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AB69408

Anti-HSPA6 antibody

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(4 Publications)

Rabbit Polyclonal HSPA6 antibody. Suitable for WB and reacts with Human samples. Cited in 4 publications. Immunogen corresponding to Synthetic Peptide within Human HSPA6 conjugated to Keyhole Limpet Haemocyanin.

View Alternative Names

HSP70B', HSPA6, HSP70B, Heat shock 70 kDa protein 6, Heat shock 70 kDa protein B', Heat shock protein family A member 6

1 Images
Western blot - Anti-HSPA6 antibody (AB69408)
  • WB

Unknown

Western blot - Anti-HSPA6 antibody (AB69408)

All lanes:

Western blot - Anti-HSPA6 antibody (ab69408) at 1/1000 dilution

Lane 1:

Cell lysates prepared from untreated human Hela cells

Lane 2:

Cell lysates prepared from heat shock treated (2hrs) Hela cells

Predicted band size: 71 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Synthetic Peptide within Human HSPA6 conjugated to Keyhole Limpet Haemocyanin. The exact immunogen used to generate this antibody is proprietary information.

P17066

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1 µg/mL", "WB-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
Preservative: 0.09% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
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
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The HSPA6 protein also known as Heat Shock 70kDa Protein 6 plays an important role in cellular stress response. It has a molecular weight of approximately 70 kDa. HSPA6 belongs to the heat shock protein 70 family which helps cells cope with stress by functioning as molecular chaperones. This protein is expressed in various tissues but is notably upregulated in response to heat shock and other stress conditions. HSPA6 assists in maintaining protein homeostasis by preventing the aggregation of unfolded proteins and assisting in the refolding process.
Biological function summary

Heat Shock 70kDa Protein 6 acts as a molecular chaperone and facilitates the stabilization and proper folding of unfolded or misfolded proteins under stress conditions. It operates independently and does not appear to form part of a larger protein complex unlike some other heat shock proteins. HSPA6 helps cells recover from stress damage by transporting proteins across cellular membranes and aiding in the assembly of multiprotein complexes. This function is important for maintaining cellular integrity especially during and after exposure to stressors.

Pathways

Heat Shock 70kDa Protein 6 plays a role in the cellular stress response pathway. It synergistically collaborates with other heat shock proteins like HSP70 and HSP90 which are important in protein folding and protection against stress-induced damage. Additionally HSPA6 interacts within the unfolded protein response pathway a critical mechanism in the endoplasmic reticulum to manage stress. This relationship with other heat shock proteins and pathways allows cells to maintain function and resilience under stress.

Heat Shock 70kDa Protein 6 has links to conditions associated with cellular stress including neurodegenerative diseases such as Alzheimer’s disease. Misfolded proteins are a hallmark of such diseases and HSPA6’s chaperoning functions are relevant to these pathological processes. Additionally HSPA6 has been studied in the context of cancer where its expression can be altered due to the high metabolic and replication stress experienced by tumors. In these disorders HSPA6 works alongside HSP70 to combat the accumulation of misfolded proteins and preserve cellular health.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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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).
See full target information HSPA6
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Publications (4)

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

Frontiers in cell and developmental biology 9:660576 PubMed34041241

2021

Long Noncoding RNA Activates Canonical Wnt/β-Catenin Signaling Through Small Heat Shock Proteins HSPA6 and CRYAB.

Applications

Unspecified application

Species

Unspecified reactive species

Jingjing Fa,Xiaoqing Zhang,Xiaoping Zhang,Ming Qi,Xingyu Zhang,Qihua Fu,Zhuoming Xu,Yunqian Gao,Bo Wang

Molecular cancer 20:68 PubMed33853613

2021

CircPTPRA blocks the recognition of RNA N-methyladenosine through interacting with IGF2BP1 to suppress bladder cancer progression.

Applications

Unspecified application

Species

Unspecified reactive species

Fei Xie,Chao Huang,Feng Liu,Hui Zhang,Xingyuan Xiao,Jiayin Sun,Xiaoping Zhang,Guosong Jiang

Oxidative medicine and cellular longevity 2019:1659468 PubMed31281566

2019

Oxidative Stress Induced by the Deubiquitinase Inhibitor b-AP15 Is Associated with Mitochondrial Impairment.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaonan Zhang,Belén Espinosa,Amir Ata Saei,Padraig D'Arcy,Roman A Zubarev,Stig Linder

The Journal of pharmacology and experimental thera 365:291-300 PubMed29523700

2018

Total RNA Sequencing of Rett Syndrome Autopsy Samples Identifies the M Muscarinic Receptor as a Novel Therapeutic Target.

Applications

Unspecified application

Species

Unspecified reactive species

Rocco G Gogliotti,Nicole M Fisher,Branden J Stansley,Carrie K Jones,Craig W Lindsley,P Jeffrey Conn,Colleen M Niswender
View all publications
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