Product: Hsc70 Antibody
Catalog: AF5187
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 70 kD; 71kD(Calculated).
Uniprot: P11142
RRID: AB_2837673

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IF/ICC 1:100-1:500, IHC 1:50-1:200, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Reactivity:
Human,Mouse,Rat,Monkey
Prediction:
Pig(100%), Zebrafish(89%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%)
Clonality:
Polyclonal
Specificity:
Hsc70 Antibody detects endogenous levels of total Hsc70.
RRID:
AB_2837673
Cite Format: Affinity Biosciences Cat# AF5187, RRID:AB_2837673.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

2410008N15Rik; Constitutive heat shock protein 70; Epididymis luminal protein 33; Epididymis secretory sperm binding protein Li 72p; Heat shock 70 kDa protein 8; Heat shock 70kD protein 10; Heat shock 70kD protein 8; Heat shock 70kDa protein 8; Heat shock cognate 71 kDa protein; Heat shock cognate protein 54; Heat shock cognate protein 71 kDa; Heat shock protein 8; Heat shock protein A8; Heat-shock70-KD protein 10, formerly; HEL 33; HEL S 72p; HSC54; HSC71; Hsc73; HSP71; HSP73; HSP7C_HUMAN; HSPA10; HSPA8; LAP1; Lipopolysaccharide associated protein 1; LPS associated protein 1; LPS associated protein; MGC102007; MGC106514; MGC114311; MGC118485; MGC131511; MGC29929; N-myristoyltransferase inhibitor protein 71; NIP71;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P11142 HSP7C_HUMAN:

Ubiquitous.

Description:
Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.
Sequence:
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Chicken
100
Rabbit
100
Zebrafish
89
Xenopus
78
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P11142 As Substrate

Site PTM Type Enzyme
S2 Acetylation
S2 Phosphorylation
K3 Acetylation
K3 Ubiquitination
T13 Phosphorylation
Y15 Phosphorylation
S16 Phosphorylation
K25 Ubiquitination
T37 Phosphorylation
T38 Phosphorylation
S40 Phosphorylation
Y41 Phosphorylation
T45 Phosphorylation
T47 Phosphorylation
R49 Methylation
K56 Acetylation
K56 Ubiquitination
T64 Phosphorylation
T66 Phosphorylation
K71 Acetylation
K71 Ubiquitination
S85 Phosphorylation
K88 Acetylation
K88 Methylation
K88 Ubiquitination
K102 Ubiquitination
Y107 Phosphorylation
K108 Acetylation
K108 Ubiquitination
T111 Phosphorylation
K112 Acetylation
K112 Ubiquitination
S113 Phosphorylation
T125 Phosphorylation
K126 Ubiquitination
K128 Acetylation
K128 Ubiquitination
Y134 Phosphorylation
K137 Acetylation
K137 Ubiquitination
T138 Phosphorylation
T140 Phosphorylation
Y149 Phosphorylation
S153 Phosphorylation
T158 Phosphorylation
K159 Acetylation
K159 Ubiquitination
T163 Phosphorylation
T177 Phosphorylation
Y183 Phosphorylation
K187 Acetylation
K187 Ubiquitination
K188 Ubiquitination
K220 Ubiquitination
S221 Phosphorylation
T222 Phosphorylation
T226 Phosphorylation
K246 Acetylation
K246 Methylation
K246 Ubiquitination
K251 Ubiquitination
S254 Phosphorylation
K257 Acetylation
K257 Sumoylation
K257 Ubiquitination
T265 Phosphorylation
T273 Phosphorylation
S277 Phosphorylation
T298 Phosphorylation
T313 Phosphorylation
K319 Acetylation
K319 Ubiquitination
K325 Ubiquitination
K328 Acetylation
K328 Ubiquitination
S329 Phosphorylation
T341 Phosphorylation
K345 Ubiquitination
K348 Acetylation
K348 Ubiquitination
K357 Acetylation
K357 Sumoylation
K357 Ubiquitination
K361 Acetylation
K361 Sumoylation
K361 Ubiquitination
S362 Phosphorylation
Y371 Phosphorylation
S381 Phosphorylation
S400 Phosphorylation
T411 Phosphorylation
K415 Ubiquitination
T418 Phosphorylation
K423 Ubiquitination
T427 Phosphorylation
Y431 Phosphorylation
K451 Acetylation
K451 Ubiquitination
K458 Ubiquitination
T462 Phosphorylation
R469 Methylation
T477 Phosphorylation
K497 Ubiquitination
K500 Ubiquitination
T502 Phosphorylation
K507 Acetylation
K507 Sumoylation
K507 Ubiquitination
S511 Phosphorylation
K512 Acetylation
K512 Sumoylation
K512 Ubiquitination
K524 Acetylation
K524 Ubiquitination
Y525 Phosphorylation
K526 Ubiquitination
K531 Ubiquitination
K535 Ubiquitination
K539 Acetylation
K539 Ubiquitination
S541 Phosphorylation
S544 Phosphorylation
Y545 Phosphorylation
K550 Ubiquitination
K557 Methylation
K557 Ubiquitination
K561 Acetylation
K561 Methylation
K561 Ubiquitination
K567 Methylation
K569 Methylation
K573 Ubiquitination
C574 S-Nitrosylation
K583 Acetylation
K583 Sumoylation
K583 Ubiquitination
K589 Acetylation
K589 Ubiquitination
K597 Acetylation
K597 Ubiquitination
K601 Acetylation
K601 Methylation
K601 Ubiquitination
C603 S-Nitrosylation
T608 Phosphorylation
K609 Ubiquitination
S613 Phosphorylation
S637 Phosphorylation
S638 Phosphorylation
T641 Phosphorylation

