Analytical Data
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Gene name
LDB1
- Application
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Alternative Names
CLIM2; NLI; Carboxy Terminal LIM Domain Protein 2; LIM domain-binding factor CLIM2; Nuclear LIM interactor
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86U70
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Expression Region
Asp112~Gln411
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Molecular Weight
43kDa
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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
LDB1 (LIM domain-binding protein 1) is a crucial transcriptional co-regulator that plays an essential role in various developmental processes and cellular functions, particularly in hematopoiesis and neural differentiation. Its primary function is to modulate gene expression by forming complexes with various DNA-binding transcription factors, enabling the precise regulation of target genes. Research into LDB1 has gained traction due to its implications in developmental disorders and cancers, where its dysregulation may contribute to abnormal cell differentiation and proliferation. Understanding the structural and functional dynamics of LDB1 through recombinant protein studies can provide insights into its mechanistic roles in transcriptional regulation. By expressing LDB1 as a recombinant protein, researchers can elucidate its interacting partners, target genes, and regulatory pathways. This research is further enhanced by employing advanced techniques such as cryo-electron microscopy and mass spectrometry, which allow for detailed analysis of protein complexes. Overall, the study of LDB1 and its recombinant forms represents a promising avenue for uncovering the complexities of gene regulation and its implications in health and disease.
