Anti-Hsc70/HSPA8 Antibody Picoband® fluoro647 Vervoeging

HSPA8 (heat shock 70kDa protein 8) also known as HSC70, HSC71, HSP73, HSPA10, FORMERLY, LAP1 or LPS-ASSOCIATED PROTEIN 1, is a  heat shock protein  that in humans is encoded by the  HSPA8  gene. The  HSPA8  gene contains 9 exons and spans 5 kb. The deduced  HSPA8  protein has 646 amino acids and a predicted molecular mass of 70,899 Da. The HSPA8 gene is mapped on 11q24.1. HSPA8 plays an important role in cells by transiently associating with nascent polypeptides to facilitate correct folding. HSP73 also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Rapid decay involves AU-rich binding protein AUF1, which complexes with heat-shock proteins HSC70 and HSP70, translation initiation factor EIF4G, and poly (A) -binding protein. In the absence of Il3, Hsc70 formed a complex with Hsp40 and Hip, and this complex, in association with Eif4g and Pabp, formed a high-stability complex with Bim mRNA that protected it from ribonucleases.

Heat shock cognate 71 kDa protein; Heat shock 70 kDa protein 8; Lipopolysaccharide-associated protein 1; LAP-1; LPS-associated protein 1; HSPA8; HSC70, HSP73, HSPA10

HSPA8

3312

P11142

Human, Mouse, Rat

No cross-reactivity with other proteins

A synthetic peptide corresponding to a sequence at the C-terminus of human Hsc70, different from the related mouse and rat sequences by one amino acid.

Ubiquitous. .

Flow Cytometry

Chaperones, Heat Shock Proteins, Protein Trafficking, Signal Transduction

Immunogen affinity purified.

Liquid

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. .

1. Chappell, T. G., Welch, W. J., Schlossman, D. M., Palter, K. B., Schlesinger, M. J., Rothman, J. E. Uncoating ATPase is a member of the 70 kilodalton family of stress proteins. Cell 45: 3-13, 1986. 2. Hohfeld, J., Minami, Y., Hartl, F.-U. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589-598, 1995. 3. Matsui, H., Asou, H., Inaba, T. Cytokines the regulation of Bim mRNA stability by heat-shock cognate protein 70. Molec. Cell 25: 99-112, 2007.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

70898 MW

No cross reactivity with other proteins.

6

Heat shock cognate 71 kDa protein

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

Belongs to the heat shock protein 70 family.

Heat shock cognate 71 kDa protein

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.