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Western blot
Immunocytochemistry
ImmunoprecipitationAntibody data
- Antibody Data
- Antigen structure
- References [13]
- Comments [0]
- Validations
- Western blot [1]
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- Product number
- ABIN2486782 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-DnaJ (Hsp40) Homolog, Subfamily B, Member 1 (DNAJB1) antibody (Atto 390)
- Antibody type
- Polyclonal
- Description
- Rabbit Antiserum
- Reactivity
- Human
- Host
- Rabbit
- Vial size
- 100 μL
- Storage
- 4°C
Submitted references Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis.
Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function.
Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells.
Proteins of the PDI family: unpredicted non-ER locations and functions.
Role of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein.
BiP and PDI cooperate in the oxidative folding of antibodies in vitro.
The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.
Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells.
Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.
Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal.
A novel 40-kDa protein induced by heat shock and other stresses in mammalian and avian cells.
The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein.
Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product.
Na KS, Park BC, Jang M, Cho S, Lee do H, Kang S, Lee CK, Bae KH, Park SG
Molecules and cells 2007 Oct 31;24(2):261-7
Molecules and cells 2007 Oct 31;24(2):261-7
Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function.
Schultz-Norton JR, McDonald WH, Yates JR, Nardulli AM
Molecular endocrinology (Baltimore, Md.) 2006 Sep;20(9):1982-95
Molecular endocrinology (Baltimore, Md.) 2006 Sep;20(9):1982-95
Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells.
Janiszewski M, Lopes LR, Carmo AO, Pedro MA, Brandes RP, Santos CX, Laurindo FR
The Journal of biological chemistry 2005 Dec 9;280(49):40813-9
The Journal of biological chemistry 2005 Dec 9;280(49):40813-9
Proteins of the PDI family: unpredicted non-ER locations and functions.
Turano C, Coppari S, Altieri F, Ferraro A
Journal of cellular physiology 2002 Nov;193(2):154-63
Journal of cellular physiology 2002 Nov;193(2):154-63
Role of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein.
Delom F, Mallet B, Carayon P, Lejeune PJ
The Journal of biological chemistry 2001 Jun 15;276(24):21337-42
The Journal of biological chemistry 2001 Jun 15;276(24):21337-42
BiP and PDI cooperate in the oxidative folding of antibodies in vitro.
Mayer M, Kies U, Kammermeier R, Buchner J
The Journal of biological chemistry 2000 Sep 22;275(38):29421-5
The Journal of biological chemistry 2000 Sep 22;275(38):29421-5
The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.
Melville MW, Hansen WJ, Freeman BC, Welch WJ, Katze MG
Proceedings of the National Academy of Sciences of the United States of America 1997 Jan 7;94(1):97-102
Proceedings of the National Academy of Sciences of the United States of America 1997 Jan 7;94(1):97-102
Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells.
Michels AA, Kanon B, Konings AW, Ohtsuka K, Bensaude O, Kampinga HH
The Journal of biological chemistry 1997 Dec 26;272(52):33283-9
The Journal of biological chemistry 1997 Dec 26;272(52):33283-9
Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.
Hattori H, Liu YC, Tohnai I, Ueda M, Kaneda T, Kobayashi T, Tanabe K, Ohtsuka K
Cell structure and function 1992 Feb;17(1):77-86
Cell structure and function 1992 Feb;17(1):77-86
Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal.
Yoshimori T, Semba T, Takemoto H, Akagi S, Yamamoto A, Tashiro Y
The Journal of biological chemistry 1990 Sep 15;265(26):15984-90
The Journal of biological chemistry 1990 Sep 15;265(26):15984-90
A novel 40-kDa protein induced by heat shock and other stresses in mammalian and avian cells.
Ohtsuka K, Masuda A, Nakai A, Nagata K
Biochemical and biophysical research communications 1990 Jan 30;166(2):642-7
Biochemical and biophysical research communications 1990 Jan 30;166(2):642-7
The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein.
Bardwell JC, Tilly K, Craig E, King J, Zylicz M, Georgopoulos C
The Journal of biological chemistry 1986 Feb 5;261(4):1782-5
The Journal of biological chemistry 1986 Feb 5;261(4):1782-5
Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product.
Ohki M, Tamura F, Nishimura S, Uchida H
The Journal of biological chemistry 1986 Feb 5;261(4):1778-81
The Journal of biological chemistry 1986 Feb 5;261(4):1778-81
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