| SKU | Size | Availability | Price | Qty |
|---|---|---|---|---|
| rp170125-10μg (Trial Size) Apply for free trial size（?） Every year, as a valued customer, you have the exclusive opportunity to explore and enjoy three different trial products of your choice, absolutely free! | 10μg | In stock | $59.90 | |
| rp170125-50μg | 50μg | In stock | $139.90 | |
| rp170125-100μg | 100μg | In stock | $219.90 | |
| rp170125-1mg | 1mg | Available within 8-12 weeks(?) Production requires sourcing of materials. We appreciate your patience and understanding. | $1,699.90 |
Carrier Free, >95% SDS-PAGE, E.coli, N-His tag, 47-679 aa
| Product Name | Recombinant Human Grp75/MOT Protein, >95% SDS-PAGE, high purity |
|---|---|
| Synonyms | 75 kDa glucose regulated protein; 75 kDa glucose-regulated protein; CSA; Glucose Regulated Protein; Grp 75; GRP-75; GRP75; GRP75_HUMAN; Heat shock 70 kDa protein 9; Heat shock 70kD protein 9; heat shock 70kDa protein 9; Heat shock 70kDa protein 9B; Heat s |
| Grade | Azide Free, Carrier Free |
| Product Description | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining. |
| Specifications & Purity | Carrier Free, Azide Free, ≥95%(SDS-PAGE) |
| Purity | >95% SDS-PAGE |
| Endotoxin Concentration | ＜1.0 EU/μg |
| Expression System | E. coli |
| Amino Acids | 47-679 aa |
| Sequence | MGSSHHHHHHSSGLVPRGSHASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQA |
| Protein Tag | N-His |
| Predicted molecular weight | 70.9 kDa |
| SDS-PAGE | 70.5 kDa, reducing conditions; 70.5 kDa, non-reducing conditions |
Recombinant Human Grp75/MOT protein (rp170125) - SDS-PAGE
Recombinant Human Grp75/MOT protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 70.5 kDa.
| Form | Transparent gelatinous |
|---|---|
| Reconstitution | We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 0.5 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilu |
| Storage Temp | Store at -20°C,Avoid repeated freezing and thawing |
| Shipped In | Ice chest + Ice pads |
| Stability And Storage | Store at -20°C stable up to 1 year. Avoid freeze / thaw cycle. |
Enter Lot Number to search for COA:
To view the certificate results,please click on a Lot number.For Lot numbers from past orders,please use our order status section
| Lot Number | Certificate Type | Date | Item |
|---|---|---|---|
 ZJ23F1101777 | Certificate of Analysis | Dec 01, 2023 | rp170125 |
| ZJ23F1101776 | Certificate of Analysis | Dec 01, 2023 | rp170125 |
| ZJ23F1101775 | Certificate of Analysis | Dec 01, 2023 | rp170125 |
| ZJ23R1100125 | Certificate of Analysis | Nov 14, 2023 | rp170125 |
| 1. Hochstrasser, D F DF and 9 more authors.. (1992) Human liver protein map: a reference database established by microsequencing and gel comparison.. Electrophoresis, [PMID:1286669] |
| 2. Domanico, S Z SZ, DeNagel, D C DC, Dahlseid, J N JN, Green, J M JM and Pierce, S K SK.. (1993) Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family.. Molecular and cellular biology, [PMID:7684501] |
| 3. Bhattacharyya, T T and 6 more authors.. (1995) Cloning and subcellular localization of human mitochondrial hsp70.. The Journal of biological chemistry, (27): [PMID:7829505] |
| 4. Hughes, G J GJ and 8 more authors.. (1993) Human liver protein map: update 1993.. Electrophoresis, [PMID:8313870] |
| 5. Ji, H H and 5 more authors.. () A two-dimensional gel database of human colon carcinoma proteins.. Electrophoresis, [PMID:9150948] |
| 6. Andersen, Jens S JS and 5 more authors.. (2003) Proteomic characterization of the human centrosome by protein correlation profiling.. Nature, (4): [PMID:14654843] |
| 7. Shan, Yuxi Y, Napoli, Eleonora E and Cortopassi, Gino G.. (2007) Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones.. Human molecular genetics, (15): [PMID:17331979] |
| 8. Uhrigshardt, Helge H, Singh, Anamika A, Kovtunovych, Gennadiy G, Ghosh, Manik M and Rouault, Tracey A TA.. (2010) Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis.. Human molecular genetics, (1): [PMID:20668094] |
| 9. Chen, Tim H-P TH and 6 more authors.. (2011) Knockdown of Hspa9, a del(5q31.2) gene, results in a decrease in hematopoietic progenitors in mice.. Blood, (3): [PMID:21123823] |
| 10. Peng, Chao C and 18 more authors.. (2011) The first identification of lysine malonylation substrates and its regulatory enzyme.. Molecular & cellular proteomics : MCP, [PMID:21908771] |
| 11. Ahmad, Yasmeen; Boisvert, Francois-Michel; Lundberg, Emma; Uhlen, Mathias and Lamond, Angus I.. (2012) Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization.. Molecular & cellular proteomics : MCP, [PMID:22002106] |
| 12. Alkhaja, Alwaleed K AK and 10 more authors.. (2012) MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization.. Molecular biology of the cell, [PMID:22114354] |
| 13. Dores-Silva, P R PR, Minari, K K, Ramos, C H I CH, Barbosa, L R S LR and Borges, J C JC.. (2013) Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone.. International journal of biological macromolecules, [PMID:23462535] |
| 14. Matsuzaki, Hiroshi H, Fujimoto, Takahiro T, Tanaka, Masatoshi M and Shirasawa, Senji S.. (2013) Tespa1 is a novel component of mitochondria-associated endoplasmic reticulum membranes and affects mitochondrial calcium flux.. Biochemical and biophysical research communications, (12): [PMID:23501103] |
| 15. Tsuneki, Masayuki M and 9 more authors.. (2013) Extracellular heat shock protein A9 is a novel interaction partner of podoplanin in oral squamous cell carcinoma cells.. Biochemical and biophysical research communications, (26): [PMID:23541579] |
| 16. Cai, Kai K and 5 more authors.. (2013) Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU).. The Journal of biological chemistry, (4): [PMID:23940031] |
| 17. Guo, Ailan and 15 more authors.. (2014) Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.. Molecular & cellular proteomics : MCP, [PMID:24129315] |
| 18. Schmitz-Abe, Klaus K and 27 more authors.. (2015) Congenital sideroblastic anemia due to mutations in the mitochondrial HSP70 homologue HSPA9.. Blood, (17): [PMID:26491070] |
| 19. Royer-Bertrand, Beryl B and 14 more authors.. (2015) Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-PLUS syndrome of congenital malformations and skeletal dysplasia.. Scientific reports, (24): [PMID:26598328] |
| 20. Shan, Yuxi Y and Cortopassi, Gino G.. (2016) Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly.. Mitochondrion, [PMID:26702583] |
