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H0161

Sigma-Aldrich

Hyaluronic Acid Binding Protein bovine

lyophilized powder

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1 ML
$184.00
0.1 ML
$206.00
0.5 ML
$531.00
7 ML
$568.00
1 ML
$830.00

$184.00

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All Photos(1)

Select a Size

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1 ML
$184.00
0.1 ML
$206.00
0.5 ML
$531.00
7 ML
$568.00
1 ML
$830.00

About This Item

MDL number:
MFCD02099073
UNSPSC Code:
12352202
NACRES:
NA.56

$184.00

Check Cart for Availability

biological source

bovine

Quality Level

200

form

lyophilized powder

technique(s)

immunofluorescence: suitable

UniProt accession no.

P81282

storage temp.

−20°C

Gene Information

cow ... VCAN(282662)

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species reactivity

human

species reactivity

human

species reactivity

human

species reactivity

human

antibody form

culture supernatant

antibody form

culture supernatant

antibody form

culture supernatant

antibody form

culture supernatant

biological source

rabbit

biological source

rabbit

biological source

rabbit

biological source

rabbit

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

clone

EPR3653, monoclonal

clone

EP88, monoclonal

clone

EP3622, monoclonal

clone

EP204, monoclonal

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

General description

Hyaluronic acid (HA) is a linear polysaccharide consisting of a repeating disaccharide of N-acetyl D-glucosamine (GlcNAc) and D-glucuronic acid (GlcA) with 1→4 interglycosidic linkages and these disaccharide repeating units are in turn linked by β (1→3) linkages. The number of repeating disaccharides in a HA molecule ranges from 2,000 to 25,000, which relates to a molecular mass of 106-107. The unique biological roles of HA is mainly due to the specific binding and interaction with HA-binding proteins also known as hyaladherins. Most hyaladherins is composed of a specific binding domain, also called a link module, which is composed of two α-helices and two antiparallel β-sheets.[1]
Karl Meyer and John Palmer first isolated hyaluronic acid (HA) from the vitreous of bovine eyes. They coined the name “hyaluronic acid” as a conjugation of two words, hyaloid (vitreous) and uronic acid. HA has an extended random coil structure in physiological solution. Due to its random-coil structure and high molecular weight (HMW), HA forms very viscose and elastic solution with a huge hydrodynamic volume.

Application

Hyaluronic Acid Binding Protein bovine may be used for incubation of specimens for immunofluorescence analysis of human megakaryocytes.[2]

Biochem/physiol Actions

Hyaluronic Acid Binding Protein (HABP) levels increases during oocyte maturation and it promotes cumulus expansion during in vitro maturation.[3]
In addition to being an important structural component of tissues in all vertebrates, HA is also associated with several biological functions including intracellular signaling.[1]
May be useful in hyaluronic acid binding or detection.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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    Certificates of Analysis (COA)

    Lot/Batch Number
    0000408524
    0000408524
    0000310836
    0000319060
    SLCM4619

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    Hyaluronan based hydrogels provide an improved model to study megakaryocyte-matrix interactions
    Currao M, et al.
    Experimental Cell Research, 346(1), 1-8 (2016)
    A G Haus
    Radiologic clinics of North America, 25(5), 913-928 (1987-09-01)
    Today there are many dedicated mammographic x-ray units available that are capable of providing high-quality screen-film mammograms. Likewise, screen-film combinations designed for mammography are capable of providing images with appropriate contrast, resolution, and noise levels. Proper film processing is most
    Identification of hyaluronic acid-binding proteins and their expressions in porcine cumulus-oocyte complexes during in vitro maturation
    Yokoo M, et al.
    Biology of Reproduction, 67(4), 1165-1171 (2002)
    G Perides et al.
    The Journal of biological chemistry, 264(10), 5981-5987 (1989-04-05)
    A glial hyaluronate-binding protein (GHAP) with an isoelectric point of 4.3-4.4 was isolated from human brain white matter. The 60-kDa glycoprotein appeared to be quite resistant to proteolysis, and comparison with GHAP from a viable glioma removed at surgery showed
    Tal M Dankovich et al.
    Nature communications, 12(1), 7129-7129 (2021-12-10)
    The brain extracellular matrix (ECM) consists of extremely long-lived proteins that assemble around neurons and synapses, to stabilize them. The ECM is thought to change only rarely, in relation to neuronal plasticity, through ECM proteolysis and renewed protein synthesis. We

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