P21-Activated Kinase 6 (PAK6) antibody

Details for Product No. ABIN264684
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Antigen
Synonyms pak6, si:ch211-158b22.3, PAK5, 4732456M09
Reactivity
Human
(94), (31), (30), (19), (14), (12), (12), (2)
Host
Rabbit
(94), (1)
Clonality
Polyclonal
Conjugate
Un-conjugated
(4), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1)
Application
Western Blotting (WB)
(65), (30), (23), (20), (20), (16), (5), (5), (2), (1)
Pubmed 3 references available
Quantity 0.1 mg
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Catalog No. ABIN264684
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Immunogen Synthetic peptide corresponding to 13 amino acids near the center of human PAK6
Specificity This antibody reacts to the middle region of PAK6. The p21-activated kinases (PAKs) are serine-threonine kinases that bind to the active forms of Cdc42 and Rac. PAK6 proteins are not activated by Cdc42/Rac binding. PAK6 has been shown to be activated by MAP kinase kinase 6, and p38 MAP kinase, suggesting that PAK6 may play a role in the cellular response to stress-related signals.
Purification Immunoaffinity chromatography
Alternative Name PAK6
Background This gene encodes a protein that shares a high degree of sequence similarity with p21-activated kinase (PAK) family members. The proteins of this family are Rac/Cdc42-associated Ste20-like Ser/Thr protein kinases, characterized by a highly conserved amino-terminal Cdc42/Rac interactive binding (CRIB) domain and a carboxyl- terminal kinase domain. PAK kinases are implicated in the regulation of a number of cellular processes, including cytoskeleton rearrangement, apoptosis and the MAP kinase signaling pathway. The protein encoded by this gene was found to interact with androgen receptor (AR), which is a steroid hormone-dependent transcription factor that is important for male sexual differentiation and development. The p21-activated protein kinase 6 gene was found to be highly expressed in testis and prostate tissues and the encoded protein was shown to cotranslocate into the nucleus with AR in response to androgen. Regulation of PAK6 kinase activity occurs through multiple sites of phosphorylation. Activation of PAK6 requires autophosphorylation of Ser-560 and MKK-6 induced phosphorylation of Tyr-566. In addition, p38 MAPK can phosphorylate Ser-165, which increases PAK6 kinase activity. Thus, multiple signaling pathways may regulate the activity of PAK6 through differential phosphorylation. PAK6, a novel AR-interacting protein, shares a high degree of sequence similarity with p21-activated kinases. PAK6 cotranslocates into the nucleus with AR in response to androgen. In addition, AR and ERalpha transcriptional activites were inhibited by PAK6 in transient transfections with episomal and integrated reporter genes. PAK, which is highly expressed in testis and prostate tissues, could contribute to the effects of tamoxifen in breast cancer and in other tissues.
Alternate names: PAK-5, PAK-6, PAK5, Serine/threonine-protein kinase PAK 6, p21-activated kinase 6
Gene ID 56924
NCBI Accession NP_001122100
UniProt Q9NQU5
Research Area Signaling, Kinases/Phosphatases
Application Notes Western blot: 1 - 2g/ml.
Restrictions For Research Use only
Format Liquid
Buffer PBS containing 0.02% 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.
Handling Advice DO NOT FREEZE!
Storage 4 °C
Storage Comment Store the antibody undiluted at 2-8°C.
Expiry Date 12 months
Background publications Kaur, Liu, Gjoerup et al.: "Activation of p21-activated kinase 6 by MAP kinase kinase 6 and p38 MAP kinase." in: The Journal of biological chemistry, Vol. 280, Issue 5, pp. 3323-30, 2005 (PubMed).

Varadwaj, Varadwaj: "Can a single molecule of water be completely isolated within the subnano-space inside the fullerene C60 cage? A quantum chemical prospective." in: Chemistry (Weinheim an der Bergstrasse, Germany), Vol. 18, Issue 48, pp. 15345-60, 2012 (PubMed).

Taskin, Sasso, Dimaki et al.: "Combined cell culture-biosensing platform using vertically aligned patterned peptide nanofibers for cellular studies." in: ACS applied materials & interfaces, Vol. 5, Issue 8, pp. 3323-8, 2013 (PubMed).

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