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Key Documents

HPA010023

Sigma-Aldrich

Anti-HSPA4 antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonyme(s) :

Anti-HSP70RY, Anti-Heat shock 70 kDa protein 4, Anti-Heat shock 70-related protein APG-2

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About This Item

Code UNSPSC :
12352203
Numéro HPA (Human Protein Atlas):
Nomenclature NACRES :
NA.43

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Gamme de produits

Prestige Antibodies® Powered by Atlas Antibodies

Forme

buffered aqueous glycerol solution

Espèces réactives

human, mouse, rat

Technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

Séquence immunogène

FEELGKQIQQYMKIISSFKNKEDQYDHLDAADMTKVEKSTNEAMEWMNNKLNLQNKQSLTMDPVVKSKEIEAKIKELTSTCSPIISKPKPKVEPPKEEQKNAEQNGPVDG

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... HSPA4(3308)

Description générale

HSPA4 (heat shock protein family A (Hsp70) member 4) is a chaperone protein with an activity similar to that of Hsp110, and thus, is considered to be a member of the hsp110 protein family. It is a cytoplasmic protein and is composed of a nucleotide-binding domain (NBD) and a peptide-binding domain (PBD) intervened by a flexible linker region. In adult mouse tissues, HSPA4 mRNA has a wide range of expression with the highest expression in spleen, ovary and testis.

Immunogène

Heat shock 70 kDa protein 4 recombinant protein epitope signature tag (PrEST)

Application

Anti-HSPA4 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.

Actions biochimiques/physiologiques

HSPA4 (heat shock protein family A (Hsp70) member 4) is up-regulated in breast, ovarian, pancreatic and colon cancers. It plays an essential role in the migration, invasiveness and transformation of cancer cells. It is a candidate cancer stem cells (CSCs) marker for gastric cancer. This protein is induced in response to radioactive and acidic pH stress, and is up-regulated in HCC (hepatocellular carcinoma). This protein is up-regulated by NBS1 protein, which is elevated in the chromosomal-instability syndrome called Nijmegen breakage syndrome (NBS). This protein plays a critical role in normal spermatogenesis. The over-expression of HSPA4 is related with poor prognosis in HBV (hepatitis B virus)-associated early-stage HCC.

Caractéristiques et avantages

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Liaison

Corresponding Antigen APREST71595

Forme physique

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Informations légales

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Mauricio Krause et al.
Clinical science (London, England : 1979), 128(11), 789-803 (2015-04-18)
The 70 kDa heat-shock protein (HSP70) family is important for a dynamic range of cellular processes that include protection against cell stress, modulation of cell signalling, gene expression, protein synthesis, protein folding and inflammation. Within this family, the inducible 72 kDa and
R Roufayel et al.
Cell death & disease, 5, e1546-e1546 (2014-11-28)
Protein-damaging stress stimulates cell destruction through apoptosis; however, non-lethal proteotoxic stress induces an adaptive response leading to the increased synthesis of heat shock proteins, which inhibit apoptosis. In this study, we sought to determine the mechanism responsible for the accumulation
Stefan Tukaj
Postepy higieny i medycyny doswiadczalnej (Online), 68, 722-727 (2014-06-18)
Heat shock proteins 70 (Hsp70) play an important role in maintaining cellular homeostasis. As molecular chaperones, Hsp70 are responsible for proper folding of newly synthesized polypeptides and refolding of misfolded and aggregated proteins. Hsp70 are involved in cellular transport and
Won Suk Yang et al.
Journal of proteome research, 11(2), 1078-1088 (2011-11-15)
Although doxorubicin (Doxo) and docetaxel (Docet) in combination are widely used in treatment regimens for a broad spectrum of breast cancer patients, a major obstacle has emerged in that some patients are intrinsically resistant to these chemotherapeutics. Our study aimed
Torsten Held et al.
Reproduction (Cambridge, England), 142(1), 133-144 (2011-04-14)
Heat-shock protein 110 (HSP110) family members act as nucleotide exchange factors (NEF) of mammalian and yeast HSP70 chaperones during the ATP hydrolysis cycle. In this study, we describe the expression pattern of murine HSPA4, a member of the HSP110 family

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