protein

Recombinant Human Adiponectin glycosilated, HEK

MBS142310

0.002 mg

140 USD

Recombinant Protein

Recombinant Human Adiponectin glycosilated, HEK

Adiponectin glycosilated

Acrp30 Human, HEK; Adiponectin Human Recombinant, HEK; Acrp30; AdipoQ; GBP-28; APM-1; ACDC; Acrp30 HEK

adiponectin; Adiponectin; adiponectin; 30 kDa adipocyte complement-related protein; adipocyte complement-related 30 kDa protein; adipose most abundant gene transcript 1 protein; adipose specific collagen-like factor; gelatin-binding protein 28; adiponectin, C1Q and collagen domain containing; 30 kDa adipocyte complement-related protein; Adipocyte complement-related 30 kDa protein; ACRP30; Adipocyte, C1q and collagen domain-containing protein; Adipose most abundant gene transcript 1 protein; apM-1; Gelatin-binding protein

Acrp30

ADIPOQ; ADIPOQ; ACDC; ADPN; APM1; APM-1; GBP28; ACRP30; ADIPQTL1; ACDC; ACRP30; APM1; GBP28; ACRP30; apM-1

ADIPO_HUMAN

HEK293 (Human Embryonic Kidney cell line)

244

ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

Greater than 98% as determined by HPLC and SDS PAGE.

Filtered (0.4 um) and lyophilized from 0.5 mg/ml in 20mM Tris Buffer, 20mM NaCl, pH 7.5. White lyophilized (freeze-dried) powder.

For long term, store lyophilized AdipoQ at -20 degree C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4 degree C for a limited period of time; it does not show any change after two weeks at 4 degree C. The lyophilized protein remains stable for 24 months when stored at -20 degree C.

Activity in vitro: In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 ug/ml.

Patent Rights: The sale and/or commercial use of Recombinant Adiponectin is prohibited in the United States of America (U.S.A). Solubility: Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.

CYTOKINES AND GROWTH FACTORS; Cytokines; Adiponectin

Description: The Acrp30 Human Recombinant produced in HEK293 cells is fused with FLAG tag. Introduction: Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

295317372

NP_001171271.1

NM_001177800.1

Q15848

26,414 Da

AMPK Signaling Pathway (198868); AMPK Signaling Pathway (989139); AMPK Signaling Pathway (992181); Adipocytokine Signaling Pathway (83093); Adipocytokine Signaling Pathway (505); Adipogenesis Pathway (198832); Developmental Biology Pathway (477129); Non-alcoholic Fatty Liver Disease (NAFLD) Pathway (862188); Non-alcoholic Fatty Liver Disease (NAFLD) Pathway (862314); PPAR Signaling Pathway (83042)

This gene is expressed in adipose tissue exclusively. It encodes a protein with similarity to collagens X and VIII and complement factor C1q. The encoded protein circulates in the plasma and is involved with metabolic and hormonal processes. Mutations in this gene are associated with adiponectin deficiency. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Apr 2010]

adiponectin: Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW. Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely aditionally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts with CTRP9A via the C1q domain (heterotrimeric complex). Synthesized exclusively by adipocytes and secreted into plasma. Protein type: Endoplasmic reticulum; Secreted, signal peptide; Secreted; Hormone. Chromosomal Location of Human Ortholog: 3q27. Cellular Component: extracellular space; cell surface; collagen; endoplasmic reticulum; extracellular region. Molecular Function: identical protein binding; protein binding; protein homodimerization activity; hormone activity; cytokine activity; sialic acid binding; receptor binding. Biological Process: circadian rhythm; negative regulation of MAP kinase activity; negative regulation of phagocytosis; negative regulation of smooth muscle cell proliferation; negative regulation of hormone secretion; membrane hyperpolarization; response to glucocorticoid stimulus; positive regulation of cellular protein metabolic process; negative regulation of smooth muscle cell migration; glucose homeostasis; negative regulation of granulocyte differentiation; positive regulation of interleukin-8 production; positive regulation of glucose import; negative regulation of gluconeogenesis; response to glucose stimulus; adiponectin-mediated signaling pathway; negative regulation of protein amino acid autophosphorylation; negative regulation of blood pressure; negative regulation of cell migration; protein homooligomerization; response to nutrient; generation of precursor metabolites and energy; positive regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of heterotypic cell-cell adhesion; positive regulation of signal transduction; glucose metabolic process; negative regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of tumor necrosis factor production; negative regulation of fat cell differentiation; negative regulation of synaptic transmission; response to sucrose stimulus; membrane depolarization; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of fatty acid metabolic process; response to ethanol; fatty acid beta-oxidation; cellular response to insulin stimulus; negative regulation of macrophage differentiation; negative regulation of low-density lipoprotein receptor biosynthetic process; negative regulation of inflammatory response; response to hypoxia; brown fat cell differentiation; fatty acid oxidation; response to activity; positive regulation of protein amino acid phosphorylation; negative regulation of transcription, DNA-dependent; positive regulation of myeloid cell apoptosis; positive regulation of blood pressure. Disease: Adiponectin, Serum Level Of, Quantitative Trait Locus 1

0.002 mg

140 USD

0.01 mg

205

1 mg

5365