product summary
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company name :
StressMarq Biosciences
product type :
antibody
product name :
HSC70 (HSP73) Antibody
catalog :
SMC-151B
quantity :
200 µg
price :
330.00 USD
clonality :
monoclonal
host :
mouse
conjugate :
nonconjugated
clone name :
1F2-H5
reactivity :
human, mouse, rat
application :
western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation, proximity ligation assay
more info or order :
citations: 5
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product information
Catalog No :
SMC-151B
Product Name :
HSC70 (HSP73) Antibody
Description :
Mouse Anti-Human HSC70 (HSP73) Monoclonal IgG2a Kappa
Target :
HSC70 (HSP73)
Conjugate :
Unconjugated
2021 List Price :
330.00 USD
Currency :
USD
Research Area(s) :
Cancer Heat Shock Cell Signaling Protein Trafficking Chaperone Proteins
Alternative Name(s) :
HSC54 Antibody, HSC71 Antibody, HSC73 Antibody, HSP71 Antibody, HSP73 Antibody, HSPA10 Antibody, HSPA8 Antibody, LAP1 Antibody, NIP71 Antibody
Size :
200 µg
Category :
Antibodies
Product Type :
Monoclonal
Clone Number :
1F2-H5
Immunogen :
Full length human HSC70
Immunogen Species :
Human
Accession Number :
NP_006588.1
Swiss-Prot :
P11142
Applications :
WB IHC ICC/IF IP ELISA PLA PBA AM
Host Species :
Mouse
Isotype :
IgG2a Kappa
Species Reactivity Abbreviation :
Hu Ms Rt
Species Reactivity Full Name :
Human Mouse Rat
Antibody Dilution :
WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.
Purification :
Protein G Purified
Storage Buffer :
PBS pH7.4, 50% glycerol, 0.09% sodium azide
Concentration :
1 mg/ml
Specificity :
Detects ~73kDa. Does not cross react with HSP70.
Storage Temperature :
-20ºC
Shipping Temperature :
Blue Ice or 4ºC
Cite this Product :
StressMarq Biosciences Cat# SMC-151B, RRID: AB_2120165
Certificate of Analysis :
1 µg/ml of SMC-151 was sufficient for detection of HSC70 in 10 µg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Cellular Localization :
Cytoplasm Melanosome
Scientific Background :
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5).
When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).
References :
1. Brown C.L. et al. (1993) J.Cell Biol., 120 (5): 1101-1112.
2. Boorstein W.R., Ziegelhoffer T., and Craig E.A. (1993)J. Mol. Evol. 38(1): 1-17.
3. Rothman J. (1989), Cell 59: 591-601.
4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887.
5. Bork P., Sander C., and Valencia A. (1992) Proc. Nut1Acad. Sci. USA 89: 7290-7294.
6. Brown C.L. et al. (1996) J. Biol. Chem. 271(2): 833-840.
Field of Use :
Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
Image Filenames :
SMC-151_Hsc70-Hsp73_Antibody_1F2-H5_ICC-IF_Human_Heat-Shocked-HeLa-Cells_100x_Composite.png SMC-151_Hsc70_Antibody_1F2-H5_WB_Human_Cell-lysates_1.png SMC-151_Hsc70-Hsp73_Antibody_1F2-H5_ICC-IF_Human_Heat-Shocked-HeLa-Cells_20x_Composite.png SMC-151_Hsc70_Antibody_1F2-H5_ICC-IF_Human_HaCaT-cells_1.png
more info or order :
company information

StressMarq Biosciences
PO Box 55036 CADBORO BAY
3825 Cadboro Bay Road
Victoria BC V8N 4G0
3825 Cadboro Bay Road
Victoria BC V8N 4G0
info@stressmarq.com
http://www.stressmarq.com1-250-294-9065
headquarters: canada
StressMarq Biosciences Inc. is a bioreagents company producing high-quality antibodies, antibody conjugates, proteins, assay kits, and small molecules for the life sciences.
With over 17,000 products, we offer a wide range of products for scientists in cancer, neuroscience, epigenetics, cell signalling, and cellular stress research areas.
Based in Victoria, BC, with a small but dedicated group of scientists, StressMarq provides highly-validated products that are sold with our quality guarantee, and supported by our years of scientific expertise. Our products are available in over 50 countries through our extensive distributor network.
StressMarq draws on scientific excellence from around the globe. We strive to partner with academic or for-profit institutions through licensing agreements to bring cutting-edge research tools to the scientific community.
With over 17,000 products, we offer a wide range of products for scientists in cancer, neuroscience, epigenetics, cell signalling, and cellular stress research areas.
Based in Victoria, BC, with a small but dedicated group of scientists, StressMarq provides highly-validated products that are sold with our quality guarantee, and supported by our years of scientific expertise. Our products are available in over 50 countries through our extensive distributor network.
StressMarq draws on scientific excellence from around the globe. We strive to partner with academic or for-profit institutions through licensing agreements to bring cutting-edge research tools to the scientific community.
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