Recombinant Human Fibulin-1 (FBLN1) Protein (Myc&His)

Name: Recombinant Human Fibulin-1 (FBLN1) Protein (Myc&His)
Brand: Beta LifeScience
SKU: BLC-06101P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Fibulin-1 (FBLN1) Protein (Myc&His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P23142
Target Symbol	FBLN1
Synonyms	Basement membrane protein 90; BM 90; FBLN; Fbln1; FBLN1_HUMAN; FIBL 1; FIBL-1; FIBL1; Fibulin 1; Fibulin-1
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	C-Myc&C-6His
Target Protein Sequence	DVLLEACCADGHRMATHQKDCSLPYATESKECRMVQEQCCHSQLEELHCATGISLANEQDRCATPHGDNASLEATFVKRCCHCCLLGRAAQAQGQSCEYSLMVGYQCGQVFQACCVKSQETGDLDVGGLQETDKIIEVEEEQEDPYLNDRCRGGGPCKQQCRDTGDEVVCSCFVGYQLLSDGVSCEDVNECITGSHSCRLGESCINTVGSFRCQRDSSCGTGYELTEDNSCKDIDECESGIHNCLPDFICQNTLGSFRCRPKLQCKSGFIQDALGNCIDINECLSISAPCPIGHTCINTEGSYTCQKNVPNCGRGYHLNEEGTRCVDVDECAPPAEPCGKGHRCVNSPGSFRCECKTGYYFDGISRMCVDVNECQRYPGRLCGHKCENTLGSYLCSCSVGFRLSVDGRSCEDINECSSSPCSQECANVYGSYQCYCRRGYQLSDVDGVTCEDIDECALPTGGHICSYRCINIPGSFQCSCPSSGYRLAPNGRNCQDIDECVTGIHNCSINETCFNIQGGFRCLAFECPENYRRSAATLQQEKTDTVRCIKSCRPNDVTCVFDPVHTISHTVISLPTFREFTRPEEIIFLRAITPPHPASQANIIFDITEGNLRDSFDIIKRYMDGMTVGVVRQVRPIVGPFHAVLKLEMNYVVGGVVSHRNVVNVHIFVSEYWF
Expression Range	30-703aa
Protein Length	Full Length of Mature Protein
Mol. Weight	77.3 kDa
Research Area	Cancer
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	Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Protein Families	Fibulin family
Database References	HGNC: 3600 OMIM: 135820 KEGG: hsa:2192 STRING: 9606.ENSP00000331544 UniGene: PMID: 29715435 Fibulin-1 is expressed in breast cancer cell lines, interacts wtih SHBG, and is increased by estradiol PMID: 29940241 This study demonstrated that FBLN1 can effectively promote osteogenic differentiation of human nasal inferior turbinate-derived mesenchymal stem cells into osteoblasts. PMID: 28445604 This study demonstrated that fibulin-1 (FBLN1) was detected in the serums of Alzheimer disease patients PMID: 27911324 Interestingly and in contrast with our expectation, we found that the expression level of FBLN-4 and BCRP were downregulated in tumor compared to adjacent normal tissues. FBLN-4 was associated with grade histology and therefore can be considered as a potential prognostic biomarker. PMID: 28282800 Serum and vitreous fibulin-1 concentrations are elevated under diabetic retinopathy condition. PMID: 27422995 Galectin-3 and fibulin-1 levels are elevated in heart failure patients with impaired glucose metabolism. Reduced LV contractile reserve among HF patients with DM does not to have an independent impact on plasma Gal-3 and fibulin-1 levels. PMID: 28068900 changes in methylation levels in cfDNA associated with hepatocellular carcinoma and could represent useful plasma-based biomarker PMID: 28333958 The FBLN1/FGF8 interaction may also be involved in the survival of neural crest cell population during development. PMID: 27402846 Low expression of fibulin-1 is associated with gastric cancer. PMID: 26779638 LDH associated positively with fibulin-1 (beta = 0.23; p < 0.001) and ROS (beta = 0.11; p = 0.30) in blacks only with cardiovascular disease. PMID: 26631026 The procedure described is the first to our knowledge that enables a large scale purification of Fibulin-1 from human plasma. PMID: 26826315 Study identifies a novel fibulin-1D variant, named fibulin-1D', comprising 638 amino acids with molecular weight of 70.5 kDa. Fibulin-1D' lacks a secretion sequence, has a truncated N-terminus domain and binds to the intracellular domain of integrin beta1. PMID: 25661773 The purpose of this study was to develop and characterize robust quantitative assays for the emerging cardiovascular biomarker fibulin-1 and its circulating isoforms in human plasma. PMID: 25331251 Extracellular matrix biomarker, fibulin-1 and its association with soluble uPAR in a bi-ethnic South African population PMID: 25456503 Treatment with low-dose spironolactone reduced plasma fibulin-1 levels in patients with type 2 diabetes and resistant hypertension. PMID: 24739800 fibulin-1 expression is associated with NMIBC grade and recurrence, it is epigenetically down-regulated and functions as a tumor suppressor gene and angiogenesis inhibitor in bladder cancer. PMID: 25234557 Plasma fibulin-1 is independently associated with pulse wave velocity in type 2 diabetics. PMID: 23866070 Increased levels