Analytical Data
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基因名
HSPA5
- Application
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别名
HSPA5；HSPA5BP1；KIAA1583；Transmembrane Protein 132A
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种属
Human
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表达系统
E. coli
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标签
N-terminal His-Tag
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P11021
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表达区间
19-654aa
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氨基酸序列
EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL
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分子量
72.9kDa
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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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Identification
Protein Description
HSPA5, also known as BiP (Binding Immunoglobulin Protein), is a member of the heat shock protein 70 (HSP70) family and plays a crucial role in the endoplasmic reticulum (ER) stress response and protein homeostasis. It serves as a molecular chaperone, assisting in the proper folding of nascent proteins and preventing aggregation under stress conditions. Research into HSPA5 has gained momentum due to its implications in various pathological conditions, including neurodegenerative diseases, cancer, and metabolic disorders. The upregulation of HSPA5 has been identified as a protective response to ER stress, which is often triggered by factors such as oxidative stress, hypoxia, and the accumulation of misfolded proteins. Recent studies have also highlighted its role in regulating cellular apoptosis and autophagy, making it a potential therapeutic target. The ability to produce recombinant HSPA5 protein allows for detailed analysis of its structure-function relationships, interactions with other chaperones and client proteins, and its mechanistic role in cellular stress responses. Understanding the molecular dynamics of HSPA5 not only sheds light on fundamental cellular processes but also paves the way for innovations in targeted therapies for diseases associated with dysregulated protein homeostasis. As the demand for biopharmaceuticals and novel therapeutic strategies grows, research surrounding HSPA5 continues to expand, offering significant insights into its potential utility in clinical applications.
