Analytical Data
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基因名
HSPA1L
- Application
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别名
HSPA1L；Heat shock 70 kDa Protein 1-like
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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
P34931
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表达区间
1-641aa
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氨基酸序列
MATAKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ VAMNPQNTVF DAKRLIGRKF NDPVVQADMK LWPFQVINEG GKPKVLVSYK GENKAFYPEE ISSMVLTKLK ETAEAFLGHP VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA AAIAYGLDKG GQGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR LLQDYFNGRD LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTALIKRNS TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTKDNNLLGR FDLTGIPPAP RGVPQIEVTF DIDANGILNV TATDKSTGKV NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA KNALESYAFN MKSVVSDEGL KGKISESDKN KILDKCNELL SWLEVNQLAE KDEFDHKRKE LEQMCNPIIT KLYQGGCTGP ACGTGYVPGR PATGPTIEEV D
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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
HSPA1L, a member of the heat shock protein 70 (HSP70) family, plays a critical role in cellular stress responses and protein homeostasis. It is involved in various biological processes, including protein folding, assembly, and degradation, which are essential for maintaining cellular integrity under stress conditions such as heat shock, oxidative stress, and inflammation. Research on HSPA1L has gained attention due to its potential implications in various diseases, including cancer, neurodegenerative disorders, and infections. The interest in this recombinant protein arises from its ability to enhance cell survival and functionality, suggesting a protective mechanism against cellular stress. Additionally, HSPA1L may serve as a therapeutic target or biomarker due to its involvement in critical signaling pathways and cellular processes. The generation of recombinant HSPA1L protein has facilitated studies examining its structural properties, functional roles, and interaction with other cellular proteins. Understanding the molecular mechanisms of HSPA1L action contributes to the development of novel therapeutic strategies aimed at modulating its activity in disease contexts. Furthermore, due to its immunogenic properties, HSPA1L is being explored as a potential candidate for vaccine development, particularly in cancer immunotherapy. Overall, the study of HSPA1L recombinant protein is a promising field that bridges basic research with clinical applications, aiming to improve therapeutic outcomes in various health conditions.
