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HSPA9 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P38646 |
|---|---|
| Other Accession | NP_004125.3 |
| Clone Names | 90625099 |
| Gene ID | 3313 |
|---|---|
| Other Names | Stress-70 protein, mitochondrial, 75 kDa glucose-regulated protein, GRP-75, Heat shock 70 kDa protein 9, Mortalin, MOT, Peptide-binding protein 74, PBP74, HSPA9, GRP75, HSPA9B, mt-HSP70 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | HSPA9 (HGNC:5244) |
|---|---|
| Synonyms | GRP75, HSPA9B, mt-HSP70 |
| Function | Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (PubMed:26702583). Regulates erythropoiesis via stabilization of ISC assembly (PubMed:21123823, PubMed:26702583). May play a role in cell cycle regulation via its interaction with and promotion of degradation of TP53 (PubMed:24625977, PubMed:26634371). May play a role in the control of cell proliferation and cellular aging (By similarity). |
| Cellular Location | Mitochondrion. Nucleus, nucleolus. Cytoplasm |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of the heat shock protein 70gene family. The encoded protein is primarily localized to themitochondria but is also found in the endoplasmic reticulum, plasmamembrane and cytoplasmic vesicles. This protein is a heat-shockcognate protein. This protein plays a role in cell proliferation,stress response and maintenance of the mitochondria. A pseudogeneof this gene is found on chromosome 2.
References
Li, Y., et al. Environ. Health Perspect. 118(7):936-942(2010)Luo, W.I., et al. Protein Expr. Purif. 72(1):75-81(2010)Goswami, A.V., et al. J. Biol. Chem. 285(25):19472-19482(2010)Iosefson, O., et al. FEBS Lett. 584(6):1080-1084(2010)Rikova, K., et al. Cell 131(6):1190-1203(2007)
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