Analytical Data
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Gene name
FBLIM1
- Application
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Alternative Names
FBLIM1；FBLP1;Filamin-binding LIM Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WUP2
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Expression Region
1-373aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMASKPEKRVASSVFITLAPPRRDVAVA EEVRQAVCEARRGRPWEAPAPMKTPEAGLAGRPSPWTTPGRAAATVPAAP MQLFNGGCPPPPPVLDGEDVLPDLDLLPPPPPPPPVLLPSEEEAPAPMGA SLIADLEQLHLSPPPPPPQAPAEGPSVQPGPLRPMEEELPPPPAEPVEKG ASTDICAFCHKTVSPRELAVEAMKRQYHAQCFTCRTCRRQLAGQSFYQKD GRPLCEPCYQDTLERCGKCGEVVRDHIIRALGQAFHPSCFTCVTCARCIG DESFALGSQNEVYCLDDFYRKFAPVCSICENPIIPRDGKDAFKIECMGRN FHENCYRCEDCRILLSVEPTDQGCYPLNNHLFCKPCHVKRSAAGCC
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Molecular Weight
43 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
FBLIM1, or F-actin binding LIM protein 1, is a multi-functional protein primarily known for its role in cell adhesion, migration, and signal transduction. It is characterized by its LIM domains, which facilitate protein-protein interactions and link cytoskeletal elements to cell signaling pathways. Research has increasingly focused on the role of FBLIM1 in various cellular processes, including its implications in cancer progression, fibrosis, and muscle differentiation. Alterations in FBLIM1 expression and function have been associated with several pathological conditions, suggesting its potential as a biomarker or therapeutic target. Investigating the structure and function of recombinant FBLIM1 protein is crucial for understanding its specific molecular mechanisms. The recombinant protein can be used to elucidate the interactions with other cellular components, assess its role in actin organization, and explore its involvement in disease states. By employing techniques such as co-immunoprecipitation and cell-based assays, researchers aim to clarify the contributions of FBLIM1 to cellular dynamics and its potential regulation by extracellular stimuli. The insights gained from studying FBLIM1 not only enrich our understanding of cellular biology but also pave the way for the development of novel interventions in diseases characterized by dysregulated cellular behavior.
