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SRP3199

Sigma-Aldrich

gAcrp30 from mouse

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

mouse

recombinant

expressed in E. coli

assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

potency

<15 μg/mL

mol wt

16.6 kDa

packaging

pkg of 25 μg

technique(s)

cell culture | mammalian: suitable

impurities

<0.1 EU/μg endotoxin, tested

color

white to off-white

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

mouse ... ADIPOQ(11450)

General description

gAcrp30 is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, gAcrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. Recombinant murine gAcrp30 is a 16.6 kDa protein consisting of 145 amino acid residues.

Biochem/physiol Actions

gAcrp30 is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Recombinant murine gAcrp30 is a 16.6 kDa protein consisting of 145 amino acid residues.

Sequence

MKGEPGEAAY MYRSAFSVGL ETRVTVPNVP IRFTKIFYNQ QNHYDGSTGK FYCNIPGLYY FSYHITVYMK DVKVSLFKKD KAVLFTYDQY QEKNVDQASG SVLLHLEVGD QVWLQVYGDG DHNGLYADNV NDSTFTGFLL YHDTN

Physical form

Lyophilized from 5 mM Tris, pH 7.6.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in 5 mM Tris, pH 7.6 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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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E Hu et al.
The Journal of biological chemistry, 271(18), 10697-10703 (1996-05-03)
Adipose differentiation is accompanied by changes in cellular morphology, a dramatic accumulation of intracellular lipid and activation of a specific program of gene expression. Using an mRNA differential display technique, we have isolated a novel adipose cDNA, termed adipoQ. The
P E Scherer et al.
The Journal of biological chemistry, 270(45), 26746-26749 (1995-11-10)
We describe a novel 30-kDa secretory protein, Acrp30 (adipocyte complement-related protein of 30 kDa), that is made exclusively in adipocytes and whose mRNA is induced over 100-fold during adipocyte differentiation. Acrp30 is structurally similar to complement factor C1q and to
J Fruebis et al.
Proceedings of the National Academy of Sciences of the United States of America, 98(4), 2005-2010 (2001-02-15)
Adipocyte complement-related protein (30 kDa) (Acrp30), a secreted protein of unknown function, is exclusively expressed in differentiated adipocytes; its mRNA is decreased in obese humans and mice. Here we describe novel pharmacological properties of the protease-generated globular head domain of

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