Hsp40/DNAJ (C-Term) antibody

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(4), (3), (2)
Plasmodium falciparum
(33), (16), (16), (3), (2), (1), (1), (1), (1)
(27), (10)
(1), (1)
Western Blotting (WB), Immunofluorescence (IF)
(33), (17), (12), (11), (10), (5), (5), (2)
Pubmed 9 references available
Catalog no. ABIN361684
Quantity 25 µg
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Immunogen C-terminal peptide of Pf11_0513 conjugated to KLH
Specificity Detects an 62 kDa protein, corresponding to P.falciparum Hsp40 on SDS PAGE immunoblot, in samples from P.Falciparum origin.
It is species specific to P.falciparum, does not cross-rect to any protein from human erythrocytes.
Purification Protein A Purified
Alternative Name Hsp40
Background Synonyms:
HSPB2, also known as MKBP is the most divergent member of the sHSP family with only 30 % sequence identity to all other mammalian sHSPS. MKBP is known to associate specifically with myotonic dystrophy protein kinase (DMPK) in skeletal muscle. MKBP enhances the kinase activity of DMPK and protects it from heat-induced activation. MKBP also shows a unique nature compared to other sHSps, in that the expression of MKBP is not induced by heat shock. In unstressed skeletal muscle, MKBP forms large oligomeric complexes with HSPB3 in the cytosol which are localized on mitochondria and the neuromuscular junction. During stress, these complexes dissolve and MKBP’s localization to mitochondria increases, leading to increased cell survival. Pinz et al. tried to find a distinct role for MKBP in terms of cardiac mechanics and finds that it is required for normal systolic performance and normal cardiac energetic.HSPB2 has also been found to be expressed in several cancer cell lines, including human breast cancer, suggesting that MKBP may be an important factor in tumor transformation and metastasis.
Gene ID 811045
NCBI Accession XP_001348169.2
UniProt Q8IHM7
Research Area Signaling, Heat Shock Proteins
Application Notes Recommended Dilution: 1:2000 (WB), 1:50 (IF)
Restrictions For Research Use only
Concentration 1.8 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Storage -20 °C
Supplier Images
anti-Hsp40/DNAJ (C-Term) antibody Hsp40 (Pf11_01513), malarial parasite lysate.
Background publications Suzuki, Sugiyama, Hayashi et al.: "MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase." in: The Journal of cell biology, Vol. 140, Issue 5, pp. 1113-24, 1998 (PubMed).

Sugiyama, Suzuki, Kishikawa et al.: "Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation." in: The Journal of biological chemistry, Vol. 275, Issue 2, pp. 1095-104, 2000 (PubMed).

Pinz, Robbins, Rajasekaran et al.: "Unmasking different mechanical and energetic roles for the small heat shock proteins CryAB and HSPB2 using genetically modified mouse hearts." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 22, Issue 1, pp. 84-92, 2008 (PubMed).

General 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).

Hosts (27), (10)
Reactivities (33), (16), (16), (3), (2), (1), (1), (1), (1)
Applications (33), (17), (12), (11), (10), (5), (5), (2)
Conjugates (1), (1)
Epitopes (4), (3), (2)
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