Thermo Fisher Scientific HSPE1 Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

0.1-0.5 µg/mL

-

Immunohistochemistry (Paraffin) (IHC (P))

0.5-1 µg/mL

-

Immunocytochemistry (ICC/IF)

5 µg/mL

-

Flow Cytometry (Flow)

1-3 µg/1x10^6 cells

-

Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

A synthetic peptide corresponding to a sequence at the C-terminus of human Cpn10 (81-102aa VVLDDKDYFLFRDGDILGKYVD). if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:HSPE1,uniProtId:P61604-1,ncbiNodeId:9606,antigenRange:81-102,antigenLength:102,antigenImageFileName:PA5-79415_HSPE1_P61604-1_Rabbit.svg,antigenImageFileNamePDP:PA5-79415_HSPE1_P61604-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Concentration

500 µg/mL

Purification

Antigen affinity chromatography

Storage buffer

PBS with 5mg BSA

Contains

0.05mg sodium azide, 0.05mg thimerosal

Storage conditions

-20°C

Shipping conditions

Ambient (domestic); Wet ice (international)

RRID

AB_2746531

Product Specific Information

Reconstitute with 0.2 mL of distilled water to yield a concentration of 500 µg/mL.

Target Information

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the low molecular weight HSPs, the immunophilins and the HSP 110 family. The low molecular weight family includes HSP 10, HSP 20, HSP 27 (Heme Oxygenase 1), HSP 32 and HSP 40. Chaperonins are ubiquitous, indispensable proteins that facilitate protein folding in an ATP-dependent manner, enhancing the yield of properly folded substrate protein under conditions where spontaneous folding does not occur. Chaperonins are typified by the E. coli heat-shock proteins GroEL and GroES (HSP 10). HSP 10 is a heptameric ring of identical 10 kDa subunits that binds to each end of GroEL to form a symmetric, functional heterodimer.

⚠WARNING: This product can expose you to chemicals including mercury, which is known to the State of California to cause birth defects or other reproductive harm. For more information go to www.P65Warnings.ca.gov.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.