Recombinant Human Filamin-A (FLNA) Protein (His&Myc)

Name: Recombinant Human Filamin-A (FLNA) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-05163P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Filamin-A (FLNA) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P21333
Target Symbol	FLNA
Synonyms	ABP 280 ; ABP-280; Actin-binding protein 280; Alpha filamin; Alpha-filamin; APBX; CSBS; CVD1; Endothelial actin binding protein; Endothelial actin-binding protein; Filamin 1; Filamin A alpha; Filamin A; Filamin-1; Filamin-A; FLN; FLN-A; FLN1; FLNA; FLNA_HUMAN; FMD; MNS; NHBP; Non muscle filamin ; Non-muscle filamin; OPD; OPD1; OPD2; XLVD; XMVD
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	SSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAP
Expression Range	2-274aa
Protein Length	Partial
Mol. Weight	38.0 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.
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	Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking. Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance. During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons.
Subcellular Location	Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Perikaryon. Cell projection, growth cone.
Protein Families	Filamin family
Database References	HGNC: 3754 OMIM: 300017 KEGG: hsa:2316 STRING: 9606.ENSP00000358866 UniGene: PMID: 29146485 silencing filamin A may inhibit the invasion and migration of breast cancer cells by upregulating 14-3-3sigma. PMID: 30074213 FLNA overexpression suppressed the proliferation of Bladder Carcinoma cells, blocked cell cycle and promoted apoptosis of Bladder Carcinoma cell. PMID: 29288417 Silencing filamin A (FLNa) expression in lung cancer cell line A549 cells promoted proliferation, migration, and invasiveness of A549 cells by enhancing the activation of epidermal growth factor receptor and ERK signaling pathway. PMID: 29272322 Reduced RNA editing of FLNA gene is associated with psoriasis. PMID: 29592874 Data indicate mutations in FLNA (Filamin A) associated with Ebstein anomaly. PMID: 29237676 these observations describe a new mechanism of tissue-specific regulation of FLNA that could reflect the differing mechanical requirements of these cell types during development. PMID: 29024177 This study also indicates that FLNA may affect white matter integrity in patients with periventricular nodular heterotopia related epilepsy. PMID: 29062687 The mutations of the FLNA gene were observed in 7 (30.4%) of the 23 patients who with Sporadic periventricular nodular heterotopia. PMID: 28411558 Data show that AR-deficient and highly metastatic prostate cancer cell lines express higher levels of filamin A compared to normal prostate epithelial cells and AR-positive and less metastatic prostate cancer. Also, the results identified that Cao2+ via CaR-mediated signaling induces filamin A cleavage and promotes the migration in AR-deficient and highly metastatic prostate cancer cells. PMID: 27206800 FLNA is downregulated in parathyroid tumors and parallels the CASR expression levels. Loss of FLNA reduces CASR mRNA and protein expression levels and the CASR-induced ERK phosphorylation. FLNA is involved in receptor expression, membrane localization and ERK signaling activation of both 990R and 990G CASR variants. PMID: 27872158 We report two brothers carrying a loss-of-function mutation of FNLA with gonadal differentiation disorder and hypospadias. Specific staining for AR shows almost an absolute absence of these receptors in the testicular tissue. PMID: 28432720 Lowering the FLNA level elevated RalA activity and resulted in selective interference with the normal intracellular trafficking and signaling of the D2R and D3R, through GRK2 and beta-arrestins, respectively. FLNA is a multi-functional protein that acts as a platform on which D2R and D3R can interact with various proteins causing selective regulation of these receptors occurs in combination with GRK2 and beta-arrestins. PMID: 27188791 FLNA upregulation correlates with Snail-induced epithelial to mesenchymal transition in colorectal carcinoma. PMID: 28778796 Our findings expand the male-specific phenotype of FLNA mutations that now includes classical-like EDS with lethal cardiac valvular dystrophy, and offer further insights for the genotype-phenotype correlations within this spectrum. PMID: 27739212 Study identifies ANXA4 and FLNA as up-regulated in buccal squamous cell carcinoma arising from oral submucous fibrosis. PMID: 27485544 These results provide new insights into the regulation of SK2 channel trafficking by the cytoskeletal proteins FLNA and alpha-actinin2, involving distinct recycling pathways PMID: 27779751 Respiratory failure secondary to progressive obstructive lung disease during infancy may be the presenting phenotype of FLNA-associated periventricular nodular heterotopia. PMID: 28457522 The actin regulator FLNA interacts with the endoplasmic reticulum stress kinase PERK and this interaction is required for the efficient formation of ER-plasma membrane contact sites. PMID: 28238652 CCR2B and beta2AR signals to FLNa to stimulate its endocytosis and recycling to the plasma membrane. PMID: 27909248 In humans, mutations in the actin-binding protein Filamin-C result in myopathies, but the underlying molecular function is not well understood. Here we show using Drosophila indirect flight muscle that the filamin ortholog Cheerio in conjunction with the giant elastic protein titin plays a crucial role in keeping thin filaments stably anchored