Analytical Data
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Gene name
Podoplanin
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简介
The Podoplanin protein is a multifaceted regulator that affects cell migration and adhesion through multiple interactions. In hemo-lymphatic dissociation, Podoplanin binds to CLEC1B, triggering platelet activation that is counteracted by the CD9 interaction. Podoplanin Protein, Human (HEK293, His-Fc) is the recombinant human-derived Podoplanin protein, expressed by HEK293 , with C-hFc, C-His labeled tag.
- Application
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Alternative Names
Podoplanin; Aggrus; Glycoprotein 36; Gp36; T1-Alpha; T1A; PDPN; GP36
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Species
Human
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Source
HEK293
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Tag
C-hFc;C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86YL7-1
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Expression Region
A23-K123
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Protein Length
Partial
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Molecular Weight
50.2 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
Podoplanin, a glycoprotein primarily expressed in lymphatic endothelial cells, plays a critical role in various physiological and pathological processes, including lymphangiogenesis, tissue repair, and tumor progression. Its ability to enhance cell migration, support lymphatic vessel formation, and interact with the platelet aggregation mechanism has garnered significant research interest, particularly in cancer biology and immunology. In the context of tumor microenvironments, podoplanin is often upregulated in various malignancies, correlating with aggressive tumor behavior and poor patient prognosis. Furthermore, it serves as a potential biomarker for certain types of cancers, prompting investigations into its therapeutic targeting. The development of recombinant podoplanin proteins has emerged as a vital tool for studying its biological functions, interactions, and potential as a drug target. Researchers utilize these recombinant proteins to elucidate the signaling pathways mediated by podoplanin and to explore its roles in immune escape and tumor metastasis. The insights gained from such studies could pave the way for novel therapeutic strategies aimed at restricting tumor growth and improving clinical outcomes for patients with podoplanin-positive malignancies. As such, the ongoing research into podoplanin and its recombinant forms holds promise not only for advancing our understanding of cancer biology but also for fostering innovation in targeted therapies and diagnostics.
