|Application ||WB, IHC-P|
|Predicted||Human, Mouse, Rat, Rabbit, Hamster, Monkey, Bovine|
|Calculated MW||70898 Da|
|Dilution||IHC-P (5 µg/ml), WB (0.5 - 4 µg/ml)|
|Other Names||HSPA8, Heat shock 70 kDa protein 8, Heat shock 70kd protein 10, Heat shock 70kD protein 8, Heat shock cognate protein 54, HSP71, HSPA10, HSC71, HSP73, LPS-associated protein 1, Heat shock 70kDa protein 8, NIP71, HSC54, HSC70, LAP1|
|Target/Specificity||The antibody detects a 71 kD Hsc70. A ~40 kD band can also be detected in human samples. Jurkat cell lysate and mouse small intestine lysate can be used as positive controls. Blocking peptide is also available.|
|Reconstitution & Storage||Affinity purified|
|Precautions||Anti-HSPA8 / HSC70 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||HSC70, HSP73, HSPA10|
|Function||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. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) et 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 CHIP.|
|Cellular 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|
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