JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB89366

Recombinant Human HSPA6 protein (His tag N-Terminus)

Be the first to review this product! 리뷰 제출

|

(0 출판물)

Recombinant Human HSPA6 protein (His tag N-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
1 이미지
SDS-PAGE - Recombinant Human HSPA6 protein (His tag N-Terminus) (AB89366)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human HSPA6 protein (His tag N-Terminus) (AB89366)

15% SDS-PAGE showing ab89366 at approximately 73.2kDa (3μg).

주요 정보

Purity

>90% SDS-PAGE

ab89366 is purified using conventional chromatography techniques.

발현 시스템

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P17066-1

Animal free

No

Carrier free

No

Species

Human

보관 버퍼

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl

storage-buffer

style
left-column

보완 제품

Reagents, Controls & Accessories

AB313996

Prestained Protein Ladder - Extra broad molecular weight (3 - 260 kDa)

SDS-PAGE - Prestained Protein Ladder - Extra broad molecular weight (3 - 260 kDa) (AB313996)

  • 0
  • 0
Proteins & Peptides

AB134607

Recombinant Human C1orf33 protein (His tag N-Terminus)

SDS-PAGE - Recombinant Human C1orf33 protein (His tag N-Terminus) (AB134607)

  • 0
  • 0
Primary Antibodies

AB212044

Anti-HSPA6 antibody

Immunocytochemistry/ Immunofluorescence - Anti-HSPA6 antibody (AB212044)

  • 0
  • 0
Primary Antibodies

AB4729

Anti-Histone H3 (acetyl K27) antibody - ChIP Grade

BOND RX™ Validated

ChIP - Anti-Histone H3 (acetyl K27) antibody - ChIP Grade (AB4729)

  • 5
  • 85
Primary Antibodies

AB9049

Anti-Histone H3 (di methyl K36) antibody - ChIP Grade

BOND RX™ Validated

ChIP - Anti-Histone H3 (di methyl K36) antibody - ChIP Grade (AB9049)

  • 5
  • 24
style
left-column

Reactivity 정보

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

서열 정보

[{"linker":null,"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P17066","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
style
left-column

특성 및 보관 정보

제형
Liquid
배송 시 보관 조건
Blue Ice
적절한 단기 보관 조건
-20°C
적절한 장기 보관 조건
-20°C
분주 정보
Upon delivery aliquot
보관 정보
Avoid freeze / thaw cycle
False
style
left-column

추가 정보

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.
style
left-column

일반 정보

기능

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).

서열 유사성

Belongs to the heat shock protein 70 family.

style
left-column

제품 프로토콜

style
left-column

타겟 정보

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

대체 명칭 보기

HSP70B', HSPA6, HSP70B, Heat shock 70 kDa protein 6, Heat shock 70 kDa protein B', Heat shock protein family A member 6
style
left-column
style
left-column
style
right-column

Product promise

저희는 고품질 시약으로 고객님의 연구를 서포트하고자 최선을 다하고 있으며, 모든 단계에서 함께 하겠습니다. 만약 제품이 기대한 성능을 보이지 않을 경우에도 Product Promise로 보호받으실 수 있습니다.
자세한 내용은 이용 약관을 확인해 주세요.

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com