Analytical Data
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Gene name
SYF2
- Application
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Alternative Names
CBPIN; CCNDBP1 interactor; CCNDBP1-interactor; DKFZp564O2082; fSAP29; Functional spliceosome associated protein 29; GCIP interacting protein p29; GCIPIP; NTC31; P29; Pre mRNA splicing factor SYF2; Pre-mRNA-splicing factor syf2; syf2; SYF2 homolog; SYF2 homolog RNA splicing factor (S. cerevisiae); SYF2 homolog RNA splicing factor; SYF2_HUMAN
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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
O95926
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Expression Region
2-243 aa
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AA Sequence
AAIAASEVL VDSAEEGSLA AAAELAAQKR EQRLRKFREL HLMRNEARKL NHQEVVEEDK RLKLPANWEA KKARLEWELK EEEKKKECAA RGEDYEKVKL LEISAEDAER WERKKKRKNP DLGFSDYAAA QLRQYHRLTK QIKPDMETYE RLREKHGEEF FPTSNSLLHG THVPSTEEID RMVIDLEKQI EKRDKYSRRR PYNDDADIDY INERNAKFNK KAERFYGKYT AEIKQNLERG TAV
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Molecular Weight
28.7 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
SYF2 protein, a member of the splicing factor family, plays a significant role in the regulation of RNA splicing and cellular gene expression. Its involvement in essential biological processes has garnered attention in recent years, particularly concerning its implications in various diseases, including cancer. Research has shown that alterations in the expression and function of splicing factors like SYF2 can lead to aberrant splicing patterns, resulting in the production of dysfunctional proteins that contribute to tumorigenesis and other pathological conditions. Understanding the structure and function of SYF2 at the molecular level is crucial for elucidating its role in splicing regulation and cellular homeostasis. Recent advancements in recombinant protein technology have enabled the production and characterization of SYF2, facilitating in-depth studies of its biochemical properties and interaction with other splicing components. This research not only enhances our understanding of splicing mechanisms but also opens avenues for therapeutic interventions targeting splicing dysregulation in diseases where SYF2 is implicated. Thus, the study of SYF2 recombinant protein is pivotal for both basic biological research and potential clinical applications, highlighting its importance in the field of molecular biology and medicine.
