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Mouse Anti-HSPA9 Recombinant Antibody (30A5) (CBMAB-G1073-LY)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat, Pig, Cattle, Dog, Chicken, Friut fly, Guinea pig, Hamster, Rabbit, Sheep, Frog
Clone
30A5
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
Native human Grp75 (Mortalin)
Specificity
Human, Mouse, Rat, Pig, Cattle, Dog, Chicken, Friut fly, Guinea pig, Hamster, Rabbit, Sheep, Frog
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Heat Shock Protein Family A (Hsp70) Member 9
Introduction
This gene encodes a member of the heat shock protein 70 gene family. The encoded protein is primarily localized to the mitochondria but is also found in the endoplasmic reticulum, plasma membrane and cytoplasmic vesicles. This protein is a heat-shock cognate protein. This protein plays a role in cell proliferation, stress response and maintenance of the mitochondria. A pseudogene of this gene is found on chromosome 2.[provided by RefSeq, May 2010]
Entrez Gene ID
Human3313
Mouse15526
Rat291671
Guinea pig100719079
Hamster100689405
Pig100521183
Dog474697
Cattle517535
Chicken416183
Rabbit100347135
Sheep101112054
Frog407910
UniProt ID
HumanP38646
MouseP38647
RatP48721
Guinea pigH0UYD9
HamsterP86233
DogE2RAU5
PigA0A287ADJ2
CattleQ3ZCH0
RabbitG1SRF7
ChickenQ5ZM98
SheepW5Q4W8
FrogQ6NVU3
Alternative Names
Heat Shock Protein Family A (Hsp70) Member 9; Heat Shock 70kDa Protein 9 (Mortalin); 75 KDa Glucose-Regulated Protein; Peptide-Binding Protein 74; Mortalin2; Mortalin; HSPA9B; GRP-75; GRP75; PBP74; MOT; Epididymis Secretory Sperm Binding Protein Li 124m; Heat Shock 70kDa Protein 9B (Mortalin-2); Catecholamine-Regulated Protein 40; Stress-70 Protein; Mitochondrial;
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.
More Infomation

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

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