Analytical Data
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Gene name
FHL1
- Application
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Alternative Names
FHL1；SLIM1；Four and a half LIM domains 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
Q13642
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Expression Region
1-280aa
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AA Sequence
MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGAD SKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPK CKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYC VTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRF TAVEDQYYCVDCYKNFVAKKCAGCKNPITGFGKGSSVVAYEGQSWHDYCF HCKKCSVNLANKRFVFHQEQVYCPDCAKKL
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Molecular Weight
57 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
Related Products
Protein Description
FHL1 (four and a half LIM domains protein 1) is a member of the LIM domain protein family, which is known for its role in various cellular processes, including muscle development, cell signaling, and gene transcription. Initial studies have shown that FHL1 is expressed in multiple tissues, particularly in skeletal muscle and cardiac tissue, suggesting its significant role in muscle-related functions. Research has indicated that FHL1 may be involved in regulating skeletal muscle hypertrophy and play a part in muscle degeneration diseases. Additionally, the dysregulation of FHL1 has been linked to several pathological conditions, including cardiomyopathy and muscular dystrophies. Efforts to produce recombinant FHL1 proteins have been undertaken to elucidate its molecular mechanisms and interactions at a biochemical level, as well as to explore its potential as a therapeutic target. The generation of these recombinant proteins allows researchers to investigate the structure-function relationships of FHL1, understand how it interacts with other proteins and cellular components, and assess its impact on cellular pathways. Furthermore, recombinant FHL1 can be utilized in high-throughput screening for small molecules or compounds that could modulate its function, opening avenues for the development of novel therapeutic strategies for muscle-related disorders. Given the complexities of muscle biology and the potential implications of FHL1 in muscular diseases, ongoing studies are critical to unravel its precise roles and therapeutic potential in both health and disease.
