Recombinant Human Gelsolin (GSN) Protein (His)

Name: Recombinant Human Gelsolin (GSN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01519P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Cytokines, Recombinant proteins

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Product Overview

Description	Recombinant Human Gelsolin (GSN) 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	P06396
Target Symbol	GSN
Synonyms	AGEL;Actin-depolymerizing factor;ADF
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	DEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA
Expression Range	514-782aa
Protein Length	Partial
Mol. Weight	33.5 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	Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.
Subcellular Location	[Isoform 2]: Cytoplasm, cytoskeleton.; [Isoform 1]: Secreted.
Protein Families	Villin/gelsolin family
Database References	HGNC: 4620 OMIM: 105120 KEGG: hsa:2934 STRING: 9606.ENSP00000362924 UniGene: Hs.522373
Associated Diseases	Amyloidosis 5 (AMYL5)
Tissue Specificity	Phagocytic cells, platelets, fibroblasts, nonmuscle cells, smooth and skeletal muscle cells.

Gene Functions References

the gelsolin N184K variant is subjected to the same aberrant proteolytic events responsible for the formation of amyloidogenic fragments in the previously characterized mutants. PMID: 27633054
Induction of cell stress alters the actin cytoskeleton in intestinal epithelial cells via changes in the actin-binding proteins villin-1 and gelsolin. PMID: 29274870
Gelsolin upregulation promotes radioresistance in non-small cell lung cancer cells, at least partially, through activation of phosphoinositide 3-kinase/Akt signaling. PMID: 27121073
Results identify GSN as target of miR-200a which inhibits the release of microvesicles in hepatocellular carcinoma cells by functionally regulating GSN. PMID: 28440466
Gelsolin enhances the invasive capacity of colon cancer cells via elevating intracellular superoxide (O2.-) levels by interacting with Cu/ZnSOD, and gelsolin gene expression positively correlates with urokinase plasminogen activator (uPA), an important matrix-degrading protease invovled in cancer invasion. PMID: 27391159
these data profile the importance of the physical interaction between HPV16 E7 and gelsolin in the acquisition of the metastatic phenotype by cervical cancer cells PMID: 27072581
Our study highlights gelsolin as an important pro-disseminative factor contributing to the aggressive phenotype of diffuse gastric cancer PMID: 27058427
study strongly supported the contribution of the genes ITGA2B, GSN and RHOA and the two pathways "regulation of actin cytoskeleton" and "leukocyte transendothelial migration" to osteoporosis risk. PMID: 27153759
SSH1 binds to gelsolin via actin filaments in the cytosolic fraction. Gelsolin promoted solubilization of actin filaments and SSH1 in cell-free assays and in cultured cells. PMID: 25451266
free actin likely contributes to impaired host defense by blocking scavenger receptor binding of bacteria. PMID: 28385809
analysis of how YopO disrupts normal gelsolin function to alter host actin dynamics and thus cripple phagocytosis PMID: 28280241
Our present study implied that the synergistic effect of pGSN and pIgA induced glomerular fibrosis via the TGF-beta1/Smads signal transduction pathway. This might be a potential mechanism for the glomerular fibrosis observed in IgAN patients. PMID: 28208683
The expression levels of GSN were observed to be reduced in colon carcinoma (CC) cells, and the reduced expression level of GSN was often associated with a poorer metastasisfree survival rate in patients with CC (P=0.04). In addition, the overexpression of GSN inhibited the invasion of CC cells in vitro. PMID: 27573444
in chronic hemodialysis patients, lower pGSN levels were not associated with hospitalization, all-cause and cardio-vascular mortality, even though pGSN was inversely correlated with age, CRP and IL-6, suggesting that inflammation may influence pGSN PMID: 28114138
PODXL enhances motility and invasiveness through an increase in gelsolin-actin interactions in cell protrusions. PMID: 27461278
These findings suggest that gelsolin may have a role in the disease process in atopic dermatitis patients. PMID: 26318415
Plasma GSN may play an important role in the development of immunoglobulin A (IgA) nephropathy. PMID: 27997897
beta-Catenin seems to be involved in the regulation of gelsolin expression, which in turn affects the migratory ability of colonic cancer cells PMID: 27798885
hypoxia or GSN overexpression induces HIF-1alpha expression and reduces the expression of survival markers p-Akt and Bcl-2 in H9c2 cardiomyoblast cells PMID: 27193608
Increasing amount of amyloid are associated with the severity of clinical features in hereditary gelsolin amyloidosis. PMID: 27879149
