Analytical Data
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Gene name
BAG1
- Application
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Alternative Names
BAG1；HAP；BAG family molecular chaperone regulator 1
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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
Q99933
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Expression Region
1-345aa
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AA Sequence
MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSGRPPAR STASGHDRPT RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW SEEATQSEEA TQGEEMNRSQ EVTRDEESTR SEEVTREEMA AAGLTVTVTH SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV IGVPQSFQKL IFKGKSLKEM ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV EKIADQLEEL NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN FKDSRLKRKG LVKKVQAFLA ECDTVEQNIC QETERLQSTN FALAE
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Molecular Weight
38.7 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
BAG1, a member of the Bcl-2-associated athanogene (BAG) family, plays a significant role in cellular processes such as protein folding, degradation, and apoptosis regulation. The BAG1 protein contains a BAG domain that interacts with heat shock proteins (HSPs), particularly HSP70, to mediate stress responses and enhance protein chaperoning mechanisms. It has been implicated in various physiological processes and diseases, including cancer, neurodegeneration, and cardiac dysfunction. Research has highlighted BAG1's potential as a therapeutic target due to its ability to modulate cell survival and apoptosis pathways. By understanding the molecular mechanisms underlying BAG1 interactions and functions, scientists aim to develop innovative strategies for disease intervention, particularly in conditions where cellular stress and misfolded proteins are prevalent. Thus, the study of BAG1 recombinant protein is crucial for elucidating its role in health and disease, potentially leading to novel therapeutic approaches that leverage its unique properties in regulating cellular homeostasis.