of fibulin-1 were independently associated with higher levels of suPAR and NT-proBNP especially in patients with lower aortic valve stenosis PMID: 25014213 Mutation of fibulin-1 causes a novel syndrome involving the central nervous system and connective tissues. PMID: 24084572 FBLN1 functions as a novel candidate tumor suppressor gene in CM, and its downregulation may be due to promoter hypermethylation. PMID: 23907575 Increased plasma fibulin-1 levels are associated with diabetes and impaired kidney function. PMID: 23294625 Fibulin-1 is down regulated in renal cell carcinoma through promoter hypermethylation. PMID: 23391467 In single regression analysis, NT-proBNP was significantly associated with fibulin-1 in African men and Caucasian women. PMID: 22349089 Fibulin-1 is down-regulated in atrial tissue from patients with atrial fibrillation, perhaps reflecting the myocardial structural changes that may have taken place during arrhythmia. PMID: 20451270 plasma levels of fibulin-1 could serve as a potential indicator to monitor kidney malfunction or kidney damage PMID: 21888404 Fibulin-1 accumulates in the arterial wall and in plasma of patients with type 2 diabetes, and appears to be a factor associated with arterial extracellular matrix changes in type 2 diabetes. PMID: 21926180 Promoter hypermethylation of FBLN1 was significantly associated with advanced stage hepatocellular carcinoma, multiple tumors and increased tumor size. PMID: 21268132 data collectively suggest fibulin-1C may be worthy of further investigation as a target for airway remodeling in asthma PMID: 20967215 Fibulin-1 protein was expressed in guinea pig sclera and cultured human scleral fibroblasts. PMID: 20405022 the pattern of fibulin-1 within human atherosclerotic lesions and the potential for fibulin-1, perhaps derived from the blood and acting in conjunction with fibrinogen, to play a role in the etiology and cardiovascular disease progression PMID: 19693531 Fibulin-1 has pronounced inhibitory effects on cell attachment and spreading promoted by fibronectin (FN) and suppresses the motility of a variety of cell types on FN substrates. PMID: 11792823 structural and functional characterization of promoter PMID: 11829738 FBLN1 disrupted by a t(12;22) translocation is associated with a complex type of synpolydactyly. PMID: 11836357 binding of HPV E6 protein to fibulin-1 PMID: 12200142 findings indicate that elevated expression and altered processing of fibulin-1 is associated with human breast cancer PMID: 12644824 The gene responsible for a unique vitreoretinal dystrophy is located on chromosome 22q13. PMID: 12912698 mutations in the splice acceptor site of fibulin-1 exon 19, but no MYH9 mutations,were found in family individuals affected by autosomal-dominant giant platelet syndromes associated with aberrant antisense gene regulation of the fibulin-1 gene. PMID: 14635206 FBLN seems to have an immunological and pathobiological role in breast neoplasm surveillance. PMID: 14691454 The preferential induction of the fibulin-1C variant, which is overexpressed in ovarian and breast cancer, might play an important role in estrogen-promoted carcinogenesis. PMID: 15528301 fiblin-1 is an important molecule that mediates progesterone action in human endometrial stromal cells differentiation towards implantation PMID: 15774544 fibulin-1 is a new regulator of ADAMTS-1-mediated proteoglycan proteolysis and may play an important role in proteoglycan turnover in tissues where there is overlapping expression PMID: 16061471 Coexpression of fibulin-1 with GROalpha abrogates key aspects of the transformed phenotype, including colonic tumor formation in a murine xenograft model. PMID: 17062666 degradation of basement membrane by cathepsin D liberates both fibulin-1 fragments and fibulin-5, which function to inhibit angiogenesis PMID: 18222970 FBLN1 was identified as a novel candidate tmour suppressor gene epigenetically downregulated in gastric cancer PMID: 18985039 Like tenascin-C, fibulin-1 inhibits fibroblast spreading and cell-mediated contraction of a fibrin-fibronectin matrix. PMID: 19109427 fibulin-1 and -2 respond differentially to single and repeated damaging noxae, and their expression is differently present in liver cells PMID: 19609566

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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.