Analytical Data
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Gene name
DNAJA4
- Application
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Alternative Names
DnaJ (Hsp40) homolog subfamily A member 4; DnaJ (Hsp40) homolog; subfamily A; member4; DNAJ A4; DnaJ heat shock protein family (Hsp40) member A4; DnaJ homolog subfamily A member 4; DNAJA 4
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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
Q8WW22
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Expression Region
1-397aa
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AA Sequence
MVKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFSSPMDIFDMFFGGGGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSVEKCPLCKGRGMQIHIQQIGPGMVQQIQTVCIECKGQGERINPKDRCESCSGAKVIREKKIIEVHVEKGMKDGQKILFHGEGDQEPELEPGDVIIVLDQKDHSVFQRRGHDLIMKMKIQLSEALCGFKKTIKTLDNRILVITSKAGEVIKHGDLRCVRDEGMPIYKAPLEKGILIIQFLVIFPEKHWLSLEKLPQLEALLPPRQKVRITDDMDQVELKEFCPNEQNWRQHREAYEEDEDGPQAGVQCQTA
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Molecular Weight
69.41 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
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Protein Description
DNAJA4, a member of the DnaJ heat shock protein family, plays a crucial role in protein folding and protection against cellular stress. This chaperone is particularly involved in the regulation of protein quality control mechanisms within the endoplasmic reticulum (ER), assisting in the proper folding of nascent polypeptides and facilitating the refolding or degradation of misfolded proteins through the ER-associated degradation (ERAD) pathway. Dysregulation of DNAJA4 has been implicated in various diseases, including neurodegenerative disorders and certain cancers, where it may contribute to the accumulation of misfolded proteins. As such, understanding the molecular mechanisms and functional implications of DNAJA4 is of significant interest in the fields of cell biology and biomedicine. Recent studies have focused on characterizing its structure, functional domains, and interaction partners, as well as its role in cellular stress responses. These investigations aim to elucidate the potential of DNAJA4 as a therapeutic target or biomarker, particularly in contexts where protein misfolding is a hallmark. Additionally, research into the recombinant expression of DNAJA4 has enabled the production of this protein in vitro, facilitating the investigation of its biochemical properties and interactions with other proteins. By unraveling the complex dynamics of DNAJA4, researchers hope to better understand its contributions to cellular homeostasis and its potential implications in disease, paving the way for innovative therapeutic strategies.
