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 (C-His) is the recombinant mouse-derived Bcl-XL, expressed by E. coli , with C-6*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-6*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
27 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 Bcl-2 family of proteins, plays a crucial role in the regulation of apoptosis, or programmed cell death, which is essential for maintaining cellular homeostasis and tissue integrity. Dysregulation of Bcl-XL is implicated in various diseases, including cancers, where its overexpression can lead to tumor survival and resistance to therapy. This has sparked significant interest in Bcl-XL as a potential therapeutic target. The study of recombinant Bcl-XL protein has enabled researchers to explore its functional mechanisms, interaction with other apoptosis regulators, and its role in cellular signaling pathways. By producing recombinant Bcl-XL in vitro, scientists can investigate its structure-function relationships and develop specific inhibitors that may restore apoptotic processes in cancer cells. This research has yielded insights into the therapeutic potential of Bcl-XL antagonists, paving the way for novel cancer treatments that aim to enhance the efficacy of existing therapies and overcome resistance mechanisms. The ongoing exploration of Bcl-XL’s biological roles and its clinical significance continues to be a promising avenue in the fight against malignancies and other pathologies linked to aberrant apoptosis.
