Recombinant Human Bcl-2-like protein 10 (BCL2L10)

Shipped with Ice Packs
In Stock

Description

Introduction to Recombinant Human Bcl-2-like protein 10 (BCL2L10)

Recombinant Human Bcl-2-like protein 10 (BCL2L10) is a member of the B-cell lymphoma-2 (Bcl-2) family of proteins, which play crucial roles in regulating apoptosis, or programmed cell death. BCL2L10 is less studied compared to other members of this family but has been implicated in various cellular processes, including cell survival and cancer progression.

Role in Cancer

Recent studies have highlighted the role of BCL2L10 in cancer, particularly in melanoma. BCL2L10 is overexpressed in melanoma and acts as a pro-survival factor, reducing the cytotoxic effects of drugs such as cisplatin, dacarbazine, and ABT-737 . Additionally, BCL2L10 enhances aggressive features of melanoma cells by promoting cell migration, invasion, and vasculogenic mimicry .

Table 1: BCL2L10's Role in Melanoma

PropertyEffect of BCL2L10 Overexpression
Cell MigrationIncreased
Cell InvasionIncreased
Vasculogenic MimicryIncreased
Tumor GrowthNot significantly affected
AngiogenesisNot significantly affected

Signaling Pathways and Mechanisms

BCL2L10 influences various signaling pathways. In melanoma, it positively affects the phosphorylation of extracellular-signal-regulated kinase (ERK) and the expression of markers associated with cell invasion, such as urokinase plasminogen activator receptor (uPAR) and matrix metalloproteinases (MMPs) . Additionally, BCL2L10 regulates intracellular calcium levels, which can impact cell signaling and survival .

Research Findings in Other Cancers

In ovarian cancer, BCL2L10 has been shown to influence metabolic pathways. Knockdown of BCL2L10 leads to decreased expression of genes involved in metabolism, such as succinate dehydrogenase complex subunit D (SDHD) and isocitrate dehydrogenase 1 (IDH1), suggesting a role in regulating the tricarboxylic acid (TCA) cycle .

Table 2: BCL2L10's Impact on Metabolic Genes in Ovarian Cancer

GeneEffect of BCL2L10 Knockdown
SDHDDecreased expression
IDH1Decreased expression
LCLAT1Decreased expression
ENOPH1Decreased expression
IDI1Decreased expression
HPRT1Decreased expression
ATP6V1DDecreased expression

Product Specs

Form
Lyophilized powder
Note: While we prioritize shipping the format currently in stock, please specify your format preference in order notes for customized preparation.
Lead Time
Delivery times vary depending on the purchasing method and location. Consult your local distributor for precise delivery estimates.
Note: Standard shipping includes blue ice packs. Dry ice shipping requires prior arrangement and incurs additional charges.
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Centrifuge the vial briefly before opening to consolidate the contents. Reconstitute the protein in sterile, deionized water to a concentration of 0.1-1.0 mg/mL. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting at -20°C/-80°C. Our standard glycerol concentration is 50% and serves as a guideline.
Shelf Life
Shelf life depends on storage conditions, buffer composition, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized forms have a 12-month shelf life at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquoting is essential for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type is determined during the manufacturing process.
If you require a specific tag, please inform us; we will prioritize its development.
Synonyms
BCL2L10; BCLB; Bcl-2-like protein 10; Bcl2-L-10; Anti-apoptotic protein NrH; Apoptosis regulator Bcl-B
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-194
Protein Length
full length protein
Species
Homo sapiens (Human)
Target Names
BCL2L10
Target Protein Sequence
MADPLRERTELLLADYLGYCAREPGTPEPAPSTPEAAVLRSAAARLRQIHRSFFSAYLGY PGNRFELVALMADSVLSDSPGPTWGRVVTLVTFAGTLLERGPLVTARWKKWGFQPRLKEQ EGDVARDCQRLVALLSSRLMGQHRAWLQAQGGWDGFCHFFRTPFPLAFWRKQLVQAFLSC LLTTAFIYLWTRLL
Uniprot No.

