Analytical Data
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Gene name
BCL2L10
- Application
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Alternative Names
BCL2L10；BCL-B；BCLB；BOO；Bcl-2-like Protein 10
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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
Q9HD36
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Expression Region
1-172aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMVDQLRERTTMADPLRERTELLLADYL GYCAREPGTPEPAPSTPEAAVLRSAAARLRQIHRSFFSAYLGYPGNRFEL VALMADSVLSDSPGPTWGRVVTLVTFAGTLLERGPLVTARWKKWGFQPRL KEQEGDVARDCQRLVALLSSRLMGQHRAWLQAQGGWDGFCHFFRT
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Molecular Weight
22 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
Related Products
Protein Description
BCL2L10, also known as BCL-2-like 10 or BCL2L10A, is a member of the BCL-2 family of proteins, which are critical regulators of apoptotic processes and cell survival. Research has shown that BCL2L10 plays a significant role in various cellular functions, including the regulation of apoptosis, cell cycle progression, and stress responses. Its expression has been linked to several types of cancers, where it can act as an oncogene by inhibiting programmed cell death and promoting tumor cell survival. Given its implications in malignancies, BCL2L10 has garnered attention as a potential therapeutic target for cancer treatment. Studies have explored its mechanisms of action, revealing that BCL2L10 can interact with other pro-apoptotic and anti-apoptotic proteins, influencing the overall balance of cell survival and death. Additionally, the investigation of BCL2L10 as a biomarker for cancer prognosis has emerged, highlighting its potential utility in clinical settings. Understanding the functional roles of BCL2L10 in the apoptotic pathways and its impact on tumorigenesis is crucial for developing targeted therapies that can efficiently eliminate cancer cells while sparing normal tissues. Ongoing research aims to elucidate the complex regulatory networks involving BCL2L10 and its interactions with various signaling pathways, as well as to explore its potential in combination therapies to enhance the efficacy of existing cancer treatments.
