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AV48129

Sigma-Aldrich

Anti-CD36 antibody produced in rabbit

affinity isolated antibody

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Synonym(s):
Anti-CD36 molecule (thrombospondin receptor), Anti-CHDS7, Anti-FAT, Anti-GP3B, Anti-GP4, Anti-GPIV, Anti-PASIV, Anti-SCARB3
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

mol wt

53 kDa

species reactivity

human

concentration

0.5 mg - 1 mg/mL

technique(s)

immunohistochemistry: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CD36(948)

General description

CD36 is a glycoprotein that functions as a receptor for thrombospondin in platelets. Studies have reported that TLR4 signaling inhibited the expression of CD36 and subsequently slowed hematoma absorption. CD36 mediates NLRP3 inflammasome stimulation during inflammation.
Rabbit Anti-CD36 antibody recognizes bovine, rabbit, canine, human, pig, and rat CD36.

Immunogen

Synthetic peptide directed towards the N terminal region of human CD36

Application

Rabbit Anti-CD36 antibody is suitable for western blot applications at a concentration of 1 μg/ml and for immunohistochemistry applications at a concentration of 4-8 μg/ml.

Biochem/physiol Actions

CD36 is the fourth major glycoprotein of the platelet surface and serves as a receptor for thrombospondin in platelets and various cell lines. Since thrombospondins are widely distributed proteins involved in a variety of adhesive processes, this protein may have important functions as a cell adhesion molecule. It binds to collagen, thrombospondin, anionic phospholipids and oxidized LDL. It directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes and it binds long chain fatty acids and may function in the transport and/or as a regulator of fatty acid transport. Mutations in its gene cause platelet glycoprotein deficiency.The protein encoded by this gene is the fourth major glycoprotein of the platelet surface and serves as a receptor for thrombospondin in platelets and various cell lines. Since thrombospondins are widely distributed proteins involved in a variety of adhesive processes, this protein may have important functions as a cell adhesion molecule. It binds to collagen, thrombospondin, anionic phospholipids and oxidized LDL. It directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes and it binds long chain fatty acids and may function in the transport and/or as a regulator of fatty acid transport. Mutations in this gene cause platelet glycoprotein deficiency. Three alternatively spliced transcript variants encoding the same protein isoform have been found for this gene.

Sequence

Synthetic peptide located within the following region: MGCDRNCGLIAGAVIGAVLAVFGGILMPVGDLLIQKTIKKQVVLEEGTIA

Physical form

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

Disclaimer

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.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Frederick J Sheedy et al.
Nature immunology, 14(8), 812-820 (2013-07-03)
Particulate ligands, including cholesterol crystals and amyloid fibrils, induce production of interleukin 1β (IL-1β) dependent on the cytoplasmic sensor NLRP3 in atherosclerosis, Alzheimer's disease and diabetes. Soluble endogenous ligands, including oxidized low-density lipoprotein (LDL), amyloid-β and amylin peptides, accumulate in
Huang Fang et al.
Journal of immunology (Baltimore, Md. : 1950), 192(12), 5984-5992 (2014-05-09)
Promoting hematoma absorption is a novel therapeutic strategy for intracerebral hemorrhage (ICH); however, the mechanism of hematoma absorption is unclear. The present study explored the function and potential mechanism of CD36 in hematoma absorption using in vitro and in vivo

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