Western Blot (WB)
(Western blot analysis of Parasite Lysates showing detection of HSP60 protein using Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185). Primary Antibody: Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185) at 1:1000.)
Rabbit Hsp60 Polyclonal Antibody | anti-PF10_0153 antibody
Hsp60 (P. Falciparum) Antibody
Reactivity
Cross-reacts with E Coli Hsp60, GroEl.
Applications
Western Blot, Immunofluorescence
Synonyms
Hsp60; Polyclonal Antibody; Hsp60 (P. Falciparum) Antibody; CH60_PLAFG; Chaperonin CPN60; mitochondrial; PfHsp60; anti-PF10_0153 antibody
Host
Rabbit
Reactivity
Cross-reacts with E Coli Hsp60, GroEl.
Clonality
Polyclonal
Form/Format
Protein A Purified
Concentration
1.83mg/mL (varies by lot)
Sequence Length
1743
Applicable Applications for anti-PF10_0153 antibody
Western Blot (WB), Immunofluorescence (IF)
Application Notes
1:2000 (WB)
Certificate of Analysis
0.9 ug/mL of SPC-185 was sufficient for detection of PfHsp60 in 20ug of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.
Storage Buffer
PBS pH7.4, 50% glycerol, 0.09% sodium azide
Preparation and Storage
-20 degree C
Western Blot (WB)
(Western blot analysis of Parasite Lysates showing detection of HSP60 protein using Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185). Primary Antibody: Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185) at 1:1000.)
Western Blot (WB)
(Western blot analysis of Parasite Lysates showing detection of HSP60 protein using Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185). Primary Antibody: Rabbit Anti-HSP60 Polyclonal Antibody (SPC-185) at 1:1000.)
Related Product Information for anti-PF10_0153 antibody
Background Info: This protein A Affinity purified antibody detects an 60kD protein, corresponding to P.falciparum Hsp60 on SDS PAGE immunoblot; in samples from P.Falciparum origin.
Scientific Background: In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. Hsp60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian Hsp60 (1-3). Whereas mammalian Hsp60 is localized within the mitochondria, plant Hsp60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that Hsp60 is present in so many different species. The common characteristics of the Hsp60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, Hsp60 with its co-chaperonin, Hsp10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of Hsp60-Hsp10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of Hsp60 and Hsp10 is their protective functions against infection and cellular stress. Hsp60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
Scientific Background: In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. Hsp60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian Hsp60 (1-3). Whereas mammalian Hsp60 is localized within the mitochondria, plant Hsp60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that Hsp60 is present in so many different species. The common characteristics of the Hsp60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, Hsp60 with its co-chaperonin, Hsp10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of Hsp60-Hsp10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of Hsp60 and Hsp10 is their protective functions against infection and cellular stress. Hsp60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
Product Categories/Family for anti-PF10_0153 antibody
References
1. Hartl F.U. (1996) Nature 381: 571-579. 2. Bukau B., and Horwich A.L. (1998) Cell 92: 351-366. 3. Hartl F.U and Hayer-Hartl M. (2002) Science 295: 1852-1858. 4. Jindal S., et al. (1989) Molecular and Cellular Biology 9: 2279-2283. 5. La Verda D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64- 71. 6. Itoh H., et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7. Gupta S. and Knowlton A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris C.C., et al. (2006) Cell Stress Chaperones 11: 116- 128. 9. Lai H.C., et al. (2007) Am. J. Physiol. Endocrinol. Metab 292: E292-E297.
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
Molecular Weight
79,445 Da
NCBI Official Full Name
Plasmodium falciparum 3D7 heat shock protein 60 (PF10_0153) mRNA, complete cds
NCBI Official Symbol
PF10_0153
NCBI Protein Information
heat shock protein 60
UniProt Protein Name
Chaperonin CPN60, mitochondrial
UniProt Entry Name
CH60_PLAFG
Uniprot Description
Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
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Product Notes
The PF10_0153 (Catalog #AAA805526) is an Antibody produced from Rabbit and is intended for research purposes only. The product is available for immediate purchase. The Hsp60 (P. Falciparum) Antibody reacts with Cross-reacts with E Coli Hsp60, GroEl. and may cross-react with other species as described in the data sheet. AAA Biotech's Hsp60 can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), Immunofluorescence (IF). 1:2000 (WB). Researchers should empirically determine the suitability of the PF10_0153 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "Hsp60, Polyclonal Antibody" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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