Analytical Data
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基因名
SSA1
- Application
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别名
SSA1；HIS2；Histatin-3
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P19474
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表达区间
1-475aa
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氨基酸序列
MASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEISQEAREGTQGERCAVHGERLHLFCEKDGKALCWVCAQSRKHRDHAMVPLEEAAQEYQEKLQVALGELRRKQELAEKLEVEIAIKRADWKKTVETQKSRIHAEFVQQKNFLVEEEQRQLQELEKDEREQLRILGEKEAKLAQQSQALQELISELDRRCHSSALELLQEVIIVLERSESWNLKDLDITSPELRSVCHVPGLKKMLRTCAVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCPLNIGSQGSTDY
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分子量
56.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
SSA1 (Stress-70 protein) is a member of the heat shock protein (Hsp70) family, which plays a critical role in cellular stress responses, protein folding, and prevention of aggregation. Research on SSA1 has gained considerable attention due to its involvement in various biological processes, such as protein synthesis, transport, and degradation, particularly under stressful conditions like heat shock or oxidative stress. The high conservation of Hsp70 proteins across species highlights their fundamental importance in cell biology. In the context of disease, SSA1 has been implicated in neurodegenerative disorders, cancer, and infections, making it a potential therapeutic target. Recent advancements in recombinant protein technology have facilitated the production and study of SSA1 in vitro, allowing researchers to investigate its structure, function, and potential interactions with other cellular proteins. By understanding the mechanisms by which SSA1 and similar heat shock proteins operate, scientists aim to uncover novel strategies for intervention in various diseases associated with protein misfolding and aggregation. This research not only contributes to our fundamental understanding of molecular chaperones but also paves the way for the development of therapeutic approaches aimed at enhancing cellular resilience against stress.
