ELISA Kits

Laminin is a large basement membrane glycoprotein composed of three subunits designated the A, B1, and B2. Laminin has diverse biological functions, which include stimulating epithelial cell growth and differentiation. The nucleotide sequence of human laminin A chain has an open reading frame encoding 3075-amino acids. The human laminin A chain is at locus 18p11.3. The nucleotide sequence of the human laminin B1 reveals a 5358-base pair open reading frame that potentially codes for 1786 amino acids, including 20 amino acids of a presumptive signal peptide. The gene for the human laminin-B1 chain has been localized to chromosome 7, band q31. The B2 chain consists of six distinct domains, including two domains with alpha-helical, coiled-coil structures, two domains with cysteine-rich homologous repeats, and two globular domains. The amino acid sequences of the B2 and B1 chains demonstrate considerable homology.

Leptin(or obese, OB) is a circulating hormone that is expressed abundantly and specifically in the adipose tissue. Human ob protein is a 166-amino acid polypeptide with a putative signal sequence and is 84 and 83% homologous to the mouse and rat ob proteins, respectively. Northern blot analysis reveals that OB RNA is present at a high level in adipose tissue but at much lower levels in placenta and heart. Indeed, Leptin is first described as an adipocyte-derived signalling factor, which, after interaction with its receptors, induces a complex response including control of bodyweight and energy expenditure. Leptin seems in addition to its role in metabolic control to have important roles in reproduction and neuroendocrine signalling. Leptin is a powerful inhibitor of bone formation in vivo. Comparative mapping of mouse and human DNA indicates that the ob gene is located within a region of mouse chromosome 6 that is homologous to a portion of human chromosome 7q. The standard product use

Leptin receptor(or Obese receptor, OBR) is a single membrane-spanning receptor most related to the gp130 signal-transducing component of the IL-6 receptor, the G-CSF receptor, and the LIF receptor. OB-R mRNA is expressed not only in choroid plexus, but also in several other tissues, including hypothalamus. Leptin acts through the leptin receptor, a single-transmembrane domain receptor of the cytokine-receptor family. Leptin controls energy balance and food intake through the leptin receptor in the hypothalamus of the brain, which suggests that some polymorphisms of the leptin receptor gene(LEPR) might contribute to obesity or obesity-related diseases. Leptin is also involved in the regulation of blood pressure through the leptin receptor.

Monocyte chemoattractant protein-1(MCP-1), a member of the chemokine(chemotactic cytokine) family, is a potent monocyte agonist that is upregulated by oxidized lipids. MCP-1 is also known as CCL2, SCYA2, MCAF. MCAF is a member of family of factors involved in immune and inflammatory responses. The amino acid sequence deduced from the nucleotide sequence reveals the primary structure of the MCAF precursor to be composed of a putative signal peptide sequence of 23 amino acid residues and a mature MCAF sequence of 76 amino acid residues. MCP-1 plays a unique and crucial role in the initiation of atherosclerosis and may provide a new therapeutic target in this disorder. Human MCP-1 is a 8.7KDa non-glycoprotein, consisting of 99 amino acids in precursor form and 76 amino acids in mature form.

Chemokine(C-C motif) ligand 8, also known as monocyte chemoattractant protein 2(MCP-2), is a protein that in humans is encoded by the CCL8 gene. CCL8 is a small cytokine belonging to the CC chemokine family. The CCL8 protein is produced as a precursor containing 109 amino acids, which is cleaved to produce mature CCL8 containing 75 amino acids. The gene for CCL8 is encoded by 3 exons and is located within a large cluster of CC chemokines on chromosome 17q11.2 in humans. Monocyte chemotactic protein 2(MCP-2) is a CC chemokine that utilizes multiple cellular receptors to attract and activate human leukocytes.

Chemokine(C-C motif) ligand 7(CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3(MCP3). It belongs to the C-C chemokine family. By fluorescence in situ hybridization, mapped the MCP3 gene to chromosome 17q11.2-q12. MCP3 was identified as a physiologic substrate of gelatinase A. Cleaved MCP3 binds to CC-chemokine receptors-1, -2, and -3, but no longer induces calcium fluxes or promotes chemotaxis, and instead acts as a general chemokine antagonist that dampens inflammation, suggested that matrix metalloproteinases are both effectors and regulators of the inflammatory response.

M-CSF, also called CSF1, has a role in development of the placenta. Uterine CSF1 concentration is regulated by a synergistic action of estradiol and progesterone. CSF1 is produced by uterine glandular epithelial cells. It had been found that FMS, the CSF1 receptor, is expressed in placenta and choriocarcinoma cell lines1. The CSF1 gene is mapped to 1p21-p13 and contains 10 exons and 9 introns spanning 20 kb2. And there are 2 forms of CSF1, with 224 and 522 amino acids, resulting from alternative splicing3.

M-CSF, also called CSF1, consists of a 14-amino acid peptide, longer than the usual 8-to-11 mer recognized by most CTLs. The M-CSF gene is mapped to 1p21-p13 and contains 10 exons and 9 introns spanning 20 kb1. Although it is a single-copy gene, its expression results in the synthesis of several mRNAs, ranging in size from about 1.5 to 4.5 kb2. There are 2 forms of M-CSF, with 224 and 522 amino acids, resulting from alternative splicing3. Furthermore, M-CSF has a role in development of the placenta. Uterine M-CSF concentration is regulated by a synergistic action of estradiol and progesterone. M-CSF is produced by uterine glandular epithelial cells. It had been found that FMS, the M-CSF receptor, is expressed in placenta and choriocarcinoma cell lines4.

Macrophage-derived chemokine(MDC), also called Chemokine, cc motif, ligand 22(CCL22) or Small inducible cytokine subfamily A, member 22(SCY22). MDC is a recently identified member of the CC chemokine family. It is not closely related to other chemokines, sharing most similarity with thymus- and activation-regulated chemokine(TARC), which contains 37% identical amino acids. In addition, MDC gene is mapped to chromosome 16q13, the same position reported for the TARC gene. MDC has the four-cysteine motif and other highly conserved residues characteristic of CC chemokines, but it shares<35% identity with any of the known chemokines. Recombinant MDC was expressed in Chinese hamster ovary cells and purified by heparin-Sepharose chromatography. MDC is highly expressed in macrophages and in monocyte-derived dendritic cells, but not in monocytes, natural killer cells, or several cell lines of epithelial, endothelial, or fibroblast origin. High expression was also detected in normal thymus and l