Analytical Data
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Gene name
RALYL
- Application
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Alternative Names
RALYL; HNRPCL3; RNA-binding Raly-like protein; hRALYL; Heterogeneous nuclear ribonucleoprotein C-like 3; hnRNP core protein C-like 3
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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
Q86SE5
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Expression Region
1-291 aa
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AA Sequence
MTGKTQTSNV TNKNDPKSIN SRVFIGNLNT AIVKKVDIEA IFSKYGKIVG CSVHKGYAFV QYMSERHARA AVAGENARVI AGQPLDINMA GEPKPYRPKP GNKRPLSALY RLESKEPFLS VGGYVFDYDY YRDDFYNRLF DYHGRVPPPP RAVIPLKRPR VAVTTTRRGK GVFSMKGGSR STASGSTGSK LKSDELQTIK KELTQIKTKI DSLLGRLEKI EKQQKAEAEA QKKQLEESLV LIQEECVSEI ADHSTEEPAE GGPDADGEEM TDGIEEDFDE DGGHELFLQI K
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Molecular Weight
32.3 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
RALYL (Ras-like protein Y) is a member of the RAS superfamily of small GTPases, which play crucial roles in various cellular processes, including cell proliferation, differentiation, and survival. Research into RALYL has gained traction due to its involvement in cancer biology and pathological conditions, where aberrant signaling pathways often lead to uncontrolled cell growth. Unlike other RAS family members, RALYL has been less studied, yet emerging evidence suggests that it might regulate key pathways that contribute to malignancies. The understanding of RALYL’s function is critical as it may serve as a potential biomarker for certain tumors or as a therapeutic target. Researchers are focusing on the structural characterization of RALYL and its interaction with other cellular proteins to elucidate its exact roles and mechanisms in cancer development. By employing recombinant protein techniques, scientists aim to produce RALYL in a controlled environment, allowing for detailed functional assays and studies on its GTP-binding and hydrolysis activities. This research is essential for uncovering the therapeutic potential of targeting RALYL in cancer treatment and other diseases associated with its dysregulation. As the investigation into RALYL continues to evolve, it promises to enhance our understanding of the intricate networks that govern cell behavior and disease progression, paving the way for novel approaches in precision medicine.
