Analytical Data
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Gene name
dLK1
- Application
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Alternative Names
dLK1；DLK；Protein delta homolog 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
P80370
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Expression Region
24-297aa
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AA Sequence
AECFPACNPQNGFCEDDNVCRCQPGWQGPLCDQCVTSPGCLHGLCGEPGQ CICTDGWDGELCDRDVRACSSAPCANNGTCVSLDDGLYECSCAPGYSGKD CQKKDGPCVINGSPCQHGGTCVDDEGRASHASCLCPPGFSGNFCEIVANS CTPNPCENDGVCTDIGGDFRCRCPAGFIDKTCSRPVTNCASSPCQNGGTC LQHTQVSYECLCKPEFTGLTCVKKRALSPQQVTRLPNGYGLAYRLTPGVH ELPVQQPEHRILKVSMKELNKKTPVDHHHHHH
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Molecular Weight
30 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
dLK1, a member of the leukemia inhibitory factor (LIF) family, has garnered significant interest in the field of molecular biology due to its role in various cellular processes, including cell proliferation, differentiation, and survival. Emerging research suggests that dLK1 plays a critical role in the maintenance of pluripotency in stem cells and has potential therapeutic implications in regenerative medicine and cancer treatment. The recombinant expression of dLK1 protein allows for the exploration of its biological functions and mechanisms of action in a controlled environment. Understanding the structure-function relationship of dLK1 can provide insights into its signaling pathways and interactions with other molecules. Moreover, recombinant dLK1 has the potential to be utilized in drug discovery and the development of novel therapeutic strategies. As the demand for innovative treatments increases, investigating dLK1's properties could pave the way for breakthroughs in tackling various diseases, including cancers and degenerative conditions. Thus, the study of dLK1 recombinant protein is positioned at the intersection of fundamental biology and applied biomedical research, making it a valuable target for future studies.
