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Mouse Anti-HSPA2 Recombinant Antibody (CAP897) (CBMAB-AP2710LY)

Summary

Host Animal
Mouse
Specificity
Rat
Clone
CAP897
Antibody Isotype
IgG
Application
ICC, IHC, IP, WB

Basic Information

Immunogen
Met1~Asp633
Specificity
Rat
Antibody Isotype
IgG
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
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 2
Introduction
HSPA2 (Heat Shock Protein Family A (Hsp70) Member 2) is a Protein Coding gene. Diseases associated with HSPA2 include Inflammatory Bowel Disease 3 and Papillary Cystadenocarcinoma. Among its related pathways are Meiosis and MAPK signaling pathway. Gene Ontology (GO) annotations related to this gene include enzyme binding and glycolipid binding. An important paralog of this gene is HSPA8.
Entrez Gene ID
UniProt ID
Alternative Names
Heat Shock Protein Family A (Hsp70) Member 2; Heat Shock 70kDa Protein 2; Heat Shock 70kD Protein 2; Heat Shock-Related 70 KDa Protein 2; Heat Shock 70 KDa Protein 2; HSP70-2; HSP70-3;
Function
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365).

Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity).
Biological Process
Cellular response to unfolded protein Source: GO_Central
Chaperone cofactor-dependent protein refolding Source: GO_Central
Male meiosis I Source: Ensembl
Male meiotic nuclear division Source: ProtInc
Negative regulation of inclusion body assembly Source: UniProtKB
Positive regulation of ATPase activity Source: Ensembl
Positive regulation of ATPase-coupled calcium transmembrane transporter activity Source: Ensembl
Positive regulation of G2/M transition of mitotic cell cycle Source: Ensembl
Positive regulation of protein phosphorylation Source: Ensembl
Protein refolding Source: UniProtKB
Response to cold Source: AgBase
Response to heat Source: AgBase
Response to unfolded protein Source: ProtInc
Spermatid development Source: ProtInc
Spermatogenesis Source: UniProtKB
Synaptonemal complex disassembly Source: Ensembl
Vesicle-mediated transport Source: GO_Central
Cellular Location
Spindle. Colocalizes with SHCBP1L at spindle during the meiosis process.

Nowicka-Bauer, K., Malcher, A., Włoczkowska, O., Kamieniczna, M., Olszewska, M., & Kurpisz, M. K. (2022). Evaluation of seminal plasma HSPA2 protein as a biomarker of human spermatogenesis status. Reproductive Biology, 22(1), 100597.

Zhang, W., Shi, B., Li, S., Liu, Z., Li, S., Dong, S., ... & Zhong, M. (2022). Sleeve gastrectomy improves lipid dysmetabolism by downregulating the USP20-HSPA2 axis in diet-induced obese mice. Frontiers in Endocrinology, 13, 1041027.

Dong, Y., Li, T., Ma, Z., Zhou, C., Wang, X., & Li, J. (2022). HSPA1A, HSPA2, and HSPA8 are potential molecular biomarkers for prognosis among HSP70 family in alzheimer’s disease. Disease Markers, 2022.

Panitch, R., Hu, J., Chung, J., Zhu, C., Meng, G., Xia, W., ... & Jun, G. R. (2021). Integrative brain transcriptome analysis links complement component 4 and HSPA2 to the APOE ε2 protective effect in Alzheimer disease. Molecular psychiatry, 26(10), 6054-6064.

Huerta-Retamal, N., Sáez-Espinosa, P., Robles-Gómez, L., Avilés, M., Romero, A., Aizpurua, J., & Gómez-Torres, M. J. (2021). Human sperm chaperone HSPA2 distribution during in vitro capacitation. Journal of reproductive immunology, 143, 103246.

Yang, Y. L., Zhang, Y., Li, D. D., Zhang, F. L., Liu, H. Y., Liao, X. H., ... & Shao, Z. M. (2020). RNF144A functions as a tumor suppressor in breast cancer through ubiquitin ligase activity-dependent regulation of stability and oncogenic functions of HSPA2. Cell Death & Differentiation, 27(3), 1105-1118.

Sojka, D. R., Gogler-Pigłowska, A., Vydra, N., Cortez, A. J., Filipczak, P. T., Krawczyk, Z., & Scieglinska, D. (2019). Functional redundancy of HSPA1, HSPA2 and other HSPA proteins in non-small cell lung carcinoma (NSCLC); an implication for NSCLC treatment. Scientific Reports, 9(1), 14394.

Cao, L., Yuan, X., Bao, F., Lv, W., He, Z., Tang, J., ... & Hu, J. (2019). Downregulation of HSPA2 inhibits proliferation via ERK1/2 pathway and endoplasmic reticular stress in lung adenocarcinoma. Annals of Translational Medicine, 7(20).

Seify, M., Zarabadipour, M., Ghaleno, L. R., Alizadeh, A., & Valojerdi, M. R. (2019). The anti-oxidant roles of Taurine and Hypotaurine on acrosome integrity, HBA and HSPA2 of the human sperm during vitrification and post warming in two different temperature. Cryobiology, 90, 89-95.

Petyuk, V. A., Chang, R., Ramirez-Restrepo, M., Beckmann, N. D., Henrion, M. Y., Piehowski, P. D., ... & Myers, A. J. (2018). The human brainome: network analysis identifies HSPA2 as a novel Alzheimer’s disease target. Brain, 141(9), 2721-2739.

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

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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