Analytical Data
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Gene name
FHL5
- Application
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Alternative Names
Activator of cAMP responsive element modulator (CREM) in testis; Activator of cAMP-responsive element modulator in testis; Activator of CREM in testis; FHL-5; Fhl5; FHL5 protein; FHL5_HUMAN; Four and a half LIM domains protein 5
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5TD97
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Expression Region
1-284aa
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AA Sequence
MTTAHFYCQYCTASLLGKKYVLKDDSPYCVTCYDRVFSNYCEECKKPIESDSKDLCYKDRHWHEGCFKCTKCNHSLVEKPFAAKDERLLCTECYSNECSSKCFHCKRTIMPGSRKMEFKGNYWHETCFVCENCRQPIGTKPLISKESGNYCVPCFEKEFAHYCNFCKKVITSGGITFCDQLWHKECFLCSDCRKDLCEEQFMSRDDYPFCMDCYNHLYANKCVACSKPISGLTGAKFICFQDSQWHSECFNCGKCSVSLVGKGFLTQNKEIFCQKCGSGMDTDI
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Molecular Weight
56.98 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
FHL5 (Four-and-a-Half LIM domains protein 5) is a member of the FHL family of proteins, characterized by the presence of multiple LIM domains that are implicated in various cellular processes, including transcription regulation, cell signaling, and cytoskeletal organization. Research has increasingly focused on FHL5 due to its significant roles in cardiovascular health and development. Studies have shown that FHL5 is involved in heart muscle function, influencing myocyte development and cardiac hypertrophy. Additionally, aberrant expression of FHL5 has been linked to several diseases, including heart diseases and certain cancers, highlighting its potential as a biomarker or therapeutic target. The ability of FHL5 to interact with other proteins and influence transcriptional activity positions it as a critical player in signaling pathways that control cell fate and differentiation. Thus, the recombination and characterization of FHL5 as a recombinant protein is fundamental for understanding its functional mechanisms and biological significance, facilitating the exploration of its role in health and disease. Through advanced techniques such as protein purification and functional assays, researchers seek to elucidate the molecular interactions and pathways involving FHL5, paving the way for potential clinical applications in regenerative medicine and targeted therapies. Overall, studying FHL5 in its recombinant form provides valuable insights into its structure-function relationships and contributes to the broader understanding of LIM domain proteins in cellular biology.
