Recombinant Human FSTL1/FRP Protein

Beta LifeScience SKU/CAT #: BLA-0255P

Recombinant Human FSTL1/FRP Protein

Beta LifeScience SKU/CAT #: BLA-0255P
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Product Overview

Host Species Human
Accession Q12841
Synonym Anti FSTL1 FLJ50214 FLJ52277 Follistatin like 1 Follistatin related protein Follistatin-like protein 1 Follistatin-related protein 1 FRP FSL1 FSTL1 FSTL1 antibody FSTL1_HUMAN Micro RNA 198 MIR198 miRNA198 included OCC 1 OCC1
Description Recombinant Human FSTL1/FRP Protein was expressed in CHO cells. It is a Full length protein
Source CHO cells
AA Sequence EEELRSKSKICANVFCGAGRECAVTEKGEPTCLCIEQCKPHKRPVCGSNG KTYLNHCELHRDACLTGSKIQVDYDGHCKEKKSVSPSASPVVCYQSNRDE LRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLK FVEQNETAINITTYPDQENNKLLRGLCVDALIELSDENADWKLSFQEFLK CLNPSFNPPEKKCALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGK NQKGAQTQTEEEMTRYVQELQKHQETAEKTKRVSTKEI
Molecular Weight 33 kDa
Purity >95% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its binding ability in a functional ELISA. When this protein is coated at 200 ng/well, the concentration of recombinant human BMP-4 that produces 50% of the optimal binding response is found to be approximately 250 ng/mL.
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

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
Tissue Specificity Overexpressed in synovial tissues from rheumatoid arthritis.

Gene Functions References

  1. In cultured human pulmonary artery smooth muscle cells, hypoxia-promoted cellular viability, DNA synthesis and migration were suppressed by exogenous FSTL1 but enhanced by small interfering RNA targeting FSTL1 PMID: 28361925
  2. 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
  3. Segmental allergen challenge increases levels of airway follistatin-like 1 in patients with asthma. PMID: 27001159
  4. 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
  5. 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
  6. Dendritic cell-mediated immunity was activated by FSTL1. PMID: 29135371
  7. Fstl1serves an important role in liver fibrosis and target deletion of Fstl1 attenuated HSCs activation through suppressing TGFbeta1/Smad3 signaling pathway. PMID: 28901425
  8. 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
  9. Data show that follistatin-like 1 (FSTL1) contributed to unfavorable post-surgical outcome of hepatocellular carcinoma (HCC) patients via inhibiting cell apoptosis. PMID: 28655132
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. 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
  16. FSTL1 mRNA levels increased in castration-resistant prostate cancer in association with predominantly nuclear FSTL1. PMID: 27976415
  17. FSTL1 may induce epithelial mesenchymal transition and airway remodeling by activating autophagy. PMID: 28473327
  18. DROMs levels positively associated with Fstl1, Hemoglobin A1c and hsCRP levels. PMID: 27145224
  19. 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
  20. 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
  21. 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
  22. 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
  23. Children with chronic heart failure group had a significantly higher serum level of FSTL1 than the control group. PMID: 26903060
  24. 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
  25. FSTL1 is elevated in patients with osteoarthritis and involved in the progression of synovial inflammation. PMID: 25888873
  26. 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
  27. 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
  28. 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
  29. 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
  30. FSTL1 is a potential mediator of inflammation and insulin resistance in obesity. PMID: 24347831
  31. These results suggest that FSTL-1 may act on the NLRP3 inflammasome to promote IL-1beta secretion from monocytes/macrophages. PMID: 24470197
  32. 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
  33. 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
  34. Data show that the serum and synovial fluid (SF) FSTL1 levels were markedly higher in female OA patients than in males. PMID: 22117761
  35. FRP has the function of evoking innate immune responses as one of the endogenous TLR4 agonists. PMID: 22265692
  36. Elevated FSTL1 levels reflect not only joint diseases but also inflammation and tissue degradation in systemic autoimmune diseases. PMID: 21303509
  37. 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
  38. 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
  39. Whilst follistatin expression is unchanged, follistatin-related gene is down-regulated in endometrial carcinoma. PMID: 15296481
  40. FRP mRNA is overexpressed in rheumatoid arthritis synovium, the product of which exerts inhibitory activity on synovial cell growth PMID: 15638044
  41. TSC-36 can be induced in VSMCs (vascular smooth muscle cells) and inhibits VSMCs proliferation in vitro and in vivo. PMID: 16256108
  42. 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
  43. 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
  44. 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
  45. 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

FAQs

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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.

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