Recombinant Human Follistatin-Related Protein 1 (FSTL1) Protein (His-GST)

Name: Recombinant Human Follistatin-Related Protein 1 (FSTL1) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-07333P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality cytokines for advanced research, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Follistatin-Related Protein 1 (FSTL1) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q12841
Target Symbol	FSTL1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	ETAINITTYPDQENNKLLRGLCVDALIELSDENADWKLSFQEFLKCLNPSFNPPEKKCALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKNQKGAQTQTEEEMTR
Expression Range	176-285aa
Protein Length	Partial
Mol. Weight	43.8 kDa
Research Area	Cardiovascular
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	Secreted glycoprotein that is involved in various physiological processes, such as angiogenesis, regulation of the immune response, cell proliferation and differentiation. Plays a role in the development of the central nervous system, skeletal system, lungs, and ureter. Promotes endothelial cell survival, migration and differentiation into network structures in an AKT-dependent manner. Also promotes survival of cardiac myocytes. Initiates various signaling cascades by activating different receptors on the cell surface such as DIP2A, TLR4 or BMP receptors.
Subcellular Location	Secreted.
Database References	HGNC: 3972 OMIM: 605547 KEGG: hsa:11167 STRING: 9606.ENSP00000295633 UniGene: PMID: 28361925 Study suggests that follistatin like 1 plays an important role in lung fibrosis, and may serve as a novel therapeutic target for treatment of silicosis. PMID: 28341862 Segmental allergen challenge increases levels of airway follistatin-like 1 in patients with asthma. PMID: 27001159 Study found that FSTL1 was downregulated in non-small cell lung cancer (NSCLC) cells. FSTL1 overexpression suppressed tumor cell proliferation, altered cell cycle and induced apoptosis in addition to inhibiting cell survival, migration and invasion. Altogether, results revealed the critical tumor-suppression function of FSTL1 in NSCLC progression, suggesting it as an important factor in NSCLC progression. PMID: 29115636 Smad3 knockdown could restore the inhibition of cell proliferation induced by FSTL1 overexpression in MDAMB231FSTL1 cells, indicating that the antiproliferative effect of FSTL1 overexpression may be associated with Smad3 involved TGFbeta signaling pathway regulation. This study identified FSTL1 as an inhibitor of cell proliferation in MDAMB231 and 231BR cell lines PMID: 29048681 Dendritic cell-mediated immunity was activated by FSTL1. PMID: 29135371 Fstl1serves an important role in liver fibrosis and target deletion of Fstl1 attenuated HSCs activation through suppressing TGFbeta1/Smad3 signaling pathway. PMID: 28901425 Results showed that: 1- FSTL-1 expression is localized to the stromal compartment of the pancreas; 2- FSTL-1 expression is reduced in pancreatic cancer, and 3- FSTL-1 inhibited pancreatic cancer cell proliferation. PMID: 27886258 Data show that follistatin-like 1 (FSTL1) contributed to unfavorable post-surgical outcome of hepatocellular carcinoma (HCC) patients via inhibiting cell apoptosis. PMID: 28655132 results indicate that rs1259293 is associated with an increased risk and unfavorable postoperative prognosis of renal cell carcinoma, possibly by down-regulating FSTL1 expression in renal tissues. PMID: 27225192 Data provide evidence that FSTL1 modestly affects the proliferation of breast cancer cells and vascular endothelial cells. These findings improve the understanding of the functions of FSTL1 in breast cancer development and angiogenesis. PMID: 28857515 knockdown of FSTL1 inhibited ASM cell proliferation and migration induced by PDGF-BB at least partially via inhibiting the activation of ERK and AKT. These results provide novel insight into the pathogenesis of airway remodeling in childhood asthma and FSTL1 may be a possible therapeutic strategy for the treatment of asthma. PMID: 28393245 Fstl1 inhibited Smad1/5/8 phosphorylation by blocking the association between bone morphogenetic protein 4 and Bone Morphogenetic Protein Receptors, Type II via competitive binding to bone morphogenetic protein 4. PMID: 29212066 Data show that follistatin like-1 (FSTL1) was frequently downregulated in nasopharyngeal carcinoma (NPC) cell lines and primary tumor biopsies by promoter hypermethylation. PMID: 26918942 Results indicate the significance of follistatin-like protein 1 (FSTL1) in driving oncogenesis and metastasis in esophageal squamous cell carcinoma (ESCC) by coordinating NF-kappa B (NFkappaB) and bone morphogenetic proteins (BMP) pathway control. PMID: 28883005 FSTL1 mRNA levels increased in castration-resistant prostate cancer in association with predominantly nuclear FSTL1. PMID: 27976415 FSTL1 may induce epithelial mesenchymal transition and airway remodeling by activating autophagy. PMID: 28473327 DROMs levels positively associated with Fstl1, Hemoglobin A1c and hsCRP levels. PMID: 27145224 FSTL1 displays