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Merck
CN

H4038

Anti-Heat Shock Protein 40 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

别名:

Anti-HSP40

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
WB
Citations:
12
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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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存储类别

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

法规信息

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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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H Hattori et al.
Journal of cell science, 104 ( Pt 3), 629-638 (1993-03-01)
We have previously reported that a novel 40 kDa protein is induced by heat shock and several environmental stresses in mammalian and avian cells and that the N-terminal amino acid sequence of this 40 kDa protein has homology with the
A stress-inducible 40 kDa protein (hsp40): purification by modified two-dimensional gel electrophoresis and co-localization with hsc70 (p73) in heat-shocked HeLa cells
Hattori H, et al.
Journal of Cell Science, 104(3), 629-638 (1993)
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)
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)
HSF1 protects neurons through a novel trimerization-and HSP-independent mechanism
Verma P, et al.
The Journal of Neuroscience, 34(5), 1599-1612 (2014)

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