Target Background

Function
BCL2L10 promotes cell survival by inhibiting BAX-induced, but not BAK-induced, apoptosis. It enhances the binding of AHCYL1/IRBIT to ITPR1, reducing ITPR1-mediated calcium release from the endoplasmic reticulum in collaboration with AHCYL1/IRBIT under normal conditions. Under apoptotic stress, it dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, resulting in increased Ca²⁺ transfer to mitochondria and subsequent apoptosis promotion.
Gene References Into Functions
  1. BCL2L10-positive cells in bone marrow may serve as a biomarker for azacitidine response and overall survival, potentially impacting clinical practice. PMID: 28514758
  2. Inhibition of Bcl2l10 activity and the promotion of endoplasmic reticulum-mitochondria contact facilitate increased Ca²⁺ transfer to mitochondria and apoptosis, as suggested by research findings. PMID: 27995898
  3. A structural genetic variant disrupting BCL2L10 and PNLDC1 was identified in a family with bipolar I disorder, suggesting these genes as novel candidates for affective psychosis. PMID: 27260655
  4. BCL2L10 downregulation in hepatocellular carcinoma (HCC) and its overexpression suppressing cell growth and migration indicate a tumor-suppressor role in HCC. PMID: 27770580
  5. BCL2L10 expression acted as a starvation stress sensor, inducing simultaneous apoptosis and autophagy in HCC cells via the AMPK-mTOR signaling cascade. PMID: 28259820
  6. A BCL2L10 variant was identified as a protective factor against therapy-related myeloid neoplasms and de novo myelodysplastic syndrome. PMID: 24047476
  7. Polyubiquitination and proteasomal turnover regulate BCL2L10 expression levels and anti-apoptotic capacity. PMID: 23563182
  8. BCL2L10 is predominantly localized to mitochondria in healthy preimplantation embryos, while abnormal embryos show extra-mitochondrial localization. PMID: 23293224
  9. BCL2L10 protects cells from Bax-dependent apoptotic pathways through its interaction with the BH3 motif of Bim. PMID: 23235460
  10. BCL2L10 interacts with the BH3 domain of BECN1, and its overexpression reduces autophagy induced by various stimuli. PMID: 22498477
  11. BCL2L10 expression predicts azacitidine resistance in myelodysplastic syndrome patients. PMID: 22577154
  12. Ubiquilin stabilizes BCL2L10, promoting monoubiquitination and cytosolic relocation. PMID: 22233804
  13. BCL2L10 methylation is associated with myelodysplastic syndromes. PMID: 21760590
  14. Loss of BCL2L10 protein expression correlates with poor prognosis in gastric carcinoma. PMID: 21166696
  15. Aberrant promoter methylation of BCL2L10 is frequent in acute leukemia (both de novo and therapy-related). PMID: 21077739
  16. BCL2L10's pro-apoptotic effect and growth inhibition by siRNA suggest its tumor suppressor role in gastric cancer. PMID: 21171085
  17. Studies using homology modeling and protein-protein docking investigated the 3D structure of BCL2L10 and its interactions with the BH3 domain of BAX. PMID: 20919753
  18. BCL2L10 is frequently silenced by promoter hypermethylation in gastric cancer. PMID: 20428828
  19. NM23-H2 regulates Diva-mediated apoptosis through a previously unknown mechanism. PMID: 17532299
  20. BCL2L10 and MCL1 display reciprocal abilities to bind and neutralize Bax and Bak. PMID: 18178565
  21. Tumor-specific alterations in BCL2L10 expression may distinguish subsets of neoplasms with different clinical behaviors. PMID: 18483366
  22. Immunoprecipitation and Far-Western analysis confirmed the direct interaction of BCL2L10 and HIP1R in 293T cells. PMID: 19255499
  23. BCL2L10 is a key candidate involved in oocyte maturation, fertility, and embryo development. PMID: 19551325
Database Links

HGNC: 993

OMIM: 606910

KEGG: hsa:10017

STRING: 9606.ENSP00000260442

UniGene: Hs.283672

Protein Families
Bcl-2 family
Subcellular Location
Mitochondrion. Nucleus membrane. Endoplasmic reticulum.
Tissue Specificity
Widely expressed in adult tissues. Preferentially expressed in lung, liver and kidney.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2025 TheBiotek. All Rights Reserved.