Research Backgrounds

Function:

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21.

PTMs:

Acetylated.

ISGylated.

Trimethylation at Lys-561 reduces fibrillar SNCA binding.

Subcellular Location:

Cytoplasm. Melanosome. Nucleus>Nucleolus. Cell membrane.
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Ubiquitous.

Subunit Structure:

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7. Interacts with DNAJB12 (via J domain). Interacts with DNAJB14 (via J domain). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with TRIM5. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9 (via J domain). Interacts with MLLT11. Interacts with RNF207. Interacts with DNAJC21. Interacts with DNAJB2. Interacts with TTC1 (via TPR repeats). Interacts with SGTA (via TPR repeats) (By similarity). Interacts with HSF1 (via transactivation domain). Interacts with HOPX, HSP40 and HSP90. Interacts with STUB1. Interacts with BAG2. Interacts with BAG3. Interacts with DNAJC12. Interacts with ZMYND10. Interacts with HSPC138. Interacts with BCL2L1, GIMAP5 and MCL1; the interaction with BCL2L1 or MCL1 is impaired in the absence of GIMAP5 (By similarity). Interacts with NLPR12. Interacts with TTC4.

(Microbial infection) Interacts with SV40 VP1.

Family&Domains:

The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.

Belongs to the heat shock protein 70 family.

Research Fields

· Cellular Processes > Transport and catabolism > Endocytosis.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Genetic Information Processing > Transcription > Spliceosome.

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Viral > Measles.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.

· Organismal Systems > Aging > Longevity regulating pathway - multiple species.   (View pathway)

· Organismal Systems > Immune system > Antigen processing and presentation.   (View pathway)

· Organismal Systems > Endocrine system > Estrogen signaling pathway.   (View pathway)

References

1). Shan Y et al. Aging as a Precipitating Factor in Chronic Restraint Stress-Induced Tau Aggregation Pathology, and the Protective Effects of Rosmarinic Acid. J Alzheimers Dis 2016;49(3):829-44 (PubMed: 26577520) [IF=3.909]

Application: WB    Species: mouse    Sample: mouse

Fig. 5. The effect of chronic restraint stress on the expression of chaperone proteins. Homogenates of cerebral cortex from adult (6 months) and middle-age (13 months) mice with or without chronic restraint stress were detected by immunoblotting with antibodies against chaperones including heat shock proteins (HSP70, HSC70, HSP90, and HDJ2/HSP40) and chaperonin TCP1, and also the antibody against Pin1 (A). The protein levels were present as the fold change compared with the level in control of 13-month-old mice. The quantified data of (A) are shown in histograms (B-G). Data were expressed as mean ± SEM, n = 4. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. H) The expression of HDJ2/HSP40 or Pin1 in HEK293 cells was inhibited by siRNA, and tau gene was transfected by 2.5 g (+) or 5g (++) GV143-tau plasmids. The total extraneous tau, which contained a FLAG tag, were analyzed by anti-FLAG antibody, and P-tau was detected by PS396 antibody.

2). Liu Y et al. Memantine Differentially Regulates Tau Phosphorylation Induced by Chronic Restraint Stress of Varying Duration in Mice. Neural Plast 2019 Feb 14;2019:4168472 (PubMed: 30906318)

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