Analytical Data
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Gene name
ssaA1
- Application
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Alternative Names
ssaA1；Staphylococcal secretory antigen ssaA1
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Species
E.coli
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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
Q5HCY4
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Expression Region
27-255aa
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AA Sequence
AEQNNNGYNSNDAQSYSYTYTIDAQGNYHYTWTGNWNPSQLTQNNTYYYNNYNTYSYNNASYNNYYNHSYQYNNYTNNSQTATNNYYTGGSGASYSTTSNNVHVTTTAAPSSNGRSISNGYASGSNLYTSGQCTYYVFDRVGGKIGSTWGNASNWANAAASSGYTVNNTPKVGAIMQTTQGYYGHVAYVEGVNSNGSVRVSEMNYGHGAGVVTSRTISANQAGSYNFIH
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Molecular Weight
27.0 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
The research on the recombinant protein SSA1 (Stress-Inducible Protein 1) has gained significant attention due to its crucial role in cellular stress response and protein folding. SSA1, belonging to the Hsp70 (Heat Shock Protein 70) family, is a molecular chaperone that assists in the proper folding of nascent polypeptides and the refolding of denatured proteins, thereby promoting overall cellular homeostasis. Its expression is upregulated under stress conditions such as heat shock, oxidative stress, and various pathological states. Investigating SSA1 as a recombinant protein provides insights into its biological functions, interactions, and potential therapeutic applications, especially in diseases characterized by protein misfolding and aggregation, such as neurodegenerative disorders. Furthermore, the characterization of SSA1 can contribute to understanding the intricate mechanisms of cellular stress responses, making it a valuable target for drug design and development. The recombinant form of SSA1 can be produced in various expression systems, allowing for comprehensive studies on its structure-function relationships and interactions with other cellular components, ultimately paving the way for innovative strategies to enhance cellular resilience and combat stress-related diseases.
