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AB92433

Recombinant human HSPA2 protein

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Recombinant human HSPA2 protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB, FuncS.

View Alternative Names

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

2 Images
SDS-PAGE - Recombinant human HSPA2 protein (AB92433)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human HSPA2 protein (AB92433)

SDS-PAGE showing ab92433 :
Lane 1 : 0.5μg
Lane 2 : 1μg
Lane 3 : 2μg
Lane 4 : 5μg

Western blot - Recombinant human HSPA2 protein (AB92433)
  • WB

Unknown

Western blot - Recombinant human HSPA2 protein (AB92433)

All lanes:

anti-HSPA2

Lane 1:

Western blot - Recombinant human HSPA2 protein (ab92433) at 0.05 µg

Lane 2:

DnaK protein at 0.05 µg

false

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE, FuncS, WB

applications

Biologically active

Yes

Biological activity

ATPase activity: Positive

Accession

P54652

Animal free

No

Carrier free

No

Species

Human

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Primary Antibodies

AB108416

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Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-HSPA2 antibody [EPR4596] (AB108416)

  • 5
  • 1
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Primary Antibodies

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Anti-VCP antibody [EPR3307(2)]

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Western blot - Anti-VCP antibody [EPR3307(2)] (AB109240)

  • 4
  • 1
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

Endotoxin: >500 EU/mg as determined by LAL gel clot assay
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P54652","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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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.
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Specifications

Form

Liquid

Additional notes

Purified by Multi-step chromatography.> 95% pure as determined by SDS-PAGE and Western Blot analysis.

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General info

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).

Sequence similarities

Belongs to the heat shock protein 70 family.

Subcellular localisation

Cytoskeleton

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Product protocols

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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). 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
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