Analytical Data
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Gene name
BCL2L12
- Application
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Alternative Names
B2L12_HUMAN; BCL 2 like 12 (proline rich); BCL 2 like 12; BCL 2 like 12 isoform 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HB09
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Expression Region
1-333aa
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AA Sequence
MGRPAGLFPPLCPFLGFRPEACWERHMQIERAPSVPPFLRWAGYRPGPVRRRGKVELIKFVRVQWRRPQVEWRRRRWGPGPGASMAGSEELGLREDTLRVLAAFLRRGEAAGSPVPTPPSPAQEEPTDFLSRLRRCLPCSLGRGAAPSESPRPCSLPIRPCYGLEPGPATPDFYALVAQRLEQLVQEQLKSPPSPELQGPPSTEKEAILRRLVALLEEEAEVINQKLASDPALRSKLVRLSSDSFARLVELFCSRDDSSRPSRACPGPPPPSPEPLARLALAMELSRRVAGLGGTLAGLSVEHVHSFTPWIQAHGGWEGILAVSPVDLNLPLD
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Molecular Weight
63.1 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
BCL2L12, a member of the Bcl-2 protein family, has garnered significant interest in cancer research due to its role in regulating apoptosis and cellular survival. This protein is characterized by the presence of Bcl-2 homology (BH) domains, which facilitate its interaction with other apoptotic regulators. Studies have demonstrated that BCL2L12 can inhibit pro-apoptotic signals, thereby promoting cell survival in various malignancies, including leukemia, breast cancer, and melanoma. Its expression is often upregulated in cancerous tissues, correlating with resistance to chemotherapy and poor patient prognosis. Consequently, understanding the molecular mechanisms underlying BCL2L12's function has become crucial for developing targeted therapies. Recombinant BCL2L12 protein can be utilized in functional assays to elucidate its biochemical pathways, interaction with other proteins, and impact on cell fate. This research could unveil potential therapeutic strategies to modulate its activity, aiming to sensitize cancer cells to apoptosis and improve treatment outcomes. As such, the study of BCL2L12 not only enhances our understanding of cancer biology but also provides a promising avenue for novel therapeutic interventions.
