HSPD1 Recombinant Monoclonal Antibody

Code CSB-RA953395A0HU
Size US$210
Order now
Image
  • Western Blot
    Positive WB detected in: Hela whole cell lysate, HepG2 whole cell lysate, 293 whole cell lysate, Jurkat whole cell lysate, MCF-7 whole cell lysate, K562 whole cell lysate, Mouse brain tissue
    All lanes: HSPD1 antibody at 1:2000
    Secondary
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 62, 18 kDa
    Observed band size: 60 kDa
  • IHC image of CSB-RA953395A0HU diluted at 1:100 and staining in paraffin-embedded human liver tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4℃ overnight. The primary is detected by a Goat anti-rabbit IgG polymer labeled by HRP and visualized using 0.05% DAB.
  • IHC image of CSB-RA953395A0HU diluted at 1:100 and staining in paraffin-embedded human liver cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4℃ overnight. The primary is detected by a Goat anti-rabbit IgG polymer labeled by HRP and visualized using 0.05% DAB.
  • Immunoprecipitating HSPD1 in HepG2 whole cell lysate
    Lane 1: Rabbit control IgG instead of CSB-RA953395A0HU in HepG2 whole cell lysate. For western blotting,a HRP-conjugated Protein G antibody was used as the secondary antibody (1/2000)
    Lane 2: CSB-RA953395A0HU(3µg)+ HepG2 whole cell lysate(500µg)
    Lane 3: HepG2 whole cell lysate (10µg)
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Uniprot No.
Target Names
HSPD1
Alternative Names
60 kDa heat shock protein, mitochondrial (EC 3.6.4.9) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein), HSPD1, HSP60
Species Reactivity
Human, Mouse
Immunogen
A synthesized peptide derived from human Hsp60
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Clonality
Monoclonal
Isotype
Rabbit IgG
Clone No.
3D8
Purification Method
Affinity-chromatography
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Form
Liquid
Tested Applications
ELISA, WB, IHC, IP
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:5000
IHC 1:50-1:200
IP 1:200-1:1000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Description

The HSPD1 recombinant monoclonal antibody is produced using protein and DNA recombinant technology. Initially, a synthesized peptide derived from human Hsp60 was used to immunize mice. After some time, the spleen of the mice was aseptically removed and the total RNA of spleen cells was extracted. The cDNA obtained from RNA reverse transcription served as the template for PCR amplification of the HSPD1 antibody gene. The HSPD1 antibody gene was then cloned into a vector, which was subsequently transfected into host cells for culture. The HSPD1 recombinant monoclonal antibody was purified from the cell culture supernatant using affinity chromatography. It has been rigorously tested and validated for its ability to detect human and mouse HSPD1 protein in ELISA, WB, and IHC, IP experiments.

