Analytical Data
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Gene name
Bcl-XL
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简介
Bcl-XL protein forms heterodimers with BAX, BAK, or BCL2, but its antiapoptotic activity does not require heterodimerization with BAX. Bcl-XL Protein, Mouse (His) is the recombinant mouse-derived Bcl-XL protein, expressed by E. coli , with C-His labeled tag.
- Application
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Alternative Names
Bcl-2-like protein 1; Bcl2-L-1; Apoptosis regulator Bcl-X; Bclx
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Species
Mouse
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Source
E. coli
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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
Q64373-1
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Expression Region
M1-R212
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AA Sequence
MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEAERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNR
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Protein Length
Partial
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Molecular Weight
33 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
Bcl-XL, a member of the B-cell lymphocyte/leukemia-2 (Bcl-2) family, plays a critical role in regulating apoptosis, the process of programmed cell death. Its primary function is to promote cell survival by inhibiting the pro-apoptotic proteins, thereby controlling the balance between cell death and cell proliferation. Abnormal expression of Bcl-XL is implicated in various diseases, particularly in cancers where its overexpression can lead to resistance against chemotherapy and radiotherapy. This makes Bcl-XL a significant target for therapeutic interventions. Researchers have focused on producing recombinant Bcl-XL protein to better understand its structure, function, and interactions with other proteins. The availability of recombinant Bcl-XL allows for advanced studies on its role in the apoptotic pathway, the development of Bcl-XL inhibitors, and the design of novel cancer treatments aimed at restoring apoptosis in resistant cancer cells. Moreover, insights gained from these studies may facilitate the design of biomarker assays for cancer prognosis, ultimately contributing to more effective, personalized therapeutic strategies. The exploration of Bcl-XL through recombinant technology not only enhances our understanding of apoptosis but also paves the way for innovative approaches in the battle against cancer.
