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Merck
모든 사진(2)

Key Documents

P3902

Sigma-Aldrich

Anti-Pyk2 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

동의어(들):

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

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.44

생물학적 소스

rabbit

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

polyclonal

형태

buffered aqueous solution

분자량

antigen 110-116 kDa

종 반응성

rat, mouse, human

기술

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 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

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

일반 설명

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.

면역원

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).

애플리케이션

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

생화학적/생리학적 작용

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.

물리적 형태

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

면책조항

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

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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