Antibody data
- Antibody Data
- Antigen structure
- References [6]
- Comments [0]
- Validations [0]
Submit
Validation data
Reference
Comment
Report error
- Product number
- ABIN967734 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Protein Kinase C, epsilon (PRKCE) (AA 1-175) antibody
- Antibody type
- Monoclonal
- Antigen
- Human PKCepsilon
- Reactivity
- Human
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- 21
- Vial size
- 50 µg
- Concentration
- 250 µg/ml
- Storage
- Store undiluted at -20° C.
Submitted references Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria.
Formation of protein kinase C(epsilon)-Lck signaling modules confers cardioprotection.
Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon ), facilitating PKCepsilon translocation via enhanced PKCepsilon -RACK2 interactions: a novel mechanism of no-triggered activation of PKCepsilon.
A requirement for protein kinase C inhibition for calcium-triggered apoptosis in acute lymphoblastic leukemia cells.
Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC.
Expression of protein kinase C genes in hemopoietic cells is cell-type- and B cell-differentiation stage specific.
Baines CP, Song CX, Zheng YT, Wang GW, Zhang J, Wang OL, Guo Y, Bolli R, Cardwell EM, Ping P
Circulation research 2003 May 2;92(8):873-80
Circulation research 2003 May 2;92(8):873-80
Formation of protein kinase C(epsilon)-Lck signaling modules confers cardioprotection.
Ping P, Song C, Zhang J, Guo Y, Cao X, Li RC, Wu W, Vondriska TM, Pass JM, Tang XL, Pierce WM, Bolli R
The Journal of clinical investigation 2002 Feb;109(4):499-507
The Journal of clinical investigation 2002 Feb;109(4):499-507
Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon ), facilitating PKCepsilon translocation via enhanced PKCepsilon -RACK2 interactions: a novel mechanism of no-triggered activation of PKCepsilon.
Balafanova Z, Bolli R, Zhang J, Zheng Y, Pass JM, Bhatnagar A, Tang XL, Wang O, Cardwell E, Ping P
The Journal of biological chemistry 2002 Apr 26;277(17):15021-7
The Journal of biological chemistry 2002 Apr 26;277(17):15021-7
A requirement for protein kinase C inhibition for calcium-triggered apoptosis in acute lymphoblastic leukemia cells.
Zhu DM, Fang WH, Narla RK, Uckun FM
Clinical cancer research : an official journal of the American Association for Cancer Research 1999 Feb;5(2):355-60
Clinical cancer research : an official journal of the American Association for Cancer Research 1999 Feb;5(2):355-60
Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC.
Ohno S, Akita Y, Hata A, Osada S, Kubo K, Konno Y, Akimoto K, Mizuno K, Saido T, Kuroki T
Advances in enzyme regulation 1991;31:287-303
Advances in enzyme regulation 1991;31:287-303
Expression of protein kinase C genes in hemopoietic cells is cell-type- and B cell-differentiation stage specific.
Mischak H, Kolch W, Goodnight J, Davidson WF, Rapp U, Rose-John S, Mushinski JF
Journal of immunology (Baltimore, Md. : 1950) 1991 Dec 1;147(11):3981-7
Journal of immunology (Baltimore, Md. : 1950) 1991 Dec 1;147(11):3981-7
No comments: Submit comment
No validations: Submit validation data