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Cyclin-Dependent Kinase 5, Regulatory Subunit 1 (p35) (CDK5R1) antibody

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Synonyms Xp35.1, cdk5r1, p35, zgc:92814, CDK5R1, CDK5P35, CDK5R, NCK5A, p23, p25, p35nck5a, Cdk5r, D11Bwg0379e, P25/P35, 1110014C03Rik, Tmp21, p24delta1, PCHK23, TCTP
Chicken, Guinea Pig, Human, Mouse (Murine), Rabbit, Yeast
(92), (46), (26), (19), (17), (17), (17), (2), (2)
(68), (25), (1)
Clonality (Clone)
Monoclonal ()
(6), (6), (6), (5), (5), (5), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blotting (WB)
(62), (59), (53), (28), (20), (19), (11), (5)
Pubmed 9 references available
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Quantity 100 μg
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Immunogen Recombinant human full length p23 protein
Clone JJ6
Specificity Detects ~23 kDa.
Sensitivity 0.5 µg/mL of SMC-156 was sufficient for detection of p23 in 20 µg of heat shocked cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Alternative Name p23 (CDK5R1 Antibody Abstract)
Background P23 is a highly conserved ubiquitous protein, known to have an important function as a cochaperone for the HSP90 chaperoning system (1). Studies have revealed that p23 is a small protein (18 to 25 kDa) with a simple structure (2, 3). p23 does not have any structural homology with any other known proteins (1). p23 was first discovered as a part of the HSP90-progesterone receptor complex along with HSP70, p54 and p50 (1). p23 is a phosphor-protein, which is highly acidic and has an aspartic acid-rich c-terminal domain (1). Numerous studies have found p23 to be associated with other client proteins like Fes tyrosine kinase (4), the heme regulated kinase HRI (5), hsf1 transcription factor (4), aryl hydrocarbon receptor (4), telomerase (6), and Hepadnavirus reverse transcriptase (7). In spite of several years of study, the exact functional significance of p23 is still not clear (8). p23 is thought to be involved in the adenosine triphosphate-mediated HSP90 binding of client proteins (8). Since many HSP90 client proteins are involved in oncogenic survival signaling, a recent study has concluded p23 to be a promising target in leukemic apoptosis (9). HSP90 and its co-chaperone p23 are certainly among the emerging anti-tumor targets in oncology.
Cellular Localization: Cytoplasm
Gene ID 10728
NCBI Accession NP_006592
UniProt Q15185
Research Area Cancer, Metabolism
Application Notes Recommended Dilution: WB (1:2000) IHC (1:100), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
Image no. 1 for anti-Cyclin-Dependent Kinase 5, Regulatory Subunit 1 (p35) (CDK5R1) antibody (ABIN361805) P23 (JJ6) human cell line mix copy.
Product cited in: Shimamura, Perera, Foley et al.: "Ganetespib (STA-9090), a nongeldanamycin HSP90 inhibitor, has potent antitumor activity in in vitro and in vivo models of non-small cell lung cancer." in: Clinical cancer research : an official journal of the American Association for Cancer Research, Vol. 18, Issue 18, pp. 4973-85, 2012 (PubMed).

Background publications Felts, Toft: "p23, a simple protein with complex activities." in: Cell stress & chaperones, Vol. 8, Issue 2, pp. 108-13, 2003 (PubMed).

Hu, Toft, Anselmo et al.: "In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins." in: Journal of virology, Vol. 76, Issue 1, pp. 269-79, 2001 (PubMed).

Weaver, Sullivan, Felts et al.: "Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone." in: The Journal of biological chemistry, Vol. 275, Issue 30, pp. 23045-52, 2000 (PubMed).

Weikl, Abelmann, Buchner: "An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function." in: Journal of molecular biology, Vol. 293, Issue 3, pp. 685-91, 1999 (PubMed).

Holt, Aisner, Baur et al.: "Functional requirement of p23 and Hsp90 in telomerase complexes." in: Genes & development, Vol. 13, Issue 7, pp. 817-26, 1999 (PubMed).

Nair, Toran, Rimerman et al.: "A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor." in: Cell stress & chaperones, Vol. 1, Issue 4, pp. 237-50, 1997 (PubMed).

Pingoud, Jeltsch: "Recognition and cleavage of DNA by type-II restriction endonucleases." in: European journal of biochemistry / FEBS, Vol. 246, Issue 1, pp. 1-22, 1997 (PubMed).

Johnson, Beito, Krco et al.: "Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes." in: Molecular and cellular biology, Vol. 14, Issue 3, pp. 1956-63, 1994 (PubMed).

Catalog No. ABIN361805
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