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BRAND / VENDOR: Abcam

Abcam, ab200838, Anti-HSPA12A antibody [EPR16763]

CATALOG NUMBER: ab200838
Regular price$0.99
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Product Description

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal HSPA12A antibody. Suitable for IP, WB, ICC/IF, IHC-P and reacts with Human, Mouse, Rat samples. Cited in 3 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR16763,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Rat, Human,
Applications:IHC-P, IP, WB, ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
HSPA12A also known as Heat Shock Protein Family A (Hsp70) Member 12A is a member of the Hsp70 family of proteins involved in stress response. This protein has an approximate molecular mass of 80 kDa. HSPA12A shows expression predominantly in endothelial cells where it plays a significant role. Like other Hsp70 proteins it assists in protein folding assembly and transport within cells. HSPA12A's activity supports the maintenance of cellular proteostasis under stress conditions facilitating correct protein conformation and preventing aggregation.
Biological function summary
HSPA12A participates in processes that maintain vascular homeostasis. It may be involved in a complex with other Hsp70 proteins to provide cellular protection against various stressors. The precise composition and roles of these complexes remain under investigation. Its activity as a molecular chaperone helps protect cells from apoptosis and supports the repair of damaged proteins which is important for normal cell function and survival in stressful environments.
Pathways
HSPA12A is involved in key pathways related to cellular stress responses and cytoprotection. It interacts with signaling pathways such as the unfolded protein response and the oxidative stress response. These pathways include interactions with other chaperone proteins like Hsp90 that facilitate cellular adaptation to adverse conditions. Its involvement in these pathways suggests that HSPA12A plays a role in regulating cellular stress mechanisms and promoting recovery after stress exposure.
HSPA12A appears to have a connection to cardiovascular diseases and certain neurodegenerative disorders. In cardiovascular diseases its expression in endothelial cells suggests it may contribute to vascular integrity and function. Furthermore HSPA12A may have connections to neurodegenerative disorders as it assists in protecting neurons from protein aggregation and apoptosis. These links might involve interactions with proteins like alpha-synuclein where its chaperone role could influence the disease progression. Understanding these relationships could provide new insights into therapeutic strategies targeting these disorders.


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Collaboration

Tony Tang

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