Analytical Data
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Gene name
YES1
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简介
YES1 is a non-receptor protein tyrosine kinase that regulates processes such as cell growth, survival, apoptosis, and cell-cell adhesion. It is activated by RTKs (EGFR, PDGFR, CSF1R, FGFR) to phosphorylate downstream substrates. YES1 Protein, Human (sf9, His-GST) is the recombinant human-derived YES1 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.
- Application
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Alternative Names
Tyrosine-protein kinase Yes; p61-Yes; YES1; YES
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Species
Human
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Source
Baculovirus
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Tag
N-His;N-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07947
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Expression Region
G2-L543
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Protein Length
Full Length of Mature Protein
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Molecular Weight
75 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
YES1, a member of the SRC family of protein tyrosine kinases, plays a crucial role in various cellular processes, including cell proliferation, differentiation, and survival. Its dysregulation has been implicated in several types of cancers, making it a significant target for therapeutic interventions. Recent studies have focused on understanding the structure and function of YES1, as well as its signaling pathways and interactions with other cellular proteins. The reconstitution of YES1 into recombinant proteins allows researchers to investigate its activity in a controlled environment, facilitating insights into its biological mechanisms and potential as a drug target. Furthermore, the development of YES1 inhibitors could lead to novel cancer therapies aimed at restoring normal cellular functions in tumors with YES1 overexpression or aberrant signaling. As our understanding of YES1 expands, it continues to emerge as an important player in oncogenic signaling networks, emphasizing the need for ongoing research into its roles in health and disease.
