Thermo Fisher Scientific HSPE1 Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500-1:3,000

-

Immunohistochemistry (Paraffin) (IHC (P))

1:50-1:200

-

Immunocytochemistry (ICC/IF)

1:100-1:500

-

Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

A synthesized peptide derived from human HSPE1(Accession P61604), corresponding to amino acid residues I60-D102. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:HSPE1,uniProtId:P61604-1,ncbiNodeId:9606,antigenRange:60-102,antigenLength:102,antigenImageFileName:PA5-99171_HSPE1_P61604-1_Rabbit.svg,antigenImageFileNamePDP:PA5-99171_HSPE1_P61604-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Affinity chromatography

Storage buffer

PBS, pH 7.4, with 50% glycerol

Contains

0.02% sodium azide

Storage conditions

-20°C

Shipping conditions

Wet ice

RRID

AB_2818104

Product Specific Information

Antibody detects endogenous levels of total HSP10.

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.

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