DnaJ (Hsp40) Homolog, Subfamily B, Member 1 (DNAJB1) antibody

Antigen: DnaJ (Hsp40) Homolog, Subfamily B, Member 1 (DNAJB1)

Synonyms: DNAJ1, DROJ1, DnaJ1 64EF, EU3500, HSP40, HSP40/HDJ1, Hsp-40, anon-WO0140519.166, anon-WO0172774.135, dHDJ1, dHDJ1/HSP40, dhdj-1, DmelCG10578, CG10578, psiHSP40, hdj1, sis1, hsp40, hspf1, dnajb4, MGC89364, Hsp40, DnaJ-5, MAS5, dnaJ

Clonality: Polyclonal

Host: Rabbit

Reactivity: Plasmodium falciparum

Catalog no.: ABIN361684

Additional Information

Alternative name: Hsp40

Immunogen: C-terminal peptide of Pf11_0512 conjugated to KLH

Format: Protein A purified

Description: DnaJ/Hsp40 proteins have been preserved throughout evolution and are important for protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of chaperone proteins, Hsp70s. Because the ATP hydrolysis is essential for the activity of Hsp70s, DnaJ/Hsp40 proteins actually determine the activity of Hsp70s by stabilizing their interaction with substrate proteins. DnaJ/Hsp40 proteins all contain the J domain through which they bind to Hsp70s. Hsp40, also known as HDJ1 (1), is a basic mammalian 40kDa heat shock protein which is not only homologous to the bacterial heat shock protein (DnaJ), but also yeast DnaJ-related proteins such as SCJ1, Sec63/Npl1, YDJ1 and SIS1 (2-6). Hsp 40 is inducible by stress including heat after which is moves from the cytoplasm to the nucleus and nucleoli, an intracellular pattern similar to Hsc70/Hsp70, the mammalian homologues of the bacterial heat shock protein, DnaK (3). PF11_0513 belongs to the Hsp40 family of chaperones. This protein has a Plasmodium export element (PEXEL). It is exported out of the parasite into the infected erythrocytic compartment.

Specificity: This protein A Affinity purified antibody detects an 62kDa protein, corresponding to P. falciparum Hsp40 on SDS PAGE immunoblot, in samples from P. falciparum origin. Species cross-reactivity: It is species specific to P. falciparum and does not cross-react to any protein from human erythrocytes.

Synonyms: DNAJ1, DROJ1, DnaJ1 64EF, EU3500, HSP40, HSP40/HDJ1, Hsp-40, anon-WO0140519.166, anon-WO0172774.135, dHDJ1, dHDJ1/HSP40, dhdj-1, DmelCG10578, CG10578, psiHSP40, hdj1, sis1, hsp40, hspf1, dnajb4, MGC89364, Hsp40, DnaJ-5, MAS5, dnaJ

Application Details

Application Notes: 1:2000 dilution for western blot and a 1:50 dilution for IF. Higher dilutions can be tried.

Concentration: 1.8mg/ml

Buffer: PBS pH 7.4, 50% glycerol, 0.09% azide. Protein A affinity purified.

Storage: -20°C, 1 year+, shipped on cold packs or ambient

Research Area: Signaling, Heat Shock Proteins

Restrictions: For Research Use only

Images

Hsp40 (Pf11_01513), malarial parasite lysate

Publications

Publications: Hattori, Liu, Tohnai et al.: "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells." in: Cell structure and function, Vol. 17, Issue 1, pp. 77-86, 1992 (PubMed).

Ohtsuka, Masuda, Nakai et al.: "A novel 40-kDa protein induced by heat shock and other stresses in mammalian and avian cells." in: Biochemical and biophysical research communications, Vol. 166, Issue 2, pp. 642-7, 1990 (PubMed).

Ohki, Tamura, Nishimura et al.: "Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product." in: The Journal of biological chemistry, Vol. 261, Issue 4, pp. 1778-81, 1986 (PubMed).

Bardwell, Tilly, Craig et al.: "The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein." in: The Journal of biological chemistry, Vol. 261, Issue 4, pp. 1782-5, 1986 (PubMed).

Ohtsuka: "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ." in: Biochemical and biophysical research communications, Vol. 197, Issue 1, pp. 235-40, 1994 (PubMed).

Melville, Hansen, Freeman et al.: "The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 1, pp. 97-102, 1997 (PubMed).