Biotinylated Recombinant Human Dnaj Homolog Subfamily C Member 5 (DNAJC5) Protein (MBP&His-Avi)

Name: Biotinylated Recombinant Human Dnaj Homolog Subfamily C Member 5 (DNAJC5) Protein (MBP&His-Avi)
Brand: Beta LifeScience
SKU: BLC-06931P
Price: 815.2 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Avi-tagged proteins, Biotinylated proteins, Featured biotinylated protein molecules, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Biotinylated Recombinant Human Dnaj Homolog Subfamily C Member 5 (DNAJC5) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9H3Z4
Target Symbol	DNAJC5
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-MBP&C-6His-Avi
Target Protein Sequence	MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVFCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN
Expression Range	1-198aa
Protein Length	Full Length
Mol. Weight	69.9 kDa
Research Area	Neuroscience
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	Acts as a general chaperone in regulated exocytosis. Acts as a co-chaperone for the SNARE protein SNAP-25. Involved in the calcium-mediated control of a late stage of exocytosis. May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings.
Subcellular Location	Cytoplasm, cytosol. Membrane; Lipid-anchor. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane. Melanosome. Cell membrane.
Database References	HGNC: 16235 OMIM: 162350 KEGG: hsa:80331 STRING: 9606.ENSP00000354111 UniGene: Hs.164419
Associated Diseases	Ceroid lipofuscinosis, neuronal, 4B (CLN4B)
Tissue Specificity	Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart.

Gene Functions References

Results indicate that by assisting local lysosome/proteasome processes, CSPalpha-mediated removal of toxic proteins via extracellular vesicles plays a central role in synaptic proteostasis. PMID: 28424476
The importance of specific residues in the cysteine-string domain was investigated, revealing that a central core of palmitoylated cysteines is essential for aggregation of adult-onset neuronal ceroid lipofuscinosis CSPalpha L115R/L116 mutants. PMID: 28127059
Phosphorylation of CSP triggers a major conformational switch that modulates its protein interactions. PMID: 27452402
In fact, DnaJC5 overexpression induced tau release in cells, neurons, and brain tissue, but only when activity of the chaperone Hsc70 was intact and when tau was able to associate with this chaperone. PMID: 27261198
This study demonstrated that Neuronal ceroid lipofuscinosis with DNAJC5/CSPalpha mutation has PPT1 pathology and exhibit aberrant protein palmitoylation. PMID: 26659577
These results suggest that the degeneration seen in the patients with AD-ANCL reported here might be a consequence of both the early effects of CSPalpha mutations at the cellular soma. PMID: 26610600
the presynaptic vesicle protein CSPalpha is a key player in synaptic degeneration and protection in Alzheimer's disease. PMID: 25631211
Missense mutations in DNAJC5 does not play a major role in PD in the Chinese population. PMID: 24126164
Results indicate of a p.L116del mutation in DNAJC5 from families with autosomal dominant Kufs disease. PMID: 22978711
Palmitoylation-induced aggregation of mutant CSP-alpha proteins may underlie the development of adult-onset neuronal ceroid lipofuscinosis PMID: 22902780
association of DNAJC5 mutations with autosomal dominant Kufs disease PMID: 22235333
This is the first replication study of the identification of DNAJC5 as the disease-causing gene for autosomal dominant ANCL. The identification of the novel gene in ANCL will allow us to gain a better understanding of the pathological mechanism of ANCLs PMID: 22073189
A neuroprotective role for CSPalpha in humans is confirmed. PMID: 21820099
First evidence that CSP and HSP70, and their interactions with MARCKS, are involved in mucin secretion from airway epithelium. PMID: 18314541
Csp not only regulates the exit of CFTR from the ER, but this action is accompanied by Hsc70/Hsp70 and CHIP-mediated CFTR degradation. PMID: 19098309
Csp has a role in regulated CFTR trafficking at the plasma membrane. [CYSTEINE STRING PROTEIN] PMID: 12039948
Cysteine string protein inhibits N-type calcium channels, but is blocked by mutant huntingtin PMID: 14570907
CSP modulates G protein function by preferentially targeting the inactive GDP-bound form of G alpha(s) and promoting GDP/GTP exchange; the guanine nucleotide exchange activity of full-length CSP is regulated by Hsc70-SGT PMID: 15972823
Cysteine string protein monitors late steps in cystic fibrosis transmembrane conductance regulator biogenesis PMID: 16469739
palmitoylation of CSP is enhanced specifically by co-expression of the Golgi-localized palmitoyl transferases DHHC3, DHHC7, DHHC15, or DHHC17 PMID: 18596047
Has a role in exocytosis of large dense core vesicles. PMID: 10194413

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.