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Merck
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重要文件

P3902

Sigma-Aldrich

Anti-Pyk2 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

同義詞:

Anti-CAK-β, Anti-Proline rich Kinase 2

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About This Item

MDL號碼:
分類程式碼代碼:
12352203
NACRES:
NA.44

生物源

rabbit

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous solution

分子量

antigen 110-116 kDa

物種活性

rat, mouse, human

技術

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100 using tissue sections of human cerebellum.
immunoprecipitation (IP): 3-5 μg/mL using 150-200 μg of PC-12 rat pheochromocytoma RIPA lysate
microarray: suitable
western blot: 1:2,000 using a whole extract of LPS-stimulated P388 mouse monocyte-macrophage cells

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... PTK2B(2185)
mouse ... Ptk2b(19229)
rat ... Ptk2b(50646)

一般說明

Pyk2 (proline-rich kinase 2) protein belongs to tyrosine protein kinase family and is primarily expressed in the central nervous system and in cells derived from hematopoietic lineages. Pyk2 is found in tissues and cells like mesenchymal, epithelial, endothelial cells, neonatal cardiomyocytes, osteoclasts and neuronal cells.

免疫原

Synthetic peptide corresponding to amino acid residues 991-1009 of human Pyk2, coupled to KLH. This sequence is highly conserved in rat and mouse (1 amino acid substitution).

應用

Anti-Pyk2 antibody produced in rabbit has been used in:
  • immunocytochemistry
  • immunohistochemistry
  • western blotting

生化/生理作用

Protein tyrosine kinases (PTKs) are critical components of the signalling pathways that control cell growth, differentiation, apoptosis, metabolism, cell cycle regulation and cytoskeletal function. Pyk2 has been detected in cell-cell contacts, at focal adhesion-like structures and podosomes, cytoplasmic perinuclear region, in association with actin filaments and diffusely distributed in the cytoplasm. Pyk2 phosphorylation is critical for its interaction with SH2-containing signalling molecules and their linkage to signalling pathways that regulate extracellular-signal-regulated kinase (ERK), Janus kinases (JNK) and p38 kinases. Pyk2 has been shown to interact with Src family kinases, the growth factor receptor-bound protein 2 (Grb2)/Sos complex, p130cas, paxillin, Hic-5, and several other proteins, including inhibitors, to regulate signalling as well as cytoskeletal and morphological changes of cells. It has a crucial role in T and B cell antigen receptor signaling, cell cycle progression, metastasis, NK cytotoxicity, modulation of ion channel function and neuronal short- and long- term responses.

外觀

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide

免責聲明

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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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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存取文件庫

Sponges: A reservoir of genes implicated in human cancer
Cetkovic H, et al.
Marine drugs, 16(1), 20-20 (2018)
Pyk2 is essential for astrocytes mobility following brain lesion
Giralt A, et al.
Glia, 64(4), 620-634 (2016)
Anirban Bhattachariya et al.
Physiological reports, 2(7) (2014-10-28)
Stretch of vascular smooth muscle stimulates growth and proliferation as well as contraction and expression of contractile/cytoskeletal proteins, all of which are also regulated by calcium-dependent signals. We studied the role of the calcium- and integrin-activated proline-rich tyrosine kinase 2
Regulation of a Calcium-dependent Tyrosine Kinase in Vascular Smooth Muscle Cells by Angiotensin II and Platelet-derived Growth Factor DEPENDENCE ON CALCIUM AND THE ACTIN CYTOSKELETON
Brinson AE, et al.
The Journal of Biological Chemistry, 273(3), 1711-1718 (1998)
Shakir Hasan et al.
Toxins, 11(6) (2019-06-23)
Myeloid phagocytes have evolved to rapidly recognize invading pathogens and clear them through opsonophagocytic killing. The adenylate cyclase toxin (CyaA) of Bordetella pertussis and the edema toxin (ET) of Bacillus anthracis are both calmodulin-activated toxins with adenylyl cyclase activity that

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