Analytical Data
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Gene name
BAG4
- Application
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Alternative Names
BAG4；SODD；BAG family molecular chaperone regulator 4
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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
O95429
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Expression Region
1-457aa
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AA Sequence
MSALRRSGYG PSDGPSYGRY YGPGGGDVPV HPPPPLYPLR PEPPQPPISW RVRGGGPAET TWLGEGGGGD GYYPSGGAWP EPGRAGGSHQ EQPPYPSYNS NYWNSTARSR APYPSTYPVR PELQGQSLNS YTNGAYGPTY PPGPGANTAS YSGAYYAPGY TQTSYSTEVP STYRSSGNSP TPVSRWIYPQ QDCQTEAPPL RGQVPGYPPS QNPGMTLPHY PYGDGNRSVP QSGPTVRPQE DAWASPGAYG MGGRYPWPSS APSAPPGNLY MTESTSPWPS SGSPQSPPSP PVQQPKDSSY PYSQSDQSMN RHNFPCSVHQ YESSGTVNND DSDLLDSQVQ YSAEPQLYGN ATSDHPNNQD QSSSLPEECV PSDESTPPSI KKIIHVLEKV QYLEQEVEEF VGKKTDKAYW LLEEMLTKEL LELDSVETGG QDSVRQARKE AVCKIQAILE KLEKKGL
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Molecular Weight
49.5 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
BAG4, a member of the BAG (Bcl-2-associated athanogene) family, has garnered significant interest in the field of protein research due to its potential role in various cellular processes, including apoptosis, cancer progression, and cellular stress responses. As an anti-apoptotic protein, BAG4 interacts with molecular chaperones and modulates the activity of key proteins involved in cell survival pathways, such as Bcl-2 and HSP70. Dysregulation of BAG4 expression has been implicated in several types of cancer, making it a promising target for therapeutic intervention. Recent studies have focused on the structural characterization of BAG4, exploring its domains and binding interactions to better understand its functional mechanisms. This includes investigations into its role in modulating autophagy and its impact on proteostasis under stress conditions. By employing recombinant DNA technology, researchers aim to produce BAG4 in various expression systems, facilitating the study of its biochemical properties and interactions with other cellular components. Such efforts could reveal novel insights into BAG4’s function and its potential as a biomarker or therapeutic target in oncology and other diseases, highlighting the importance of further exploring this multifunctional protein in biomedical research.
