|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat, Rabbit, Hamster, Monkey, Bovine|
|Calculated MW||70898 Da|
|Application & Usage||Western blot analysis (0.5-4 µg/ml) and in Immunohistochemistry. However, the optimal conditions should be determined individually. The antibody detects a 71 kDa Hsc70. A ~40 kDa band can also be detected in human samples. Jurkat cell lysate and mouse small intestine lysate can be used as positive controls.|
|Other Names||HSPA8, LAP1, HSC54, HSC70, HSC71, HSP71, HSP73, HSPA10, MGC131511, MGC29929, NIP71|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit anti-Hsc70 polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5% BSA, 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||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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Provided below are standard protocols that you may find useful for product applications.
The 70 kDa heat shock cognate protein, Hsc70, is part of the Hsp70 family. The family includes both cognate members and highly inducible isoforms. Members of the Hsp70 family are molecular chaperones which are involved in many cellular functions such as protein folding, transport, maturation and degradation.
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