H4038
Anti-Heat Shock Protein 40 antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-HSP40
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~35 kDa
species reactivity
mouse, human
technique(s)
western blot: 1-2 μg/mL using total extracts of NIH3T3-L1 cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... DNAJB1(3337)
mouse ... Dnajb1(81489)
General description
Cells express an increased amount of several highly conserved proteins referred to as heat shock or heat stress proteins (Hsps). They are primarily found in the cytoplasm, nucleus, and mitochondria. Mammalian cells Hsps are classified into several families of sequence-related proteins, which are differentiated by their molecular sizes. Major families are as follows: the Hsp25/Hsp27/Hsp28 family (the small stress proteins), the Hsp40 family, the Hsp60 family, the Hsp70 family, the Hsp90 family, and the Hsp110/SSE family. HSP40, also known as DNAJB1, HSPF1, or HDJ1, is a 339-amino acid, stress inducible heat shock protein, that is homologous to the bacterial heat shock protein DnaJ, and to the yeast DnaJ-related proteins such as SCJ1, Sec63/Np11, YDJ1, and SIS1.
Heat Shock Protein 40 (HSP40) is a 40 kDa, stress inducible heat shock protein, that is homologous to the bacterial heat shock protein DnaJ, and to the yeast DnaJ-related proteins.
Immunogen
synthetic peptide corresponding to amino acids 323-339 of human HSP40, conjugated to KLH via an N-terminal added lysine residue. The peptide sequence differs from mouse in three amino acids.
Application
Anti-Heat Shock Protein 40 antibody produced in rabbit has been used in western blotting and microarray.
Biochem/physiol Actions
In heat-shocked cells, Hsp40 translocates from the cytoplasm to the nucleus and nucleoli, colocalizing with Hsp70. Hsp40 and Hsp70 have been implicated in reduction of protein aggregates produced in neurodegenerative diseases, such a Huntington′s and Parkinson′s diseases. In brain tissues from Parkinson disease patients, it has been shown that Lewy bodies (LBs) and Lewy neurites (LNs) are immunopositive for Hsp70 and Hsp40 chaperones, suggesting that altered chaperone activity may be involved in progression of Parkinson disease.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells
Michels AA, et al.
The Journal of Biological Chemistry, 274(51), 36757-36763 (1999)
HSF1 protects neurons through a novel trimerization-and HSP-independent mechanism
Verma P, et al.
The Journal of Neuroscience, 34(5), 1599-1612 (2014)
Development and application of an antibody-based protein microarray to assess physiological stress in grizzly bears (Ursus arctos)
Carlson RI, et al.
Conservation physiology, 4(1) (2016)
Lin Song et al.
PloS one, 9(12), e115752-e115752 (2014-12-30)
Heat shock proteins (HSPs) consist of a large group of chaperones whose expression is induced by high temperature, hypoxia, infection and a number of other stresses. Among all the HSPs, Hsp40 is the largest HSP family, which bind to Hsp70
A Wyttenbach et al.
Proceedings of the National Academy of Sciences of the United States of America, 97(6), 2898-2903 (2000-03-16)
Huntington's disease (HD), spinocerebellar ataxias types 1 and 3 (SCA1, SCA3), and spinobulbar muscular atrophy (SBMA) are caused by CAG/polyglutamine expansion mutations. A feature of these diseases is ubiquitinated intraneuronal inclusions derived from the mutant proteins, which colocalize with heat
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