Recombinant Human DnaJ homolog subfamily C member 10 (DNAJC10)

Code CSB-YP809006HU
MSDS
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Source Yeast
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Code CSB-EP809006HU
MSDS
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Source E.coli
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Code CSB-EP809006HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP809006HU
MSDS
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Source Baculovirus
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Code CSB-MP809006HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
DNAJC10
Uniprot No.
Alternative Names
DNAJC10; ERDJ5; UNQ495/PRO1012DnaJ homolog subfamily C member 10; EC 1.8.4.-; Endoplasmic reticulum DNA J domain-containing protein 5; ER-resident protein ERdj5; ERdj5; Macrothioredoxin; MTHr
Species
Homo sapiens (Human)
Expression Region
33-793
Target Protein Sequence
DQDFYSLL GVSKTASSRE IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWNYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL WTGNFVNSIQ TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF ELLSANTLED RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR FDCSSAPDIC SNLYVFQPSL AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPANDKEP WLVDFFAPWC PPCRALLPEL RRASNLLYGQ LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH HSAEQILEFI EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYHYHSY NGWNRDAYSL RIWGLGFLPQ VSTDLTPQTF SEKVLQGKNH WVIDFYAPWC GPCQNFAPEF ELLARMIKGK VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF YERAKRNFQE EQINTRDAKA IAALISEKLE TLRNQGKRNK DEL
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress.
Gene References into Functions
  1. Role of ERdj5 conformational dynamics in endoplasmic reticulum associated degradation PMID: 28479060
  2. ERdj5 is a member of the proteostasis network that regulates rod opsin biogenesis and supports a role for disulfide bond formation/reduction in rod opsin biogenesis and disease. PMID: 25055872
  3. ERdj5, by binding to Sel1L, triggers BiP-Cholera toxin interaction proximal to the Hrd1 complex; postulate this scenario enables the Hrd1-associated retrotranslocation machinery to capture the toxin efficiently once the toxin is released from BiP PMID: 23363602
  4. ERdj5 acts as the endoplasmic reticulum reductase, both preparing misfolded proteins for degradation and catalyzing the folding of proteins that form obligatory non-native disulfides. PMID: 23769672
  5. ERdj5 is a ubiquitous protein localized in the ER and is particularly abundant in secretory cells. Its transcription is induced during ER stress, suggesting potential roles for ERdj5 in protein folding and translocation across the ER membrane. PMID: 12411443
  6. JPDI may have roles in folding of some proteins in the ER, chaperoning by BiP and formation of proper disulfide bonds PMID: 12446677
  7. The organization of the functional motifs of hMTHr suggests that the protein might be a member of a molecular chaperone family. PMID: 14587667
  8. ERdj4 and ERdj5 promote turnover of misfolded SP-C and this activity is dependent on their ability to stimulate BiP ATPase activity. PMID: 18400946
  9. study found that an endoplasmic reticulum (ER) protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins & accelerated ER-associated degradation through its physical and functional associations with EDEM & BiP PMID: 18653895
  10. ERdj5 decreases neuroblastoma cell survival by down-regulating the UPR, raising the possibility that this protein could be a target for anti-tumor approaches. PMID: 19122239

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Subcellular Location
Endoplasmic reticulum lumen.
Database Links

HGNC: 24637

OMIM: 607987

KEGG: hsa:54431

STRING: 9606.ENSP00000264065

UniGene: Hs.516632

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