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Rabbit Anti-DNAJB14/FITC Conjugated antibody
background:
The DnaJ family, one of the largest of all the chaperone families, has evolved with diverse cellular localization and functions. The presence of a J domain defines a protein as a member of the DnaJ family. DnaJ heat-shock induced proteins are derived from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. Members of this family contain cysteine-rich regions that are composed of zinc fingers that form a peptide-binding domain responsible for chaperone function. DnaJ family members are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJB14 (DnaJ (Hsp40) homolog, subfamily B, member 14) is a 379 amino acid single-pass membrane protein containing one J domain and is thought to act as a co-chaperone. DnaJB14 exists as two alternatively spliced isoforms.
Function:
May act as a co-chaperone.
Subcellular Location:
Membrane.
Similarity:
Contains 1 J domain.
Database links:
Entrez Gene: 79982 Human
SwissProt: Q8TBM8 Human
Unigene: 577426 Human
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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