Analytical Data
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Gene name
DNAJB9
- Application
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Alternative Names
DKFZP564F1862; DnaJ (Hsp40) homolog subfamily B member 9; DnaJ homolog subfamily B member 9; DNAJB9; DNJB9_HUMAN; eEndoplasmic reticulum DNA J domain containing protein 4; Endoplasmic reticulum DnaJ homolog 4; ER resident protein ERdj4; ERdj4; MDG 1; Mdg-1; MDG1; Microvascular endothelial differentiation gene 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UBS3
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Expression Region
1-223aa
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AA Sequence
MATPQSIFIFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANRRKEYDTLGHSAFTSGKGQRGSGSSFEQSFNFNFDDLFKDFGFFGQNQNTGSKKRFENHFQTRQDGGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDSTNQHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ
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Molecular Weight
51.9 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
DNAJB9, a member of the DNAJ/Hsp40 family of proteins, plays a pivotal role in protein homeostasis by functioning as a co-chaperone for Hsp70, facilitating protein folding and degradation. Research into DNAJB9 has gained momentum due to its significant involvement in various cellular processes, including stress response and the maintenance of cellular proteostasis. Recent studies have indicated its potential role in neurodegenerative diseases, particularly in the pathogenesis of amyloid-related disorders such as Alzheimer's and Parkinson's disease. Moreover, DNAJB9 has emerged as a promising biomarker for certain cancers, given its differential expression patterns in tumor versus normal tissues. The recombinant expression and purification of DNAJB9 allow for detailed structural and functional studies, which are vital for understanding its mechanism of action and exploring therapeutic applications. By investigating DNAJB9's interactions with substrates and other chaperone proteins, researchers aim to elucidate the protein quality control pathways and their implications in disease. This background sets the stage for further studies into DNAJB9 as a potential target for therapeutic intervention, emphasizing the need for robust methodologies for its recombinant production and characterization.
