Recombinant Human Four And A Half Lim Domains Protein 1 (FHL1) Protein (His)

Name: Recombinant Human Four And A Half Lim Domains Protein 1 (FHL1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01990P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Four And A Half Lim Domains Protein 1 (FHL1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q13642
Target Symbol	FHL1
Synonyms	Skeletal muscle LIM-protein 1 (SLIM) (SLIM-1)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	AEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRFTAVEDQYYCVDCYKNFVAKKCAGCKNPITGKRTVSRVSHPVSKARKPPVCHGKRLPLTLFPSANLRGRHPGGERTCPSWVVVLYRKNRSLAAPRGPGLVKAPVWWPMKDNPGTTTASTAKNAP
Expression Range	2-323aa
Protein Length	Full Length of Mature Protein
Mol. Weight	40.3 kDa
Research Area	Immunology
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	May have an involvement in muscle development or hypertrophy.
Subcellular Location	[Isoform 1]: Cytoplasm.; [Isoform 3]: Cytoplasm. Nucleus.; [Isoform 2]: Nucleus. Cytoplasm, cytosol. Note=Predominantly nuclear in myoblasts but is cytosolic in differentiated myotubes.
Database References	HGNC: 3702 OMIM: 300163 KEGG: hsa:2273 STRING: 9606.ENSP00000071281 UniGene: PMID: 28094252 FHL1 promote paclitaxel resistance in hepatocellular carcinomas cells through regulating apoptosis induced by paclitaxel, suggesting that FHL1 may be a promising molecular target for Hepatocellular carcinoma therapy. PMID: 30249901 Altogether, the specific localization of FHL1B and its modulation in disease-patient's myoblasts confirmed FHL1-related Emery-Dreifuss muscular dystrophy as a nuclear envelope disease. PMID: 27911330 Low FHL1 expression is associated with head and neck squamous cell carcinoma. PMID: 26908444 We have uncovered FHL1 as a novel potential regulator of calcium homeostasis in both fish and humans and have implicated it in isolated hypoparathyroidism. PMID: 28444561 Mutations in FHL1 cause unclassifiable cardiomyopathy with coexisting Emery-Dreifuss muscular dystrophy. PMID: 26857240 results provide evidence that FHL1A interacts with PLEKHG2 and regulates cell morphological change through the activity of PLEKHG2. PMID: 27765816 a novel FHL1 splice site variant results in the absence of FHL1A and the abundance of FHL1C, which may contribute to the complex and severe phenotype of Uruguay syndrome. PMID: 26933038 Knockdown of FHL1 with FHL1 small interfering RNA (siRNA) promoted tumor growth and Cyclin D and cyclin E were markedly elevated at both the protein and mRNA level. PMID: 26017856 results indicate that anti-FHL1 autoantibodies in peripheral blood have promising potential as a biomarker to identify a subset of severe IIM. PMID: 26551678 In healthy individuals, FHL1A is the predominant splice variant and is mainly found in skeletal and cardiac muscle. In two individuals with an Emery-Dreifuss plus phenotype with pulmonary artery hypoplasia and facial dysmorphology, there was demonstrated loss of isoform A and B, and an almost 200-fold overexpression of isoform C. PMID: 25724586 FRG1 mice overexpressing FHL1 showed an improvement in the dystrophic phenotype PMID: 25695429 FHL1 shRNA could significantly accelerate tumor cell growth via inhibiting the expression of FHL1 PMID: 26146054 Our results suggest that miR-410 may function as an oncomiR and are consistent with its key function in regulating FHL1 in certain digestive system cancers. PMID: 25272045 These data suggested that up-regulated FHL1 in smooth muscle in HSCR might be associated with intestinal wall remodeling in HSCR and might be one of the risk factors for gastrointestinal motor dysfunction PMID: 24516350 This is the first study to show that FHL1 mutations identified in several clinically distinct myopathies lead to similar protein aggregation and impair myotube formation. PMID: 24634512 The study has revealed that FHL1C overexpression induces Jurkat cell apoptosis. PMID: 24952875 FHL-1 is the predominant complement regulator in Bruch's membrane having direct implications for age-related macular degeneration. PMID: 25305316 Data indicate that four-and-a-half LIM domain 1 gene FHL1 mutation causing isolated hypertrophic cardiomyopathy with X-chromosomal inheritance. PMID: 24114807 Data show that loss of FHL1 function leads to myopathy in vivo and suggest that loss of function of FHL1 may be one of the mechanisms underlying muscle dystrophy in patients with FHL1 mutations. PMID: 23975679 mutation of FHL1 confers a complex phenotype through both gain- and loss-of-function mechanisms PMID: 23456229 This study demonistrated that the expand the morphologic features of reducing body myopathy , clearly demonstrate the localization of FHL1 in skeletal muscles. PMID: 23965743 FHL1 downregulation is associated with oral squamous cell carcinoma. PMID: 23123766 FHL1 is a methylation-silenced tumor-suppressor gene on chromosome X in gastrointestinal cancers, and that its silencing contributes to the formation of an epigenetic field for cancerization. PMID: 22689052 A mother, daughter, and son suffering from FHL1 myopathy have a mutation in the second LIM domain of fhl1 with musculoskeletal involvement. PMID: 22541254 C224W mutation of FHLi protein had slightly elevated pulmonary artery pressure PMID: 22923418 performed a clinical, muscle MRI, and histopathological characterization and immunoblot and genetic analysis of the FHL1 protein in a family with 4 individuals affected by reducing body myopathy. Identified a novel missense mutation in FHL1 PMID: 23169582 FHL1 is a novel disease gene for hypertrophic cardiomyopathy. PMID: 22523091 A novel mechanism involving four-and-a-half LIM domain protein-1 and extracellular signal-regulated kinase-2 regulates titin phosphorylation and mechanics. PMID: 22778266 The decrease in or loss of FHL1 expression may be related to the incidence, progression, invasiveness, and metastatic potential of gastric cancer. PMID: 22143536 reduced expression of FHL1 may play an important role in the development and progression of lung cancer. PMID: 21702045 FHL1-3 inhibit HIF-1 transcriptional activity and HIF-1alpha transactivation domain function by oxygen-independent mechanisms. PMID: 22219185 In order to substantiate a possible relation between K(v1.5) and FHL1C, a pull-down assay was performed. PMID: 22053194 FHL-1 may regulate estrogen receptor signaling function through regulation of AKT activation besides the physical and functional interaction with Estrogen receptor alpha. PMID: 22094188 FHL1 dystrophies are associated with myofibrillar myopathies pathology; mutations in the LIM2 domain are associated with reducing bodies composed of distinct tubulofilaments. PMID: 22094483 We report on three British families with a heterogeneous myopathy clinical presentation segregating a single FHL1 gene mutation and haplotype, suggesting that this represents a founder mutation. PMID: 21629301 This review will profile each of the FHL1, with a comprehensive analysis of mutations, a comparison of the clinical and histopathological features and will present several hypotheses for the possible disease mechanism(s)--{REVIEW} PMID: 21310615 FHL1 protein expression is downregulated in thoracic aortic dissection. PMID: 21126853 These results indicate that USP15 is involved in the regulation of hypertrophic responses in cardiac muscle through transcriptional and post-translational modulation of SLIM1. PMID: 21219870 FHL1B/PP2A(Cbeta) interaction may illustrate a novel cell-cycle regulatory pathway. PMID: 20969868 A novel missense mutation in the LIM2 domain of FHL1 co-segregated with X-linked scapuloperoneal myopathy in the family PMID: 20633900 Expression levels of FHL1 mRNA increased in all cell lines tested, as shown by RT-PCR. The methylation index of FHL1 in our samples was significantly higher in 70 BC specimens than in 10 normal bladder epithelium specimens. PMID: 20596604 This study reported a novel LIM2 domain mutation in FHL1 in a family with Reducing body myopathy with cytoplasmic bodies and spinal rigidity. PMID: 20571991 Our finding expands the phenotypic spectrum of the recently identified FHL1-associated myopathies and widens the differential diagnosis of Emery-Dreifuss-like syndromes. PMID: 20186852 SLIM1 may play an important role during the early stages of skeletal muscle differentiation, specifically in alpha5beta1-integrin-mediated signaling pathways PMID: 12917103 FHL1 is a novel regulator of myosin-binding protein C activity that may have a role in sarcomere assembly PMID: 16407297 Fasting insulin and insulin sensitivity index responses to exercise training were associated with DNA sequence variation in FHL1 in white men. PMID: 17589823 These results characterize TLX1 as a dual function regulator whose activity in respect to FHL1 is critically dependent upon its cellular concentration, as well as cell type and promoter context. PMID: 18073142 Study characterized a new disorder, X-linked myopathy with postural muscle atrophy (XMPMA), and identified FHL1 as the causative gene. PMID: 18179888 In a large Italian-American pedigree with dominant Scapuloperoneal syndrome all of the affected individuals have a missense change (c.365G-->C) in the FHL1 gene encoding FHL1. PMID: 18179901

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.