Analytical Data
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Gene name
PLIN
- Application
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Alternative Names
Perilipin-1. Lipid droplet-associated protein
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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
O60240
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Expression Region
101-208 aa
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AA Sequence
KIPALQYPPEKIASELKDTISTRLRSARNSISVPIASTSDKVLGAALAGCELAWGVARDTAEFAANTRAGRLASGGADLALGSIEKVVEYLLPADKEESAPAPGHQQA
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Molecular Weight
37.62 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
PLIN (Perilipin) proteins are a family of lipid droplet-associated proteins that play crucial roles in regulating lipid metabolism, particularly in adipocytes and other lipid-storing cells. Research on PLIN proteins has gained momentum due to their involvement in obesity, insulin resistance, and metabolic disorders. The PLIN family consists of several members, including PLIN1, PLIN2, PLIN3, PLIN4, and PLIN5, each exhibiting distinct regulatory functions in lipid storage and mobilization. PLIN1, for instance, is predominantly expressed in adipose tissues and is integral to lipolysis regulation, while PLIN2 is widely distributed in various tissues and serves as a protective factor against lipotoxicity. Investigating the structure and function of PLIN proteins, particularly through recombinant technology, has facilitated a deeper understanding of their roles in cellular lipid dynamics. Recombinant PLIN proteins enable researchers to explore their interactions with other cellular components, such as enzymes involved in lipid metabolism, and to elucidate the mechanisms underlying their regulatory functions. This has significant implications for developing therapeutic strategies targeting metabolic diseases. Current studies also focus on the post-translational modifications and signaling pathways associated with PLIN proteins, which are critical for understanding their actions in health and disease. Overall, the study of PLIN recombinant proteins represents a promising avenue for advancing our knowledge of lipid biology and its connections to various health conditions, paving the way for innovative treatments against obesity and related metabolic disorders.
