Analytical Data
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Gene name
BAALC
- Application
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Alternative Names
BAALC；Brain and acute leukemia cytoplasmic Protein
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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
Q8WXS3
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Expression Region
1-145aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGCGGSRADA IEPRYYESWT RETESTWLTY TDSDAPPSAA APDSGPEAGG LHSGMLEDGL PSNGVPRSTA PGGIPNPEKK TNCETQCPNP QSLSSGPLTQ KQNGLQTTEA KRDAKRMPAK EVTINVTDSI QQMDRSRRIT KNCVN
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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
BAALC (B-cell acute lymphoblastic leukemia antigen) is a cell surface protein that has garnered significant attention in cancer research, particularly in hematologic malignancies. Initially identified as a potential biomarker associated with B-cell acute lymphoblastic leukemia (B-ALL), its expression has been linked to the progression and prognosis of various hematological disorders, including multiple myeloma and other leukemias. The unique expression patterns of BAALC in malignant cells, contrasted with its limited presence in normal tissues, make it an attractive target for therapeutic interventions and diagnostic purposes. Research into BAALC has driven efforts to develop recombinant proteins that can serve as tools for understanding its biological functions and interactions within the tumor microenvironment. These recombinant proteins enable detailed studies on the role of BAALC in cancer cell signaling pathways and immune responses, as well as providing a platform for therapeutic applications, such as targeted immunotherapy. By exploring the structural and functional characteristics of BAALC and its potential to serve as a target for antibody-drug conjugates or CAR T-cell therapies, researchers aim to enhance the efficacy of treatment strategies for patients with B-ALL and other related malignancies. Ongoing studies are focused on elucidating the precise mechanisms by which BAALC contributes to tumor biology, which may ultimately aid in the development of novel diagnostic and therapeutic approaches that improve patient outcomes in hematological cancers.
