Analytical Data
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Gene name
LAD1
- Application
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Alternative Names
LAD1；LAD；Ladinin-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
O00515
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Expression Region
418-517aa
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AA Sequence
SESVKSRGLPCTELFVAPVGVASKRHLFEKELAGQSRAEPASSRKENLRL SGVVTSRLNLWISRTQESGDQDPQEAQKASSATERTQWGQKSDSSLDAEV
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Molecular Weight
37 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
LAD1 (Laminin Alpha-1 chain) is a crucial component of the extracellular matrix, playing a vital role in cell adhesion, migration, and tissue development. Its significance has garnered attention in various fields, including developmental biology, cancer research, and regenerative medicine. LAD1 has been implicated in the integrity of the basement membrane, which supports tissue architecture and influences cellular behavior. Abnormalities in LAD1 expression have been linked to several pathological conditions, including cancer metastasis and genetic disorders affecting skin and muscle integrity. Researchers are particularly interested in LAD1 recombinant proteins due to their potential therapeutic applications, such as in tissue engineering and wound healing. The ability to produce LAD1 as a recombinant protein allows for detailed studies on its structure-function relationships and mechanisms of action. Furthermore, investigating LAD1 interactions with other extracellular matrix components may reveal insights into its role in cellular signaling pathways. Overall, the study of LAD1 recombinant proteins provides valuable insights into fundamental biological processes, with implications for developing novel therapeutic strategies aimed at modulating tissue repair and addressing diseases linked to extracellular matrix dysfunction.