The HSPD1 protein, also known as Hsp60, is a molecular chaperone that plays a key role in protein folding and assembly in the mitochondria of eukaryotic cells. It is involved in the folding and refolding of newly synthesized or denatured proteins. HSPD1 is a barrel-shaped protein complex that forms a cavity inside which unfolded or partially folded proteins can be properly folded in an ATP-dependent manner. In addition to its role in protein folding, HSPD1 has also been implicated in other cellular processes, including cell signaling, apoptosis, and immune response.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates 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. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
Gene References into Functions
  1. HSP60 showed pro-inflammatory properties in bronchial epithelial cells mediated by activation of TLR-4-related molecules. PMID: 28976240
  2. HSP60 silencing deactivates the mTOR pathway to suppress glioblastoma progression PMID: 27325206
  3. the effect of Hsp60 on differentiation and invasion of hepatocellular carcinoma cells might be associated with mitochondrial biogenesis PMID: 27677587
  4. The results demonstrate that HSP60 participates in mitochondrial progesterone synthesis. These findings provide novel insights into progesterone synthesis in the human placenta and its role in maintaining pregnancy. PMID: 28434777
  5. Clinical data showed that upregulation of miR-382/3-NT and downregulation of HSPD1/Trx were also observed in IgA nephropathy patients with renal interstitial fibrosis. These data supported a novel mechanism in which miR-382 targets HSPD1 and contributes to the redox imbalance in the development of renal fibrosis. PMID: 28680529
  6. Low HSP60 expression is associated with beta-cell hypertrophy and dysfunction. PMID: 27056903
  7. high level of ROS is needed for tumorigenesis and progression in tumors with low HSP60 expression PMID: 27246978
  8. HSP60 regulation of SOX9 ubiquitination mitigates the development of knee osteoarthritis. PMID: 27118120
  9. These findings shed some light on how a tumor cell may avert apoptosis using Hsp60 and point to the anti-cancer potential of drugs, such as CubipyOXA, which interfere with Hsp60/pC3 complex formation, and thus allow the apoptotic cascade to proceed. PMID: 28212901
  10. The associations of diabetes, combined with the polymorphisms in the genes of fat mass and obesity-associated gene (FTO), interleukin 6 (IL-6), and heat shock protein 60 (HSPD1), with breast cancer risk and survival in a Chinese Han population, was evaluated. PMID: 28591216
  11. 27-Hydroxycholesterol upregulates the production of HSP60 in monocytic cells. PMID: 28549691
  12. data indicate that HSP65 suppresses cholesterol efflux and increases cellular cholesterol content through an Lck-mediated pathway in T cells PMID: 27742830
  13. Doxorubicin treatment of lung mucoepidermoid cells results in Hsp60 post-translational modifications leading to the Hsp60/p53 complex dissociation and instauration of replicative senescence. PMID: 27836734
  14. Phosphorylation and subsequent transient degradation of mitochondrial Hsp60 during early hours of rotavirus-SA11 infection resulted in inhibition of premature import of nonstructural protein 4 into mitochondria, thereby delaying early apoptosis. PMID: 27665089
  15. Data show that the interaction between cell cycle and apoptosis regulator 2 (CCAR2) and heat shock protein 60 (Hsp60) increases in the presence of rotenone. PMID: 28254432
  16. NIP-SNAP-1 and -2 localized in the mitochondrial inner membrane space, whereas HSP60 localized in the matrix. Expression levels of NIP-SNAP-1 and -2 in cells were decreased by knockdown of HSP60, but not HSP10. The findings indicate that HSP60 promotes folding and maintains the stability of NIP-SNAP-1 and -2. PMID: 28011268
  17. expression elevated in lung adenocarcinoma tissue PMID: 28178129
  18. Hsp10 and Hsp60 may be implicated in carcinogenesis from its very early steps in colorectal cancer. PMID: 27491302
  19. High HSP60 expression is associated with gastric cancer. PMID: 26810190
  20. Elevated expression of HSPD1 in osteosarcoma tissues correlated with poor prognosis of the osteosarcoma patients. PMID: 27259322
  21. This review article presents accumulating proof that supports the idea that tolerization with antigenic HSP60 protein or its peptides may arrest or even prevent atherosclerosis by increased production of regulatory T cells and/or anti-inflammatory cytokines. [review] PMID: 26577462
  22. Data show that Eclipta extract upregulates heat shock protein 60 (Hsp60) which is localized in the endoplasmic reticulum (ER). PMID: 26672742
  23. Data indicate that on addition of the heat-shock proteins GroEL-GroES molecular chaperone system, the folding of the nascent chemokine receptor type 5 (CCR5) was significantly enhanced. PMID: 26585937
  24. The data show that immunohistochemistry for CD1a and Hsp60 can be of help in differential diagnosis between Keratoacantomas and well-differentiated forms of squamous cell carcinomas. PMID: 26442925