anti-inflammatory effects against oxidized low-density lipoprotein-induced pro-inflammatory cytokine production via a mechanism that involves the TLR4/MyD88/NF-kappaB and MAPK signaling pathways. PMID: 27569284 this study shows that 1) the expression of follistatin-like protein 1 is upregulated in rheumatoid arthritis patients; 2) miR-27a inhibits cell migration of rheumatoid arthritis synoviocytes by targeting follistatin-like protein 1 and restraining the TLR4/NFkappaB pathway PMID: 27498552 FSTL1 plays a critical role in immune regulation, enhancing the antigen presentation ability of dendritic cells by up-regulating NF-kappab expression and down-regulating JNK expression. PMID: 27859422 the knockdown of FSTL1 induces apoptosis through a mitotic arrest and caspase-dependent cell death. FSTL1 plays the important roles in cellular proliferation and apoptosis in lung cancer cells, and thus can be a new target for lung cancer treatment. PMID: 26716515 Children with chronic heart failure group had a significantly higher serum level of FSTL1 than the control group. PMID: 26903060 provide mechanistic insight into the regulation of erythropoiesis by FSTL1 signaling and lay a foundation for exploring FSTL1 signaling as a therapeutic target for anemia PMID: 26365350 FSTL1 is elevated in patients with osteoarthritis and involved in the progression of synovial inflammation. PMID: 25888873 administration of Fstl1 induced airway remodeling and increased OSM, whereas administration of an anti-OSM Ab blocked the effect of Fstl1 on inducing airway remodeling, eosinophilic airway inflammation PMID: 26355153 data suggest that the loss of epicardial FSTL1 is a maladaptive response to injury, and that its restoration would be an effective way to reverse myocardial death and remodelling following myocardial infarction in humans PMID: 26375005 Fstl1 is induced in response to lung injury and promotes the accumulation of myofibroblasts and subsequent fibrosis. These data suggest that Fstl1 may serve as a novel therapeutic target for treatment of progressive lung fibrosis. PMID: 25584011 FSTL1 is elevated in various inflammatory conditions and decreased during the course of treatment. FSTL1 may therefore be a valuable biomarker for such diseases. PMID: 24838142 FSTL1 is a potential mediator of inflammation and insulin resistance in obesity. PMID: 24347831 These results suggest that FSTL-1 may act on the NLRP3 inflammasome to promote IL-1beta secretion from monocytes/macrophages. PMID: 24470197 results demonstrated that follistatin-like protein 1 (Fstl1) is expressed and secreted by human myotubes and plasma Fstl1 levels are increased after exercise PMID: 23419164 A clear inverse correlation between the expression pattern of FSTL1 (pro-migratory) and miR-198 (anti-migratory) highlights the importance of this regulatory switch in controlling context-specific gene expression to orchestrate wound re-epithelialization. PMID: 23395958 Data show that the serum and synovial fluid (SF) FSTL1 levels were markedly higher in female OA patients than in males. PMID: 22117761 FRP has the function of evoking innate immune responses as one of the endogenous TLR4 agonists. PMID: 22265692 Elevated FSTL1 levels reflect not only joint diseases but also inflammation and tissue degradation in systemic autoimmune diseases. PMID: 21303509 These data suggest that Cx43 inhibits the invasion and metastasis of pulmonary giant cell carcinoma cells by modulating the secretion of FSTL1, which is regulated by histone acetylation. PMID: 21718795 DIP2A could be a cell-surface receptor protein and mediate a FOS down-regulation signal of FRP. FRP bound to DIP2A and CD14, and also with proteins of the TGF-beta superfamily PMID: 20860622 Whilst follistatin expression is unchanged, follistatin-related gene is down-regulated in endometrial carcinoma. PMID: 15296481 FRP mRNA is overexpressed in rheumatoid arthritis synovium, the product of which exerts inhibitory activity on synovial cell growth PMID: 15638044 TSC-36 can be induced in VSMCs (vascular smooth muscle cells) and inhibits VSMCs proliferation in vitro and in vivo. PMID: 16256108 Elevated myocardial expression of FST-like genes is a feature of heart failure and may be linked to both disease severity and mechanisms underlying recovery. PMID: 18617621 Fstl1 is a secreted muscle protein or myokine that can function to promote endothelial cell function and stimulates revascularization in response to ischemic insult through its ability to activate Akt-eNOS signaling PMID: 18718903 Cell migration and invasion assays demonstrated a remarkably lower cell migration and invasion capability in FSTL1-transfected cells in relation to downregulation of matrix metallopeptidase-2 PMID: 18796737 FSTL-1 is overexpressed by 2-3-fold in synovial tissues of rheumatoid arthritis patients compared with control synovium obtained from subjects undergoing knee arthroscopic anterior cruciate ligament repair. PMID: 19109154

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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.