Recombinant Human Dnaj Homolog Subfamily A Member 1 (DNAJA1) Protein (His&Myc)

Name: Recombinant Human Dnaj Homolog Subfamily A Member 1 (DNAJA1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-10982P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Dnaj Homolog Subfamily A Member 1 (DNAJA1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P31689
Target Symbol	DNAJA1
Synonyms	DJ 2; DJ2; DjA1; DnaJ (Hsp40) homolog; subfamily A; member 1; DnaJ homolog subfamily A member 1; DnaJ protein homolog 2; DNAJ2; Dnaja1; DNJA1_HUMAN; hDJ 2; HDJ-2; HDJ2; Heat shock 40 kDa protein 4; heat shock protein DNAJ like 2; Heat shock protein J2; HSDJ; HSJ-2; HSJ2; HSPF4; Human DnaJ protein 2; NEDD7; Neural precursor cell expressed developmentally down regulated 7; OTTHUMP00000021193
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQC
Expression Range	1-394aa
Protein Length	Full Length of Mature Protein
Mol. Weight	52.0 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Co-chaperone for HSPA8/Hsc70. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV.
Subcellular Location	Membrane; Lipid-anchor. Cytoplasm. Microsome. Nucleus. Cytoplasm, perinuclear region. Mitochondrion.
Database References	HGNC: 5229 OMIM: 602837 KEGG: hsa:3301 STRING: 9606.ENSP00000369127 UniGene: Hs.445203
Tissue Specificity	Ubiquitous. Isoform 2 is highly expressed in testis and lung, but detected at low levels in thymus, prostate, colon and liver.

Gene Functions References

that DNAJA1 controls the fate of misfolded stabilization of mutant p53 PMID: 27775703
Therefore, we propose that DnaJA1 is co-opted by the influenza A virus to enter the nucleus and to enhance its RNA polymerase activity in an Hsp70 cochaperone-independent manner. PMID: 25253355
structure and function of human DNAJA1 and its relationship to pancreatic cancer PMID: 24512202
we combined the Hsp70-NEF pairs with cochaperones of the J protein family (DnaJA1, DnaJA2, DnaJB1, and DnaJB4) to generate 16 permutations. PMID: 24318877
Moreover, the levels of DnaJA1 and Hsp70 seem to play against each other with regard to tau: as DnaJA1 levels increase, tau levels are reduced, but this can be prevented if Hsp70 levels are simultaneously induced. PMID: 22343013
Hdj2 directly associates with Japanese encephalitis virus nonstructural protein NS5 and facilitates viral replication. PMID: 21999493
Hsc70 and a dimer of DjA1 independently bind to an unfolded protein PMID: 20363747
Hsp40 type 1 chaperones DJA1 (DNAJA1/Hdj2) and DJA2 (DNAJA2) as key modulators of hERG degradation PMID: 19940115
Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy PMID: 11796717
HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor PMID: 11809754
sequence analysis of two isoforms PMID: 12974469
Multiple tissue polymerase chain reaction (PCR) results showed that nDnaJA1 expressed highly in testis and lung but low in thymus, prostate, colon and liver PMID: 15595953
Results indicate that DjA1 and DjB4 of subfamilies A and B of human Hsp40 have different quaternary structures and chaperone functions. PMID: 15661747
DJA1 was inhibitory of refolding with DJA2 and Hsc70. PMID: 18684711

FAQs

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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.