Analytical Data
-
Gene name
DNAJC27
- Application
-
Alternative Names
DNAJC27；RABJS；RBJ;DnaJ homolog subfamily C member 27
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NZQ0
-
Expression Region
1-273aa
-
AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEANMPK RKEPGRSLRI KVISMGNAEV GKSCIIKRYC EKRFVSKYLA TIGIDYGVTK VHVRDREIKV NIFDMAGHPF FYEVRNEFYK DTQGVILVYD VGQKDSFDAL DAWLAEMKQE LGPHGNMENI IFVVCANKID CTKHRCVDES EGRLWAESKG FLYFETSAQT GEGINEMFQT FYISIVDLCE NGGKRPTTNS SASFTKEQAD AIRRIRNSKD SWDMLGVKPG ASRDEVNKAY RKLAVLLHPD KCVAPGSEDA FKAVVNARTA LLKNIK
-
Molecular Weight
33 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
DNAJC27 is a member of the DnaJ protein family, which plays a crucial role in protein folding, cellular stress responses, and the maintenance of proteostasis. This co-chaperone is known to interact with heat shock proteins (HSPs), particularly HSP70, facilitating the proper folding and maturation of client proteins. Recent studies have highlighted the importance of DNAJC27 in various physiological processes, including mitochondrial function and cellular survival under stress conditions. Dysregulation of DNAJC27 has been implicated in several diseases, such as neurodegenerative disorders and cancer, suggesting that it may serve as a biomarker or therapeutic target. Understanding the structural characteristics and functional mechanisms of DNAJC27 through recombinant protein studies can provide insights into its role in cellular homeostasis and disease progression. By producing recombinant DNAJC27, researchers aim to investigate its interactions with client proteins and HSPs, and elucidate its contribution to cellular functions. This research holds potential for developing innovative therapeutic strategies that leverage the chaperone system to treat diseases associated with protein misfolding and aggregation.
