HPA010023
Anti-HSPA4 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-HSP70RY, Anti-Heat shock 70 kDa protein 4, Anti-Heat shock 70-related protein APG-2
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All Photos(4)
About This Item
Recommended Products
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
human, mouse, rat
technique(s)
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500
immunogen sequence
FEELGKQIQQYMKIISSFKNKEDQYDHLDAADMTKVEKSTNEAMEWMNNKLNLQNKQSLTMDPVVKSKEIEAKIKELTSTCSPIISKPKPKVEPPKEEQKNAEQNGPVDG
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... HSPA4(3308)
General description
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.
Immunogen
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.
Biochem/physiol Actions
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.
Features and Benefits
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:
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.
Linkage
Corresponding Antigen APREST71595
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Legal Information
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
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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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
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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