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SRP3283

Sigma-Aldrich

FETUIN A human

recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE), ≥95% (HPLC)

Sinónimos:

Alpha-2-HS-glycoprotein

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50 μG
$280.000

$280.000


Fecha estimada de envío24 de abril de 2025


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50 μG
$280.000

About This Item

Número de CAS:
Código UNSPSC:
12352202
NACRES:
NA.32

$280.000


Fecha estimada de envío24 de abril de 2025


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origen biológico

human

recombinante

expressed in HEK 293 cells

Ensayo

≥95% (HPLC)
≥95% (SDS-PAGE)

Formulario

lyophilized

potencia

≥100 nM

mol peso

45.0-55.0 kDa

envase

pkg of 50 μg

impurezas

<0.1 EU/μg endotoxin, tested

color

white to off-white

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

Información sobre el gen

human ... AHSG(197)

Categorías relacionadas

Descripción general

The gene AHSG (α-2-HS-glycoprotein, also referred to as fetuin-A) is mapped to human chromosome 3q27.[1] Fetuin A/AHSG is a human plasma glycoprotein belonging to the Cystatin family of proteases inhibitors.[2][3] Fetuin A is highly expressed in embryonic cells and adult hepatocytes, and is expressed to a lesser extent in monocytes/macrophages.[4] The protein has cystatin-like domains, a calcium phosphate-binding site and a TGF (transforming growth factor)-β cytokine-binding motif.[1] Recombinant human fetuin-A is a heterodimeric protein containing a 282 amino acid A chain and a 27 amino acid B chain. Due to glycosylation, recombinant fetuin-A migrates at an apparent molecular weight of 45–55kDa by SDS-PAGE run under nonreducing conditions.

Aplicación

FETUIN A human has been used to stimulate mRNA expression in human monocytic THP1 cells, human in vitro differentiated adipocytes and C57BL/6 mice.[5]

Acciones bioquímicas o fisiológicas

AHSG (α-2-HS-glycoprotein, also referred to as fetuin-A) is a major serum protein component that exerts various calcium dependent physiological activities, and can mediate growth signaling in certain tumor cells.[2] It also can act as a natural antagonist against specific TGF-β (transforming growth factor β) and BMP (bone morphogenetic protein) signaling proteins.[1] High levels of fetuin-A in the serum is associated with mild osteogenesis imperfecta. On the other hand, reduced levels are seen in Paget′s disease.[1] It is predicted as a potential biomarker for the early diagnosis of hypopharyngeal squamous cell carcinoma.[6]

Forma física

Lyophilized from 10 mM Sodium Phosphate, pH 7.8.

Reconstitución

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Association of alpha2-HS glycoprotein (AHSG, fetuin-A) polymorphism with AHSG and phosphate serum levels.
Osawa M
Human Genetics, 116, 146-151 (2005)
Proteomic identification of alpha-2-HS-glycoprotein as a plasma biomarker of hypopharyngeal squamous cell carcinoma.
Tian WD
International Journal of Clinical and Experimental Pathology, 8, 9021-9031 (2015)
Fetuin-A induces cytokine expression and suppresses adiponectin production
Hennige AM, et al.
PLoS ONE, 3(3) (2008)
Melanie Szweras et al.
The Journal of biological chemistry, 277(22), 19991-19997 (2002-03-20)
Soluble transforming growth factor-beta (TGF-beta)/bone morphogenetic protein (BMP)-binding proteins are widely distributed in mammalian tissues and control cytokine access to membrane signaling receptors. The serum and bone-resident glycoprotein alpha2-HS-glycoprotein/fetuin (ASHG) binds to TGF-beta/BMP cytokines and blocks TGF-beta1 binding to cell
alpha 2-HS glycoprotein/fetuin, a transforming growth factor-beta/bone morphogenetic protein antagonist, regulates postnatal bone growth and remodeling.
Szweras M
The Journal of Biological Chemistry, 277, 19991-19997 (2002)

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