The rs1078305 and rs10818524 SNPs of GSN were associated with increased risk for oral squamous cell carcinoma development in a Chinese Han population PMID: 26848502
Lower blood levels of gelsolin associated with progressive aortic arch calcification. PMID: 26941566
Gelsolin protein, human, yielded a receiver operating characteristics value of 89% for node-positive OSCC PMID: 25223295
GSN overexpression suppresses apoptosis while down-regulated GSN promotes apoptosis in hepatocellular carcinoma. PMID: 26823700
Fragmented gelsolins may be associated with the pathogenesis of fibrosis in RA-ILD. PMID: 26666486
gelsolin interacts with particular components of the three cytoskeleton systems and is a constituent of midbodies PMID: 26598132
novel roles for actin-depolymerizing factor and cofilin-1 in regulating the remodeling and permeability of epithelial junctions PMID: 26878213
The overexpression of GSN may inhibit the proliferation, adhesion ability and invasion of 786-0 clear cell renal cell carcinoma cell line. PMID: 26398833
Serum-expressed apolipoprotein B-100 protein, C9 Complement, and gelsolin can be used for differential diagnosis of Barrertts esophagus and adenocarcinoma of esophagus. PMID: 26404905
TGF-beta1 induced epigenetic modification of GSN could alter the EMT process in breast cancer cells. PMID: 26482896
GSNs might play a regulatory role in the suppression of the tissue damage induced by acute radiation exposure PMID: 25164111
We designed and synthesized siRNA against various exons in the gelsolin gene (GSN)..our finds reveal siRNA, which is derived from target gene exon, can form the complex with H3 histone to be involved in the regulation of gene expression PMID: 25600697
Results show that high gelsolin levels are associated with better prognosis in ER+HER2- breast cancer and a reduction in tumor cell migration. PMID: 26408687
Gelsolin expression promoted tumor-associated phenotypes by facilitating proliferative and invasive capacities of hepatocellular carcinoma(HCC) cells, which might serve as a potential therapeutic target for HCC treatment. PMID: 26149653
Based on the obtained results, we propose that the gelsolin is an important cellular target for cotinine, through which this compound influences on the basic processes involved in neoplastic transformation and metastasis, such as migration and apoptosis PMID: 25544037
Group B Streptococcus-beta-haemolysin is solely responsible for gelsolin increase causing, through membrane permeability defects, calcium influx and calpain activation. PMID: 25130983
Plasma gelsolin levels decrease in the blood of type II diabetics. Recombinant gelsolin helped in improving glycemic control in diabetic mice. PMID: 25478578
Data show that gelsolin (GSN) plays an important role in the regulation of gynecological cell fate as reflected in dysregulation in chemosensitivity. PMID: 25246592
Data indicate gelsolin in contributing to the invasive potential of LNCaP prostate adenocarcinoma cells. PMID: 25581609
Gelsolin levels were a useful tool to predict functional outcome and mortality after aneurysmal subarachnoid hemorrhage. PMID: 23880145
increased plasma levels after allergen-specific immunotherapy PMID: 24980225
Patients developing cardiopulmonary bypass acute lung injury had lower plasma gelsolin reservoir and a much more amount and rapid consumption of plasma gelsolin early after operation PMID: 25126004
This study improves the knowledge of the genetic features of Mexican patients with corneal stromal dystrophies by identifying mutations in the TGFBI, CHST6, and GSN genes. PMID: 24801599
GSN is important for chemoresistance in head-and-neck cancer PMID: 24771612
we predict that the gene silencing of GSN and/or the downstream blocking of GSN along the p38 pathway could be applied to ameliorate pathological cardiac hypertrophy in the future PMID: 24505034
Ceruloplasmin and gelsolin are closely interacted with the oncogene NF-kappab. PMID: 23925487
Plasma gelsolin is lower in normal pregnancy than in non-pregnant women. It is also significantly lower in pre-eclampsia than in normal pregnancy. PMID: 24239294
This study found significantly lower plasma gelsolin levels in patients with systemic lupus erythematosus and rheumatoid arthritis compared with healthy controls PMID: 24122723
Expression of mutant form of human gelsolin in mice under the control of a muscle-specific promoter induced myopathic changes reminiscent of human inclusion body myositis. PMID: 24047347
Gelsolin can constitute a barrier that restricts HIV-1 infection of CD4+ lymphocytes in a pre-fusion step. PMID: 23575248

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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.