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AB316691

Recombinant Human Hsp27 Protein Standard

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Recombinant Human Hsp27 Protein Standard is a Human Full Length protein, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, sELISA.

View Alternative Names

HSP27, HSP28, HSPB1, Heat shock protein beta-1, HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, Heat shock protein family B member 1, Stress-responsive protein 27, HSP 27, SRP27

2 Images
Sandwich ELISA - Recombinant Human Hsp27 Protein Standard (AB316691)
  • sELISA

Supplier Data

Sandwich ELISA - Recombinant Human Hsp27 Protein Standard (AB316691)

Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.

SDS-PAGE - Recombinant Human Hsp27 Protein Standard (AB316691)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Hsp27 Protein Standard (AB316691)

SDS-PAGE analysis of ab316691 under reducing conditions for 2ug protein.

Key facts

Purity

>80% SDS-PAGE

Expression system

HEK 293 cells

Tags

Tag free

Applications

SDS-PAGE, sELISA

applications

Biologically active

No

Accession

P04792

Animal free

Yes

Carrier free

No

Species

Human

Storage buffer

pH: 7.3 - 7.5 Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic

storage-buffer

Reactivity data

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

Product details

While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.

Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.

The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Supportteam to know which antibody pair is suitable for this protein.

Sequence info

[{"linker":null,"sequence":null,"proteinLength":"Full Length","predictedMolecularWeight":"23.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P04792","tags":[]}]

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
False

Supplementary information

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

Hsp27 also known as HSPB1 is a small heat shock protein with a molecular weight of approximately 27 kilodaltons. This protein is expressed in various tissues including muscle heart and brain. It functions as a molecular chaperone that stabilizes unfolded proteins preventing their aggregation. Hsp27 undergoes phosphorylation at specific residues which modulates its chaperone activity and interaction with other proteins.
Biological function summary

Hsp27 plays a critical role in cellular stress response by regulating actin cytoskeleton dynamics and inhibiting apoptosis. It forms part of a complex that includes other proteins such as alphaB-crystallin. This complex facilitates the reorganization of proteins under stress conditions enhancing cell survival during oxidative stress or thermal shock. Hsp27 also modulates inflammatory responses and has been shown to affect cell migration.

Pathways

Hsp27 integrates into the apoptosis and inflammation pathways. It interacts with apoptotic machinery such as caspase proteins to protect cells by hindering apoptosome formation. Additionally Hsp27 can engage with pathways involving the nuclear factor-kappa B (NF-kB) impacting inflammatory signaling. CPTC (carboxyl-pyrene-trioctylamine) can modulate these pathways by altering Hsp27 function and interactions.

Hsp27 has connections to neurodegenerative diseases and cancer. In neurodegenerative conditions such as Alzheimer's disease its chaperone activity is thought to protect neurons from misfolded protein aggregates. In cancer Hsp27 supports tumor cell survival and resistance to chemotherapy by interacting with proteins like Akt and p53. These interactions highlight the complex role of Hsp27 in modulating cellular responses in various pathological states.

Specifications

Form

Liquid

General info

Function

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed : 10383393, PubMed : 20178975). Plays a role in stress resistance and actin organization (PubMed : 19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed : 23728742).

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Post-translational modifications

Phosphorylated upon exposure to protein kinase C activators and heat shock (PubMed:8325890). Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement (PubMed:1332886, PubMed:19166925, PubMed:8093612).

Subcellular localisation

Nucleus

Product protocols

Target data

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed : 10383393, PubMed : 20178975). Plays a role in stress resistance and actin organization (PubMed : 19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed : 23728742).
See full target information HSPB1

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