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Merck
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Documenti fondamentali

AV33888

Sigma-Aldrich

Anti-KLK6 antibody produced in rabbit

affinity isolated antibody

Sinonimo/i:

Anti-Bssp, Anti-Kallikrein-related peptidase 6, Anti-Klk7, Anti-MGC9355, Anti-NEUROSIN, Anti-PRSS18, Anti-PRSS9, Anti-SP59

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

PM

25 kDa

Reattività contro le specie

human

Concentrazione

0.5 mg - 1 mg/mL

tecniche

immunohistochemistry: suitable
western blot: suitable

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... KLK6(5653)

Descrizione generale

Kallikrein-6 (KLK6) also known as zyme is part of a family of serine proteases that targets xtracellular proteins including fibronectin, vitronectin and laminin. It is found highly expressed in the brain where it has been shown to be involved in degradation of amyloid plaque protein. Additionally, it has been implicated in carcinogensis and is being investigated for its potential as a target for cancer therapy.

Immunogeno

Synthetic peptide directed towards the N terminal region of human KLK6

Azioni biochim/fisiol

Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. The gene that encodes KLK6 protein is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK6 is regulated by steroid hormones. In tissue culture, the enzyme has been found to generate amyloidogenic fragments from the amyloid precursor protein, suggesting a potential for involvement in Alzheimer′s disease.Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. The encoded enzyme is regulated by steroid hormones. In tissue culture, the enzyme has been found to generate amyloidogenic fragments from the amyloid precursor protein, suggesting a potential for involvement in Alzheimer′s disease. Multiple alternatively spliced transcript variants that encode different isoforms have been identified for this gene.

Sequenza

Synthetic peptide located within the following region: KHNLRQRESSQEQSSVVRAVIHPDYDAASHDQDIMLLRLARPAKLSELIQ

Stato fisico

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Esclusione di responsabilità

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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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Angeliki Magklara et al.
Biochemical and biophysical research communications, 307(4), 948-955 (2003-07-25)
Human kallikrein 6 (hK6) is a trypsin-like serine protease, member of the human kallikrein gene family. Studies suggested a potential involvement of hK6 in the development and progression of Alzheimer's disease. The serum levels of hK6 might be used as
Jiayi Yao et al.
Circulation research, 117(9), 758-769 (2015-08-13)
Endothelial cells have the ability to undergo endothelial-mesenchymal transitions (EndMTs), by which they acquire a mesenchymal phenotype and stem cell-like characteristics. We previously found that EndMTs occurred in the endothelium deficient in matrix γ-carboxyglutamic acid protein enabling endothelial cells to

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