Analytical Data
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Gene name
BAG5
- Application
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Alternative Names
BAG5；KIAA0873；BAG family molecular chaperone regulator 5
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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
Q9UL15
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Expression Region
1-447aa
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AA Sequence
MDMGNQHPSISRLQEIQKEVKSVEQQVIGFSGLSDDKNYKKLERILTKQLFEIDSVDTEGKGDIQQARKRAAQETERLLKELEQNANHPHRIEIQNIFEEAQSLVREKIVPFYNGGNCVTDEFEEGIQDIILRLTHVKTGGKISLRKARYHTLTKICAVQEIIEDCMKKQPSLPLSEDAHPSVAKINFVMCEVNKARGVLIALLMGVNNNETCRHLSCVLSGLIADLDALDVCGRTEIRNYRREVVEDINKLLKYLDLEEEADTTKAFDLRQNHSILKIEKVLKRMREIKNELLQAQNPSELYLSSKTELQGLIGQLDEVSLEKNPCIREARRRAVIEVQTLITYIDLKEALEKRKLFACEEHPSHKAVWNVLGNLSEIQGEVLSFDGNRTDKNYIRLEELLTKQLLALDAVDPQGEEKCKAARKQAVRLAQNILSYLDLKSDEWEY
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Molecular Weight
67.2 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
BAG5, a member of the Bcl-2-associated athanogene (BAG) family, plays a crucial role in cellular stress responses, protein homeostasis, and anti-apoptotic processes. The BAG5 protein is characterized by the presence of a BAG domain that facilitates interactions with various target proteins, including chaperones and proteasomes, thus influencing protein folding and degradation pathways. Research has indicated that BAG5 is involved in the regulation of several key cellular processes, including autophagy, cell survival, and proliferation. Its overexpression has been linked to various types of cancer, contributing to tumor development and progression by promoting resistance to chemotherapy and apoptosis. Understanding the functional mechanisms of BAG5 at the molecular level is vital for elucidating its role in cancer biology and other diseases associated with protein misfolding and aggregation. This has spurred interest in developing BAG5 as a potential therapeutic target, aiming to inhibit its function or enhance the degradation of BAG5-associated oncogenic factors. Investigating the structural features and interaction dynamics of BAG5 through recombinant protein studies could provide valuable insights into its biological significance and therapeutic potential, paving the way for novel strategies in cancer treatment and beyond.
