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AB174846

Anti-HSPA2 antibody [EPR4596-27]

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(1 Publication)

Rabbit Recombinant Monoclonal HSPA2 antibody. Suitable for WB and reacts with Human samples. Cited in 1 publication.

View Alternative Names

Heat shock-related 70 kDa protein 2, Heat shock 70 kDa protein 2, Heat shock protein family A member 2, HSPA2

1 Images
Western blot - Anti-HSPA2 antibody [EPR4596-27] (AB174846)
  • WB

Supplier Data

Western blot - Anti-HSPA2 antibody [EPR4596-27] (AB174846)

All lanes:

Western blot - Anti-HSPA2 antibody [EPR4596-27] (ab174846) at 1/1000 dilution

Lane 1:

MCF7 cell lysate at 10 µg

Lane 2:

HeLa cell lysate at 10 µg

Lane 3:

Jurkat cell lysate at 10 µg

Lane 4:

A431 cell lysates at 10 µg

Predicted band size: 70 kDa

false

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR4596-27

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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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
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: 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.

HSPA2 also known as Heat Shock Protein Family A (Hsp70) Member 2 serves as a molecular chaperone. It assists in the folding of nascent polypeptides and protection of proteins under stress. The protein has a mass of approximately 70 kilodaltons (kDa). You can find HSPA2 expressed in various tissues including the testes which suggests a role in sperm maturation and fertilization. Its expression is also notable in other tissues under stress conditions.
Biological function summary

This chaperone protein plays a role in spermatogenesis by ensuring the proper folding and functioning of sperm proteins. HSPA2 is not part of a larger protein complex but acts in coordination with co-chaperones to exert its functions. Its activities contribute to sperm development and viability impacting male fertility. HSPA2 also provides cellular protection in response to different stress stimuli such as increased temperature and toxic substances.

Pathways

HSPA2 participates in the protein folding pathway and stress response pathway. Its precise chaperone action is important for maintaining protein homeostasis; thereby it influences cellular health. In the stress response pathway HSPA2 interacts with other heat shock proteins such as HSP90AA1 coordinating to mitigate damage from cytotoxic stressors. This interaction helps to stabilize and refold misfolded proteins while facilitating their repair or degradation.

HSPA2's role in fertility and cell protection connects it to infertility and cancer. Research indicates abnormalities in HSPA2 function are associated with male infertility due to improper protein folding critical for sperm function. Similarly alterations in HSPA2 expression link to cancer progression where its regulation could impact cell survival and proliferation. Within these diseases HSPA2 interacts with proteins like tumor suppressors p53 highlighting its complex involvement in cellular responses.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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).
See full target information Heat shock-related 70 kDa protein 2

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Aging cell 21:e13707 PubMed36087066

2022

The lysosomal proteome of senescent cells contributes to the senescence secretome.

Applications

Unspecified application

Species

Unspecified reactive species

Miguel Rovira,Rebecca Sereda,David Pladevall-Morera,Valentina Ramponi,Ines Marin,Mate Maus,Julio Madrigal-Matute,Antonio Díaz,Fernando García,Javier Muñoz,Ana María Cuervo,Manuel Serrano
View all publications

Product promise

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For full details, please see our Terms & Conditions

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