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Key Documents

ABS1020

Sigma-Aldrich

Anti-Acylation Stimulating Protein Antibody

from rabbit

Sinónimos:

Complement C3, C3adesArg, C3, PZP-like alpha-2-macroglobulin domain-containing protein 1

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human

technique(s)

ELISA: suitable
flow cytometry: suitable
neutralization: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... C3(718)

General description

The protein called Acylation stimulating protein (ASP) is a cleavage fragment protein from the Complement C3 gene. C3 plays a central role in the activation of the complement system. C3’s processing by C3 convertase is the central reaction in both classical and alternative complement pathways. ASP acts as an adipogenic hormone that stimulates triglyceride synthesis and glucose transport in adipocytes, and thus it helps regulate fat storage and triglyceride synthesis. ASP stimulates triglyceride synthesis via PLC, MAPK and AKT signaling pathways and ASP promotes the phosphorylation and internalization and recycling of Complement factor C5AR2. ASP is expressed in adipocytes and released into the plasma during both the fasting and postprandial periods. Increased levels of C3 and its cleavage product ASP are associated with obesity, diabetes and coronary heart disease. Short-term endurance training reduces baseline ASP levels and subsequently fat storage.

Immunogen

recombinant protein corresponding to Human Acylation Stimulating Protein.

Application

Flow Cytometry Analysis: 10 µg/mL of this antibody blocked ASP binding to HEK-hCL52 cells (Wei, C,. et al, Am J Physiol Endocrinol Metab 293:E1482-E1491, 2007)
Neutralizing Assay Analysis: A representative lot of this antibody demonstrated neutralizing effect of ASP stimulation of TG synthesis and glucose transport in HEK-hC5L2 cells,
3T3-L1 preadipocytes, and 3T3-L1 adipocytes (Wei, C,. et al, Am J Physiol Endocrinol Metab 293:E1482-E1491, 2007)
ELISA Analysis: 0.5 µg/mL of this antibody detected ASP (PEG precipitated) in a sandwich ELISA format (Saleh, J,. et al, J. Lipid Res. 1998. 39: 884–891)
This Anti-Acylation Stimulating Protein Antibody is validated for use in Western Blotting and Flow Cytometry and Neutralizing and ELISA for the detection of Acylation Stimulating Protein.

Quality

Evaluated by Western Blotting in HEK293 expressing ASP cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected Acylation Stimulating Protein in 10 µg of HEK293 expressing ASP cell lysate.

Target description

~ 16/10 kDa observed, 10 kDa indicates native ASP, 16 kDa indicates HIS-Tag ASP. HIS-Tag was added for purification purposes. We have found no difference in Activity (measured by TGS, Fatty Acid uptake, etc) between rASP with/without the tag. Further, the ELISA was successful in measuring both.

Physical form

Format: Purified

Other Notes

Concentration: Please refer to lot specific datasheet.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Acylation-stimulating protein/C5L2-neutralizing antibodies alter triglyceride metabolism in vitro and in vivo.
Cui, W; Paglialunga, S; Kalant, D; Lu, H; Roy, C; Laplante, M; Deshaies, Y; Cianflone, K
American Journal of Physiology. Endocrinology and Metabolism null
The effects of acylation stimulating protein supplementation VS antibody neutralization on energy expenditure in wildtype mice.
Paglialunga, S; Fisette, A; Munkonda, M; Gao, Y; Richard, D; Cianflone, K
BMC Physiology null
J Saleh et al.
Journal of lipid research, 39(4), 884-891 (1998-04-29)
The objective of this study was to determine whether Acylation Stimulating Protein (ASP) is generated in vivo by human adipose tissue during the postprandial period. After a fat meal, samples from 12 subjects were obtained (up to 6 h) from

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