Analytical Data
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Gene name
PDGFAA
- Application
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Alternative Names
PDGFAA；LOC103909601；pdgfa；pdgfa-2；Platelet-derived growth factor subunit A
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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
P04085
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Expression Region
87-211aa
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AA Sequence
SIEE AVPAVCKTRT VIYEIPRSQV DPTSANFLIW PPCVEVKRCT GCCNTSSVKC QPSRVHHRSV KVAKVEYVRK KPKLKEVQVR LEEHLECACA TTSLNPDYRE EDTGRPRESG KKRKRKRLKP T
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Molecular Weight
24 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
PDGFAA, or Platelet-Derived Growth Factor-AA, is a crucial protein involved in various biological processes such as cell proliferation, migration, and differentiation, making it significant in the fields of developmental biology and regenerative medicine. The study of PDGFAA has garnered attention due to its implications in wound healing, tissue repair, and its potential role in pathological conditions like cancer and fibrotic diseases. Research has demonstrated that PDGFAA can modulate cellular responses by interacting with its receptors, activating several intracellular signaling pathways that contribute to tissue homeostasis. The reconstitution of PDGFAA as a recombinant protein offers an invaluable tool for investigating its biological properties and understanding its functional dynamics in vitro and in vivo. This recombinant approach allows for the generation of pure PDGFAA, facilitating detailed mechanistic studies and the evaluation of its therapeutic potential. Moreover, the development of PDGFAA-based therapies aims to harness its regenerative capabilities, paving the way for novel treatments in conditions characterized by impaired healing or abnormal cell proliferation. As our understanding of PDGFAA's multifaceted roles in various physiological and pathological contexts expands, the ongoing research in recombinant protein production, characterization, and application remains critical for both basic scientific inquiry and the advancement of targeted therapeutic strategies. This foundation sets the stage for future innovations in biomedicine, emphasizing the importance of PDGFAA in not only cellular biology but also in the development of effective clinical applications.
