HPA014797
Anti-HSPA13 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-Microsomal stress 70 protein ATPase core, Anti-STCH antibody produced in rabbit, Anti-Stress 70 protein chaperone microsome-associated 60 kDa protein precursor
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100 μL
$598.00
$598.00
Usually ships in 1 week. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)
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100 μL
$598.00
About This Item
$598.00
Usually ships in 1 week. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)
biological source
rabbit
Quality Level
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
technique(s)
immunohistochemistry: 1:20-1:50
immunogen sequence
AYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQIYQTYGFVPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDRKEPHSSDTELPKDKLSSADDH
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... HSPA13(6782)
General description
HSPA13 (heat shock protein 70kDa family, member 13) belongs to the heat shock protein 70 chaperone family. It has a highly conserved N-terminal domain, which contains the ATPase domain, and a unique hydrophobic leader sequence. It is a constitutively and ubiquitously expressed gene, and the encoded protein has a molecular weight of 60kDa. This gene is localized to human chromosome 21q11.1. It is localized to the microsomal region of the cell.
Immunogen
Stress 70 protein chaperone microsome-associated 60 kDa protein precursor (Microsomal stress 70 protein ATPase core).
Application
All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.
The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.
The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.
Biochem/physiol Actions
HSPA13 (heat shock protein 70kDa family, member 13) is responsible for processing both secretory and cytoplasmic proteins. It binds to misfolded or denatured peptides, and then uses ATP-derived energy to release them. Unlike other members of HSP70 family, which are induced by heat shock, this protein is activated by Ca2+ ionophore A23187. Studies in Japanese population show that variants of this gene might be linked to susceptibility to gastric cancer. This protein is capable of modulating TRAIL-mediated cell apoptosis, and hence, plays a key role in cell survival. It interacts with pH-regulating transporters NBCe1-B and NHE1, and modulates their membrane expression. Therefore, it regulates intracellular pH during stress, and facilitates cellular recovery from acidification. Mutations in this gene have been shown to be associated with Alzheimer′s disease, epilepsy and autism. It is also thought to be involved in regulating plasticity.
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 APREST72076
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
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Nobushige Yamagata et al.
Biochemical and biophysical research communications, 376(3), 499-503 (2008-09-17)
The stress 70 protein chaperone (STCH), a member of the heat shock protein 70 (HSP70) superfamily, is a microsomal protein that contains a N-terminal ATPase domain but lacks a C-terminal protein binding domain. Although cell-protective functions of HSP70 members are
Localization of STCH to human chromosome 21q11.1.
G Brodsky et al.
Genomics, 30(3), 627-628 (1995-12-10)
Jun-Seok Bae et al.
The Journal of biological chemistry, 288(9), 6295-6305 (2013-01-11)
Regulation of intracellular pH is critical for the maintenance of cell homeostasis in response to stress. We used yeast two-hybrid screening to identify novel interacting partners of the pH-regulating transporter NBCe1-B. We identified Hsp70-like stress 70 protein chaperone (STCH) as
Masayuki Aoki et al.
Biochemical and biophysical research communications, 335(2), 566-574 (2005-08-10)
Association analysis, based on linkage disequilibrium between specific alleles in the candidate loci and nearby genetic markers, has been proposed to identify genes conferring susceptibility to multifactorial diseases. Using the affected sib-pair method, we previously mapped four candidate chromosomal regions
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