Analytical Data
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基因名
dnaK
- Application
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别名
dnaK；groP；grpF；seg；Chaperone Protein DnaK
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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
P0A6Y8
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表达区间
1-638aa
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氨基酸序列
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK
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分子量
69 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
The DnaK protein, a member of the Hsp70 (heat shock protein 70) family, plays a crucial role in the molecular chaperone system of cells. It is primarily involved in the proper folding of proteins, the prevention of aggregation, and the restoration of misfolded proteins, which is essential for cellular homeostasis, especially under stress conditions such as heat shock or oxidative stress. Research on DnaK has gained significant attention due to its involvement in various biological processes, including protein translocation and assembly of multi-protein complexes. Additionally, DnaK's function in bacterial systems has made it a target for antimicrobial drug development, as inhibiting this protein can impair bacterial growth and survival. Recent advancements in structural biology have provided detailed insights into the conformational dynamics of DnaK, revealing how it interacts with substrates and the intricate regulation of its activity. Understanding the DnaK chaperone mechanism not only enhances our knowledge of fundamental cellular processes but also has potential implications in fields such as biotechnology and medicine, particularly in the context of diseases associated with protein misfolding and aggregation. As a result, the study of DnaK continues to be a vibrant area of research, linking basic science with practical applications in addressing health challenges caused by protein homeostasis dysregulation.