  25. Anti-citrullinated protein antibodies promote apoptosis of mature human osteoblasts via cell-surface binding to citrullinated heat shock protein 60. PMID: 26275591
  26. Heat shock protein 60 stimulates the migration of vascular smooth muscle cells via Toll-like receptor 4 and ERK MAPK activation PMID: 26477505
  27. Studies show that contrary to its role as a target for pathogenic autoimmune inflammatory processes, heat-shock protein 60 (HSP60) has been shown to activate immunoregulatory pathways that may lead to suppression of these diseases. PMID: 26431161
  28. Biochemical and genetic data demonstrate that FUS interacts with a mitochondrial chaperonin, HSP60, and that FUS translocation to mitochondria is, at least in part, mediated by HSP60 PMID: 26335776
  29. exposure of human promyelocytic HL-60 cells to a nontoxic concentration (10 muM) of 4-hydroxy-2-nonenal (HNE) yielded a HSP60 modified with HNE. PMID: 26078803
  30. HSP60 overexpression was associated with the disease progression and prognosis in gastric cancer, and its expression significantly correlated with the expression of MMP-9. PMID: 25207654
  31. Hsp60 is increased in both animals and patients with TLE in affected tissues, and in plasma in response to epileptic seizures, and point to it as biomarker of hippocampal stress potentially useful for diagnosis and patient management. PMID: 25801186
  32. no significant relationship between anti-hsp60 antibodies and serological markers of infection was observed, which may only indicate an indirect role of infection in the assessment of breaking the immunological tolerance against autologous HSPs PMID: 25654359
  33. Low level of HSP60 may lead to lack of anti-inflammatory response due to less Treg activation, hence, could be a counterpart in the pathogenesis of ITP. PMID: 24749912
  34. The present study indicated that HSPD1 interacted with IRF3 and it contributed to the induction of IFN-beta. PMID: 25506707
  35. Hsp60 was found to be increased in cancerous tissue in patients with large bowel cancer PMID: 26060090
  36. The immunological response to Hsp60/65 is increased in early clinical stages of ovarian cancer and the level of anti-hsp60/65 antibodies may be then a helpful diagnostic marker. PMID: 24618330
  37. an HLD4-associated (Asp-29-to-Gly) mutant of mitochondrial heat shock 60-kDa protein 1 (HSPD1) causes short-length morphologies and increases the numbers of mitochondria due to their aberrant fission and fusion cycles PMID: 25957474
  38. structural analysis of mutated human Hsp60-human Hsp10 complex PMID: 25918392
  39. Levels of circulating autoantibodies against Hsp60, Hsp70, and Hsp90 were elevated and positively correlated with both cutaneous disease activity in dermatitis herpetiformis. PMID: 24643797
  40. Data inticate that heat shock protein 60 (HSP60) interacted constitutively with NKG2D ligand ULBP2 and phosphatase of regenerating liver 3 (PRL-3) regulated HSP60 tyrosine phosphorylation. PMID: 25687758
  41. Increased levels of anti-heat-shock protein 60 (anti-Hsp60) indicate endothelial dysfunction, atherosclerosis and cardiovascular diseases in patients with mixed connective tissue disease PMID: 24838263
  42. Lysine biotinylation and methionine oxidation in the heat shock protein HSP60 synergize in the elimination of reactive oxygen species. PMID: 24582286
  43. Modified forms of LDL activate human T cells through dendritic cells. HSP60 and 90 contribute to such T-cell activation. PMID: 25395618
  44. Hsp60 mitochondrial import signal is stable in solution PMID: 24830947
  45. These seven proteins, especially HSP 60, may serve as potential biomarkers for the diagnosis of RHD. PMID: 24738046
  46. Regions in the Hsp60 molecule show structural similarity with the thyroglobulin (TG) and thyroid peroxidase (TPO) molecules supporting the notion that autoantibodies against TG and TPO are likely to recognize Hsp60 on the plasma membrane of oncocytes. PMID: 24057177
  47. Data suggest that up-regulation of HSP60/HSPD1 binding/reactivity leads to increased cytokine synthesis/secretion and other proinflammatory responses in adipocytes, especially in mature visceral adipocytes. PMID: 24672802
  48. Citrullination of HSP60 is associated with neoplasms. PMID: 24099319
  49. Antibodies to human HSP60 were found in 19 (15.8%) of 120 patients with a history of recurrent miscarriages. PMID: 24680363
  50. The pathogenic variant of rs72466451 may play a role in a subgroup of sudden infant death syndrome cases with impaired Hsp60-mediated stress response. PMID: 23823174

Show More

Hide All

Involvement in disease
Spastic paraplegia 13, autosomal dominant (SPG13); Leukodystrophy, hypomyelinating, 4 (HLD4)
Subcellular Location
Mitochondrion matrix.
Protein Families
Chaperonin (HSP60) family
Database Links

HGNC: 5261

OMIM: 118190

KEGG: hsa:3329

STRING: 9606.ENSP00000340019

UniGene: Hs.595053

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
webinars: DT3C facilitates antibody internalization X
Place an order now

I. Product details

*
*
*
*

II. Contact details

*
*

III. Ship To

*
*
*
*
*
*
*

IV. Bill To

*
*
*
*
*
*
*
*