girdin is important for formation and function of invadopodia enhanced by Dlg5-silencing in hepatocellular carcinoma cells. PMID: 28390157 Tyrosine Phosphorylation of an Actin-Binding Protein Girdin Specifically Marks Tuft Cells in Human and Mouse Gut PMID: 28375676 Overexpression of girdin is associated with invasion of hepatocellular carcinoma. PMID: 27623945 Heterotrimeric G protein signaling via GIV/Girdin is a ubiquitous mechanism in health and disease, and can be a target for molecular therapies. (Review) PMID: 26879989 miR-101 inhibits cell proliferation, migration and invasion in hepatocellular carcinoma through downregulating Girdin. PMID: 26743900 Phosphorylation of GIV at Tyr-1764/Tyr-1798 is also required to enhance PI3K-Akt signaling and tumor cell migration in response to integrin stimulation, indicating that GIV functions in Tyr(P)-dependent integrin signaling. PMID: 26887938 CCDC88A is essential for multiple aspects of normal development and loss of CCDC88A is a cause of the PEHO syndrome phenotype. PMID: 26917597 GIV is an essential upstream component that couples InsR to G-protein signaling to enhance the metabolic insulin response, and impairment of such coupling triggers IR. PMID: 26378251 Girdin regulates the migration and invasion of glioma cells via the PI3K-Akt signaling pathway. PMID: 26151295 The expression of Girdin protein in invasive breast cancer is strongly associated with lymph node metastasis. PMID: 24155038 GIV expression is up-regulated in liver after fibrotic injury and is required for hepatic stellate cells activation.Girdin is a central hub for profibrogenic signalling networks during liver fibrosis. PMID: 25043713 TAT-GIV peptides provide a novel and versatile tool to manipulate Galphai activation downstream of growth factors in a diverse array of pathophysiologic conditions. PMID: 25926659 transcriptional upregulation of Girdin expression and Girdin-Galphai3 signaling play crucial roles in regulating epithelial apicobasal polarity through the PAR complex. PMID: 25977476 GIV directly and constitutively binds the exocyst complex subunit Exo-70 and also associates with GLUT4-storage vesicles (GSVs) exclusively upon insulin stimulation. PMID: 26514725 Expression of tumor necrosis factor receptor-assicated factor 4 correlates with expression of Girdin and promotes nuclear translocation of Girdin in breast cancer PMID: 25591657 GIV and its substrate Galphai3 are recruited to active integrin complexes PMID: 26391662 the positive expression rate of Girdin in hepatocellular carcinoma tissues was 67.5%, higher than that found in adjacent tissues of 16.7% PMID: 25755745 findings suggest that the STAT3/Girdin/Akt pathway activates in osteoblasts in response to mechanical stimulation and may play a significant role in triggering osteoblast proliferation and migration during orthodontic treatment PMID: 26163263 Girdin regulates the trafficking of VE-cadherin in synergy with R-Ras. PMID: 25869066 Both SH2 and GEF domains of GIV are required for the formation of a ligand-activated ternary complex between GIV, Galphai3, and EGFR. PMID: 25187647 The study shows that girdin is phosphorylated on tyrosine 1798 when associated with structures required for migration. PMID: 25707853 The review discusses how GIV assembles alternative signaling pathways by sensing cues from various classes of surface receptors and relaying them via G protein activation. The dysregulation of this mechanism in disease is discussed. [review] PMID: 25605737 Findings demonstrate that Dlg5 interacts with and inhibits the activity of Girdin, thereby suppressing the migration of prostate cancer cells. PMID: 24662825 Girdin knockdown enhances chemosensitivity of colorectal cancer cells to oxaliplatin via TOP2B down-regulation. PMID: 25009397 This study showed that reduction of Girdin, an actin-binding protein, leads to impaired cell migration, adhesion, and invasion of human glioblastoma cells. PMID: 25060559 These results reveal that girdin regulates selective clathrin-mediated endocytosis via a mechanism involving dynamin 2, but not by operating as a cargo-specific adaptor. PMID: 25061227 This study identified a novel GWS association (1.17 x 10(-10)) mapped to chromosome 2 at rs1437396, between MTIF2 and CCDC88A, across all of the EA and AA cohorts. PMID: 24166409 Girdin was identified as a new and major regulator of the insulin signal in myoblasts and skeletal muscle. PMID: 23886629 Up-regulated autophagy was negatively associated with Girdin level. There was a significant correlation between Girdin expression and lymph nodes metastasis in invasive ductal breast carcinoma. PMID: 24326843 The levels of Girdin expression correlated inversely with the survival of esophageal squamous cell carcinoma patients. PMID: 23588413 These results demonstrate that girdin and its phosphorylation play an important role in neonatal vascular development and in pathological neovascularization in the retina. PMID: 23195430 Girdin protein may be a potential new distant metastasis biomarker of breast cancer PMID: 22116776 Our findings define EEA1 endosomes as major sites for proliferative signaling and establish that Galphas and GIV regulate EEA1 but not APPL endosome maturation PMID: 23051738 p-Girdin expression is closely correlated with the malignant progression of breast cancer. PMID: 22780975 STAT3 activation is directly integrated with the receptor tyrosine kinase-GIV-G protein signaling axis. PMID: 23066027 The Girdin protein may be a potential new early liver metastasis biomarker of colorectal cancer. PMID: 22714912 These data demonstrate that Girdin is important for efficient cell division PMID: 22755556 Girdin regulates cell movement in biological contexts that require directional cell movement PMID: 22574214

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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.