at the Z-disc PMID: 28732005 Case Report: Reduced binding of mutant FLNa to beta3 and the facilitated recruitment of talin by beta3 on platelet stimulation, explaining the increased alphaIIbbeta3 activation and the ensuing gain-of-platelet functions. PMID: 28428218 results reveal an unusual structural and thermodynamic basis for the P2204L-induced dysfunction of filamin and frontometaphyseal dysplasia disease. PMID: 28348077 Mechanistic analysis revealed that FLNA suppresses pol III gene transcription by confining the recruitment of the RNA pol III transcription machinery at the promoters of the genes that are sensitive to the alteration of FLNA expression. PMID: 27738102 FlnA more strongly binds RhoA, although both filamins overlap with RhoA expression in the cell cytoplasm. FlnA promotes RhoA activation whereas FlnB indirectly inhibits this pathway. Moreover, FlnA loss leads to diminished expression of b1-integrin, whereas FlnB loss promotes integrin expression PMID: 28175289 FLNA can function as a modulator of chemosensitivity to docetaxel in triple-negative breast cancer (TNBC) cells through regulation of the MAPK/ERK pathway both in vitro and in vivo. FLNA may serve as a novel therapeutic target for improvement of chemotherapy efficacy in TNBC. PMID: 26546439 Results indicate that mTORC2 regulates filamin A-dependent focal adhesions and cell migration. PMID: 27059097 The syndrome affecting the family shares phenotypic overlap with other syndromes caused by FLNA mutations, but appears to be a distinct phenotype, likely representing a unique genetic syndrome. PMID: 26804200 The findings in these cases are distinct from previously described FLNA related disorders by virtue of decreased joint mobility and spontaneous keloid scarring. They occur in association with a novel mutation and represent a novel genetic syndrome. PMID: 26686323 FLNA gene mutation analysis was performed in a series of 10 fetuses and a neonatally deceased newborn displaying a multiple congenital anomalies syndrome suggestive of otopalatodigital spectrum disorders. PMID: 26404489 This study expands the diversity of the phenotypes associated with loss-of-function mutations in FLNA. PMID: 26059841 Filamin-A is required to mediate SSTR2 effects in pancreatic neuroendocrine tumours PMID: 26733502 The function of different integrins is subjected to differential regulation by FLNa. PMID: 26572583 FLNA functions as a positive cellular transducer linking actin polymerization to MKL1-SRF activity, counteracting the known repressive complex of MKL1 and monomeric G-actin. PMID: 26554816 Missense substitutions in FLNA were identified in four unrelated craniosynostosis patients. PMID: 25873011 studies suggest that Vpu hijacks the FLNa function in the modulation of tetherin to neutralize the antiviral factor tetherin. PMID: 26742839 Our interpretation of these contradictions is that truncation and/or mutation of RhoGDI2 perturbs its conformation to expose a site that adventitiously binds FLNA and is not a bona-fide interaction. PMID: 26707877 Extracellular sphingosine-1-phosphate activates NF-kappaB only in melanoma cells that lack FLNA. PMID: 26552704 FLNA anchors PC2 to the actin cytoskeleton through complex PC2-FLNA-actin to reduce degradation and increase stability, and possibly regulate PC2 function in a Ca-dependent manner. PMID: 25861040 These observations imply that other interactions apart from those mediated by the canonical repeat 24 dimerisation interface contribute to FLNA homodimerization and that mutations affecting this region of the protein can have broad phenotypic effects. PMID: 25686753 Our results support FLNA as a new downstream effector of mTORC2 controlling GBM cell motility. PMID: 26134617 Familial periventricular nodular heterotopia, epilepsy and Melnick-Needles Syndrome caused by a single FLNA mutation with combined gain-of-function and loss-of-function effects PMID: 25755106 The data suggest a molecular mechanism for direct G protein-coupled receptors -cytoskeleton coupling via filamin A. PMID: 26460884 Frontometaphyseal dysplasia and keloid formation without normally present in this condition FLNA mutations have been described in six unrelated children patients. PMID: 25899317 FLNA analysis was performed by DHPLC followed by Sanger sequencing [Robertson et al., 2006]. Both sisters were heterozygous for a novel mutation, c.6611C>T in exon 41, that predicts the substitution p.Pro2204Leu within filamin repeat 20 PMID: 25820619 FLNa showed low expression in colorectal adenocarcinoma, high correlation with the incidence and development of colorectal cancer, and was considered an indicator of prognosis. PMID: 25717257 The androgen-triggered AR/filamin A complex controls, through Rac 1, the decision of cells to halt cell cycle and migration. PMID: 25476896 Virus infection and RNase L activation disrupt its association with Filamin A and release RNase L to mediate its canonical nuclease-dependent antiviral activities. PMID: 25352621 Autoinhibited filamin is refractory to phosphorylation by PKA on a known Ser(2152) site despite its consensus motif being exposed and the corresponding isolated peptide being readily phosphorylated. PMID: 25666618 this study proposes that FLNA interaction with ICL3(intracellular loop) is central for endocytosis and signaling of WT and WHIM-like CXCR4 receptors. PMID: 25355818

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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.

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