Recombinant Human HSP40 Protein (C-6His)

Name: Recombinant Human HSP40 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0851NP
Availability: InStock

BL-0851NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Heat Shock 40 kDa Protein is produced by our E.coli expression system and the target gene encoding Gly2-Ile340 is expressed with a 6His tag at the C-terminus.
Accession	P25685
Synonym	DnaJ Homolog Subfamily B Member 1; DnaJ Protein Homolog 1; Heat Shock 40 kDa Protein 1; HSP40; Heat Shock Protein 40; Human DnaJ Protein 1; hDj-1; DNAJB1; DNAJ1; HDJ1; HSPF1
Gene Background	DnaJ Homolog Subfamily B Member 1 (DNAJB1) is a member of the heat shock protein family. Heat shock proteins (HSPs) are a highly conserved family of stress response proteins. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. DNAJB1 regulates cellular processes by aiding in the folding, transport and assembly. DNAJB1 contains a J-domain which controls interaction with the ATPase domain of DnaK. DNAJB1 interacts with HSP70 and can stimulate its ATPase activity. In addition, DNAJB1 stimulates the association between HSC70 and HIP.
Molecular Mass	39.1 KDa
Apmol Mass	38 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, 1mM EDTA, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
Subcellular Location	Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.
Database References	HGNC: 5270 OMIM: 604572 KEGG: hsa:3337 STRING: 9606.ENSP00000254322 UniGene: Hs.515210

Gene Functions References

this study shows that DNAJB1/HSP40 suppresses Melanoma Differentiation-Associated Gene 5-Mitochondrial Antiviral Signaling Protein function in conjunction with HSP70 PMID: 29069650
Modeling of the different conformations of PRKACA-DNAJB1 Chimeric Kinase revealed no obvious steric interactions of the J-domain with the rest of the RIIbeta holoenzyme. PMID: 29335433
Data show that DnaJ (Hsp40) homolog, subfamily B, member 1 (DNAJB1) is a transcriptional target of forkhead box protein E3 (FOXE3) in a pathway that is crucial for the development of the anterior segment of the eye. PMID: 27218149
These results indicate that Mixed fibrolamellar hepatocellular carcinoma (mFL-HCC) is similar to pure FL-HCC at the genomic level and the DNAJB1:PRKACA fusion can be used as a diagnostic tool for both pure and mFL-HCC PMID: 27029710
These studies demonstrate an important role for cellular chaperone Hsp40/DnaJB1 in influenza A virus life cycle by assisting nuclear trafficking of viral ribonucleoproteins. PMID: 26750153
DNAJB1-PRKACA was evaluated as a key driver of fibrolamellar carcinoma and as a candidate therapeutic target PMID: 26505878
study provides a new molecular mechanism to regulate EGFR signaling through modulation of MIG6 by DNAJB1 as a negative regulator. PMID: 26239118
Whole exome sequencing followed by immunohistochemistry of fibrolamellar hepatocellular carcinoma cell lines and tumors showed two structural variants resulting in fusion transcripts: DNAJB1-PRKCA and CLPTM1L-GLIS3. PMID: 25122662
In this cohort of fibrolamellar hepatocellular carcinoma, almost 80% contained the DNAJB1-PRKACA fusion transcript. PMID: 25557953
Authors identified DNAJB1 as a negative regulator of PDCD5-mediated apoptosis and found that the apoptosis network of PDCD5 regulates cancer cell death. PMID: 25444898
We also found that, despite an initial report to the contrary, the human homolog of Sis1, Hdj1, is capable of [PSI+] prion propagation in place of Sis1 PMID: 25058638
HSP40 interacts with pyruvate kinase M2 and regulates glycolysis and cell proliferation in tumor cells. PMID: 24658033
Studies with specific phosphoantibodies indicate that MK5 phosphorylates Hsp40/DnaJB1 in vivo at Ser-149 or/and Ser-151 and Ser-171 in the C-terminal domain of Hsp40/DnaJB1. PMID: 24309468
Evidence supporting the presence of the DNAJB1-PRKACA chimeric transcript in 100% of the FL-HCCs examined (15/15) suggests that this genetic alteration contributes to tumor pathogenesis. PMID: 24578576
we discovered a new MDM2 interacting protein, DNAJB1, and provided evidence to support its p53-dependent tumor suppressor function. PMID: 24361594
HSP40 and HSP110 function together in protein homeostasis control. PMID: 24091676
methionine deprivation results in an antioxidant response that includes an increase in the levels of HSPA1A and DNAJB1 mRNA PMID: 23395854
There was a positive correlation between DnaJB1 and severity of pulmonary arterial hypertension in peripheral blood mononuclear cells from patients with limited cutaneous systemic sclerosis. PMID: 23400395
Hsp40 regulates the amount of keratin proteins via ubiquitin-proteasome pathway. PMID: 22075554
Mammalian Hsp110 (Apg-2), Hsp70 (Hsc70 or Hsp70) and Hsp40 (Hdj1) were necessary and sufficient to slowly dissolve large disordered aggregates and recover natively folded protein PMID: 22022600
Cellular localization studies showed that NP and Hsp40 co-localize primarily in the nucleus. During IAV infection in mammalian cells, expression of NP coincided with the dissociation of P58(IPK) from Hsp40 and decrease PKR phosphorylation PMID: 21698289
The antiviral activity of overexpressed DNAJC14 occurs in a time- and dose-dependent manner. PMID: 21249176
The crystal structure of full-length Hdj1 was diffracted to 3.90A resolution. PMID: 21139202
5-fluorouracil & carboplatin specifically induce expression of Hsp40 in hepatoma cells. siRNA knockdown of Hsp40 diminishes survival of drug-exposed cells. PMID: 19901540
Altered expression of HSPF1 was found in brains and lymphoblastoid cells from patients with bipolar disorder. PMID: 14743183
sequestered in discrete foci in the nucleus of the infected cell in herpes simplex virus type 1 infection PMID: 15194794
It is confirmed an increased expression of HSPF1 in the lymphoblastoid cell lines from patients with bipolar I disorder, bipolar II disorder, and schizophrenia. PMID: 15362566
Hsp40 is crucial for Nef-mediated enhancement of viral gene expression and replication PMID: 16179353
hepatitis B virus X protein is the major target of Hdj1 in the inhibition of hepatitis B virus replication PMID: 16842747
These results demonstrate a role for Hsp40/DnaJB6 in the regulation of HIV-2 PIC nuclear transport. PMID: 18032501
The 2.7A structure reveals that Hdj1 forms a homodimer in the crystal by a crystallographic two-fold axis. PMID: 18211704

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.