Recombinant Mouse Protein Flightless-1 Homolog (FLII) Protein (His-B2M)

Name: Recombinant Mouse Protein Flightless-1 Homolog (FLII) Protein (His-B2M)
Brand: Beta LifeScience
SKU: BLC-08601P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Fc receptors, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Protein Flightless-1 Homolog (FLII) Protein (His-B2M) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9JJ28
Target Symbol	FLII
Synonyms	Flii; Fli1; FliihProtein flightless-1 homolog
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-B2M
Target Protein Sequence	VGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVREEMGDESEEFLQVFDNDISYIEGGTASGFYTVEDTHYVTRMYRVYGKKNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKNERKGKAEITLLVQGQEPPGFWDVLGGEPSEIKNHVPDDFWPPQPKLYKVGLGLGYLELPQINYKLSVEHKKRPKVELMPGMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHRPRHTVVSRSLEGTE
Expression Range	495-827aa
Protein Length	Partial
Mol. Weight	52.0kDa
Research Area	Others
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 play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling. Essential for early embryonic development. May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation.
Subcellular Location	Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell junction, focal adhesion. Note=Colocalizes to actin-rich structures in blastocysts and, together with HRAS, RHOA and CDC42, in migrating fibroblasts. Localizes to centrosomes.
Database References	KEGG: mmu:14248 STRING: 10090.ENSMUSP00000002889 UniGene: Mm.339755
Tissue Specificity	Expressed in blastocyst.

Gene Functions References

Fluorescence resonance energy transfer experiments showed that FliI-NMMIIA interactions require Ca(2+) influx. We conclude that Ca(2+) influx through the TRPV4 channel regulates FliI-NMMIIA interaction, which in turn enables generation of the cell extensions essential for collagen remodeling PMID: 28526784
Flii genetic expression is enhances tissue regeneration, after claw amputation. PMID: 27595936
Studies suggest that Flii enhances cutaneous squamous cell carcinoma progression by decreasing apoptosis and enhancing tumor cell invasion. PMID: 26497552
P-Rex1 stimulates migration through enhancing the interaction between Rac1 and the actin-remodelling protein. PMID: 26887924
Genes downstream from Flii, including TGF-beta1 and TGF-beta3, showed significantly altered expression confirming a functional effect of the Rhodamine-Flii small interfering RNA on gene expression PMID: 25838352
FliI interacts with NMMIIA to promote cell extension formation, which enables collagen remodeling in fibroblasts. PMID: 25877872
FLII functions in PPARgamma activation as a molecular switch to repress transcriptional activity by interrupting formation of the PPARgamma/RXRalpha complex. PMID: 25479590
LRRFIP2 inhibits NLRP3 inflammasome activation by recruiting the caspase-1 inhibitor Flightless-I, thus outlining a new mechanism for negative regulation of NLRP3 inflammasome. PMID: 23942110
increasing the level of Flii in diabetic mouse wounds led to increased TLR4 and NF- kappa B production. Treatment of murine diabetic wounds with neutralising antibodies to Flii led to an improvement in healing with decreased expression of TLR4 PMID: 23555084
Using a mouse model of epidermolysis bullosa acquisita, the effect of "mopping up" Flii using Flii-neutralizing antibodies before, during, and after blister formation was determined. PMID: 23223144
Flii is constitutively secreted from macrophages and fibroblasts and is present in human plasma. PMID: 22718342
FliI regulates cell migration through its localization to focal adhesions and its ability to cap actin filaments, which collectively affect focal adhesion maturation. PMID: 22581781
Data show that mice with elevated Flii expression exhibit impaired wound healing. PMID: 21786402
Overexpression of Flii produced severe blistering post-induction of EBA, while decreased Flii reduced blister severity, elevated integrin expression, and improved ColVII production. PMID: 21984127
show that Flii modulation of focal adhesions and filamentous actin stress fibers is Rac1-dependent PMID: 21430700
Flii appears to have a positive role in the regeneration of hair follicles, contrary to its negative influence on wound healing in skin PMID: 21191408
performs an essential function in early embryonic development PMID: 11971982
Directly interferes with the formation of the TLR4-MyD88 signaling complex. PMID: 16424162
FliI is a contributing factor to impaired healing and strategies aimed at decreasing FliI levels in elderly skin may improve wound repair. PMID: 18191609
Flii may regulate wound repair through its effect on hemidesmosome formation and integrin-mediated cellular adhesion and migration. PMID: 19212345
These findings support the model that CISK phosphorylates FLII and activates nuclear receptor transcription and suggest a new cell survival signaling pathway mediated by PI 3-kinase and CISK. PMID: 19293151

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.