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Merck
모든 사진(1)

Key Documents

G3670

Sigma-Aldrich

Galectin-8 from rat

recombinant, expressed in E. coli, ≥90% (SDS-PAGE), buffered aqueous glycerol solution

동의어(들):

Gal-8, Po66 carbohydrate-binding protein, Prostate carcinoma tumor antigen 1

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About This Item

MDL number:
UNSPSC 코드:
12352202

생물학적 소스

rat

재조합

expressed in E. coli

분석

≥90% (SDS-PAGE)

형태

buffered aqueous glycerol solution

분자량

protein 34 kDa

포장

pkg of 100 μg

기술

cell culture | mammalian: suitable

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

유전자 정보

일반 설명

Galectin-8 is one of the β-galactoside-binding lectins called galectins, which reside in the cytosol before being released in a signal sequence-independent pathway.

생화학적/생리학적 작용

Galectin-8 functions as a danger receptor and thus, prevents the proliferation of Salmonella. It detects host glycans found on the surface of damaged Salmonella-containing vacuoles. It also maintains the endo-lysosomal integrity. This protein prevents the adhesion of human carcinoma cells to integrin-ligand coated plates. This results in induction of apoptosis.
Galectin-8 is a family member of animal lectins which selectively binds β-galactoside residues. It is a widely expressed 34 kDa protein, which is secreted by many cell types. Galectin-8 is made of two homol­o­gous regions, each having a single carbohydrate recognition domain (CRD), linked by a short peptide. Galectin-8 acts as a physiological modulator of cell adhesion and cellular growth, and may be involved in neoplastic transformation.

물리적 형태

Solution containing 20 mM Tris, pH 7.4, 1 mM DTT, 1 mM EDTA, and 30% glycerol.

분석 메모

The biological activity is measured by its ability to agglutinate human red cells.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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문서 라이브러리 방문

Osamu Suzuki et al.
International journal of oncology, 46(3), 973-980 (2015-01-13)
The interaction between cell surface glycans and extracellular matrix (ECM) including galectins is known to be closely associated with tumor cell adhesion, invasion and metastasis. We analyzed the roles of cell surface sialylation or glycosylation in galectin or ECM‑mediated cell
Y Levy et al.
The Journal of biological chemistry, 276(33), 31285-31295 (2001-05-24)
The interaction of cells with the extracellular matrix regulates cell adhesion and motility. Here we demonstrate that different cell types adhere and spread when cultured in serum-free medium on immobilized galectin-8, a mammalian beta-galactoside-binding protein. At maximal doses, galectin-8 is
Teresa L M Thurston et al.
Nature, 482(7385), 414-418 (2012-01-17)
Autophagy defends the mammalian cytosol against bacterial infection. Efficient pathogen engulfment is mediated by cargo-selecting autophagy adaptors that rely on unidentified pattern-recognition or danger receptors to label invading pathogens as autophagy cargo, typically by polyubiquitin coating. Here we show in
I Camby et al.
Brain pathology (Zurich, Switzerland), 11(1), 12-26 (2001-01-06)
Galectins, a family of mammalian lectins with specificity to beta-galactosides, are involved in growth-regulatory mechanisms and cell adhesion. A relationship is assumed to exist between the levels of expression of galectins and the level of malignancy in human gliomas. A
Y R Hadari et al.
Journal of cell science, 113 ( Pt 13), 2385-2397 (2000-06-15)
The interaction of cells with the extracellular matrix regulates cell adhesion, motility, growth, survival and differentiation through integrin-mediated signal transduction. Here we demonstrate that galectin-8, a secreted mammalian (beta)-galactoside binding protein, inhibits adhesion of human carcinoma (1299) cells to plates

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