Analytical Data
-
Gene name
PL6
- Application
-
Alternative Names
TMEM115; PL6; LUCA11.2; Transmembrane protein 115; Placental protein 6; Protein PL6
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q12893
-
Expression Region
1-351 aa
-
AA Sequence
MQRALPGARQHLGAILASASVVVKALCAAVLFLYLLSFAVDTGCLAVTPGYLFPPNFWIWTLATHGLMEQHVWDVAISLTTVVVAGRLLEPLWGALELLIFFSVVNVSVGLLGAFAYLLTYMASFNLVYLFTVRIHGALGFLGGVLVALKQTMGDCVVLRVPQVRVSVMPMLLLALLLLLRLATLLQSPALASYGFGLLSSWVYLRFYQRHSRGRGDMADHFAFATFFPEILQPVVGLLANLVHSLLVKVKICQKTVKRYDVGAPSSITISLPGTDPQDAERRRQLALKALNERLKRVEDQSIWPSMDDDEEESGAKVDSPLPSDKAPTPPGKGAAPESSLITFEAAPPTL
-
Molecular Weight
64.35 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Research on PL6 recombinant protein has gained significant attention due to its potential applications in biotechnology and medicine. PL6, a member of the lectin family, is known for its carbohydrate-binding properties, which can have critical implications in various biological processes, including cell-cell interactions and immune responses. Understanding the structure and function of PL6 is essential for elucidating its role in physiological and pathological conditions, such as cancer and inflammation. Recombinant protein technology has enabled scientists to produce PL6 in a controlled environment, allowing for extensive biochemical analyses and functional assays. The ability to generate large quantities of pure PL6 facilitates its use in therapeutic development, diagnostics, and as a research tool for studying glycan-mediated cellular pathways. Moreover, PL6's unique binding affinity may provide novel strategies for targeted drug delivery or as a biomarker in disease diagnostics. The investigation of PL6 thus merges fundamental research with practical applications, aiming to unlock its full potential in enhancing human health and understanding cellular mechanisms.











