Ydj1p (YDJ1) antibody

Details for Product No. ABIN361661
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Antigen
Reactivity
Yeast
(15)
Host
Mouse
(15)
Clonality (Clone)
Monoclonal ()
Application
Western Blotting (WB), Immunoprecipitation (IP), ELISA
(15), (15), (15)
Pubmed 8 references available
Catalog no. ABIN361661
Quantity 25 µg
Price
220.00 $   Plus shipping costs $45.00
Options
Shipping to United States (Change)
Availability Will be delivered in 3 to 4 Business Days

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen Full length protein Hsp40 (YDJ1)
Clone 2A7-H6
Isotype IgG1 kappa
Specificity Detects approx. 40 kDa.
Sensitivity 0.5 µg/mL of SMC-166 was sufficient for detection of 50 ng YDJ1 by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Alternative Name Hsp40, YDJ1
Background Synonyms:
DNAJ1, DNAJB1, HDJ1, Hsp40, HSPF1
Human Hsp40/DnaJ proteins comprise a large protein family, members of which feature the J domain (named after the bacterial DnaJ protein). The J-domain spans the first 75 N-terminal amino acids and is separated from the C-terminal by a glycine/phenylalanine-rich domain. Members of the Hsp40/DnaJ family play diverse roles in many cellular processes, such as folding, translocation, degradation and assembly of multi-protein complexes. In particular, Hdj1, the first human Hsp40/DnaJ protein identified, plays an important role in protein translation and folding, as well as in the regulation of Hsp70 function. HSP40 stimulates the ATPase activity of HSP70 which in turn causes conformational changes of the unfolded proteins. The Hsp40-Hsp70-unfolded protein complex further binds to co-chaperones Hip, Hop and HSP90 which leads to protein folding, or components of protein degradationmachinery CHIP and BAG-1. Some studies have shown that the difference between HDJ1 and type 1 DNAJ proteins including HDJ2 and yeast YdjI is the result of the possession of a zinc finger domain by the latter, which helps in the function of protein folding..
Gene ID 855661
NCBI Accession NP_014335.1
UniProt P25491
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: 1:2000 (WB)
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Storage -20 °C
Supplier Images
anti-Ydj1p (YDJ1) antibody Hsp40 (YDJ1 2A7 H6), 0.
Background publications Cyr, Lu, Douglas: "Regulation of Hsp70 function by a eukaryotic DnaJ homolog." in: The Journal of biological chemistry, Vol. 267, Issue 29, pp. 20927-31, 1992 (PubMed).

Liberek, Marszalek, Ang et al.: "Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, Issue 7, pp. 2874-8, 1991 (PubMed).

Terada, Kanazawa, Bukau et al.: "The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding." in: The Journal of cell biology, Vol. 139, Issue 5, pp. 1089-95, 1997 (PubMed).

Cheetham, Caplan: "Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function." in: Cell stress & chaperones, Vol. 3, Issue 1, pp. 28-36, 1998 (PubMed).

Lu, Cyr: "Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1." in: The Journal of biological chemistry, Vol. 273, Issue 43, pp. 27824-30, 1998 (PubMed).

Höhfeld, Cyr, Patterson: "From the cradle to the grave: molecular chaperones that may choose between folding and degradation." in: EMBO reports, Vol. 2, Issue 10, pp. 885-90, 2001 (PubMed).

Fan, Lee, Cyr: "Mechanisms for regulation of Hsp70 function by Hsp40." in: Cell stress & chaperones, Vol. 8, Issue 4, pp. 309-16, 2004 (PubMed).

Sohn, Kim, Kim et al.: "Negative regulation of hepatitis B virus replication by cellular Hsp40/DnaJ proteins through destabilization of viral core and X proteins." in: The Journal of general virology, Vol. 87, Issue Pt 7, pp. 1883-91, 2006 (PubMed).

Hosts (15)
Reactivities (15)
Applications (15), (15), (15)
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Validation Images
back to top