Analytical Data
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Gene name
HSPBAP1
- Application
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Alternative Names
HSPBAP1;PASS1;HSPB1-associated Protein 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
Q96EW2
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Expression Region
1- 488aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAAGSEATTPVIVAAGAGGEEGEHVKPFKP EKAKEIIMSLQQPAIFCNMVFDWPARHWNAKYLSQVLHGKQIRFRMGMKS MSTVPQFETTCNYVEATLEEFLTWNCDQSSISGPFRDYDHSKFWAYADYK YFVSLFEDKTDLFQDVKWSDFGFPGRNGQESTLWIGSLGAHTPCHLDSYG CNLVFQVQGRKRWHLFPPEDTPFLYPTRIPYEESSVFSKINVVNPDLKRF PQFRKAQRHAVTLSPGQVLFVPRHWWHYVESIDPVTVSINSWIELEEDHL ARVEEAITRMLVCALKTAENPQNTRAWLNPTEVEETSHAVNCCYLNAAVS AFFDRCRTSEVVEIQALRTDGEHMKKEELNVCNHMEVGQTGSQNLTTGTD KPEAASPFGPDLVPVAQRSEEPPSERGGIFGSDGKDFVDKDGEHFGKLHC AKRQQIMSNSENAIEEQIASNTTTTPQTFISTDDLLDCLVNPQVTRIVAQ LLIQGRSL
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Molecular Weight
57 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
HSPBAP1 (Heat Shock Protein 2-Associated Protein 1) is a member of the small heat shock protein family, which is known for its role in cellular stress responses and protein homeostasis. Recent studies have revealed that HSPBAP1 plays a crucial role in various cellular processes, including cytoskeletal organization, apoptosis, and the regulation of protein aggregation, especially under stress conditions. Research indicates that dysregulation of HSPBAP1 is associated with various diseases, including neurodegenerative disorders and cancer, making it a potential therapeutic target. Additionally, the recombinant expression of HSPBAP1 in model systems allows for in-depth analysis of its functional properties and molecular mechanisms. By employing techniques such as site-directed mutagenesis and affinity purification, scientists can produce and study the recombinantly expressed HSPBAP1 protein, providing insights into its interactions with other proteins and its role in cellular processes. Understanding HSPBAP1's function at a molecular level may reveal novel strategies for intervention in pathological conditions where its expression or function is altered, thus paving the way for future therapeutic applications.
