Human Recombinant HSPA9 protein, GST Tag (V2LY-0526-LY4600)

Name: Human Recombinant HSPA9 protein, GST Tag
SKU: V2LY-0526-LY4600
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

Baculovirus-Insect Cells

Protein Species

Human

Tag

GST Tag

Protein Construction

This product is Human Recombinant HSPA9 protein, GST Tag consist of Amino Acid: 47-end and predicts a molecular mass of 97 kDa.

Molecule Mass

97 kDa

Sequence

Amino Acid: 47-end

Species

Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity

Batch dependent.

Endotoxin

Please contact us for more information.

Format

Liquid

Preservative

None

Storage

Store product at -70°C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

More Infomation

Target

Full Name

Heat Shock Protein Family A (Hsp70) Member 9

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 the control of cell proliferation and cellular aging (By similarity).

Biological Process

Cellular response to unfolded protein Source: GO_Central
Chaperone cofactor-dependent protein refolding Source: GO_Central
Erythrocyte differentiation Source: UniProtKB
Inner mitochondrial membrane organization Source: UniProtKB
Iron-sulfur cluster assembly Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of erythrocyte differentiation Source: UniProtKB
Negative regulation of hematopoietic stem cell differentiation Source: Ensembl
Negative regulation of hemopoiesis Source: Ensembl
Protein export from nucleus Source: Ensembl
Protein refolding Source: GO_Central
Regulation of erythrocyte differentiation Source: UniProtKB

Cellular Location

Mitochondrion; Nucleolus

Involvement in disease

Anemia, sideroblastic, 4 (SIDBA4):
A form of sideroblastic anemia, a bone marrow disorder defined by the presence of pathologic iron deposits in erythroblast mitochondria. Sideroblastic anemia is characterized by anemia of varying severity, hypochromic peripheral erythrocytes, systemic iron overload secondary to chronic ineffective erythropoiesis, and the presence of bone marrow ringed sideroblasts. Sideroblasts are characterized by iron-loaded mitochondria clustered around the nucleus. SIDBA4 has been reported to be inherited as an autosomal recessive disease, with a pseudodominant pattern of inheritance in some families.
Even-plus syndrome (EVPLS):
An autosomal recessive syndrome characterized by epiphyseal and vertebral dysplasia, prenatal-onset short stature, a distinct craniofacial phenotype with microtia, a flat facial profile with flat nose and triangular nares, cardiac malformations, and additional findings such as anal atresia, hypodontia, aplasia cutis, and others.

Elwakeel, A. (2022). Abrogating the interaction between p53 and mortalin (Grp75/HSPA9/mtHsp70) for cancer therapy: The story so far. Frontiers in Cell and Developmental Biology, 10, 879632.

Liu, X., Teng, Z., Wang, Z., Zhu, P., Song, Z., & Liu, F. (2022). Expressions of HSPA1L and HSPA9 are associated with poor sperm quality of low‐motility spermatozoa in fertile men. Andrologia, 54(2), e14321.

Guan, Y., Zhu, X., Liang, J., Wei, M., Huang, S., & Pan, X. (2021). Upregulation of HSPA1A/HSPA1B/HSPA7 and downregulation of HSPA9 were related to poor survival in colon cancer. Frontiers in oncology, 11, 749673.

Wu, P. K., Hong, S. K., Chen, W., Becker, A. E., Gundry, R. L., Lin, C. W., ... & Park, J. I. (2020). Mortalin (HSPA9) facilitates BRAF-mutant tumor cell survival by suppressing ANT3-mediated mitochondrial membrane permeability. Science signaling, 13(622), eaay1478.

Jo, D. S., Park, S. J., Kim, A. K., Park, N. Y., Kim, J. B., Bae, J. E., ... & Cho, D. H. (2020). Loss of HSPA9 induces peroxisomal degradation by increasing pexophagy. Autophagy, 16(11), 1989-2003.

Wu, P. K., Hong, S. K., Starenki, D., Oshima, K., Shao, H., Gestwicki, J. E., ... & Park, J. I. (2020). Mortalin/HSPA9 targeting selectively induces KRAS tumor cell death by perturbing mitochondrial membrane permeability. Oncogene, 39(21), 4257-4270.

Starenki, D., Sosonkina, N., Hong, S. K., Lloyd, R. V., & Park, J. I. (2019). Mortalin (GRP75/HSPA9) promotes survival and proliferation of thyroid carcinoma cells. International journal of molecular sciences, 20(9), 2069.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

For research use only. Not intended for any clinical use.

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