Analytical Data
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Gene name
PDGF R alpha
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简介
TRF1 protein is a telomere-binding protein that plays a crucial role in telomere maintenance and chromosome stability. It is involved in regulating telomere length and preventing DNA damage. PDGF R beta Protein, Human (Biotinylated, HEK293, His) is the recombinant human-derived PDGF R beta protein, expressed by HEK293 , with C-His labeled tag.
- Application
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Alternative Names
Platelet-derived growth factor receptor beta; PDGF-R-beta; PDGFR-1; CD140b; PDGFRB
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Species
Human
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
NP_002600.1
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Expression Region
L33-K531
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Molecular Weight
57.6 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
Platelet-Derived Growth Factor Receptor Alpha (PDGFR-α) is a receptor tyrosine kinase that plays a pivotal role in cellular processes such as proliferation, survival, and migration, particularly in mesenchymal cells. Its activation by platelet-derived growth factors is essential for normal physiological processes, including wound healing and tissue repair. However, aberrant PDGFR-α signaling has been implicated in various pathological conditions, including fibrosis, atherosclerosis, and various types of cancer, prompting significant interest in this receptor as a therapeutic target. The generation of recombinant PDGFR-α proteins has allowed researchers to study the structure-function relationships of the receptor, investigate its signaling pathways, and develop potential inhibitors. This recombinant protein serves as a valuable tool in elucidating the molecular mechanisms underlying PDGFR-α function and its contributions to disease pathogenesis. Moreover, understanding the interactions between PDGFR-α and its ligands at the molecular level may provide insights into the development of novel therapeutic strategies to combat diseases associated with dysregulated PDGFR-α activity. Thus, ongoing research on PDGFR-α recombinant proteins is vital to advancing our knowledge of its biological significance and therapeutic potential.
