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Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis.Resistin blocks insulinstimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of lowdensity lipoprotein (LDL), increasing the risk of heart disease.

Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.

Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-1 Subunit B has nontoxic action, it is the functional region which binds to the receptor. The Shiga Like Toxin-1 Subunit B can be useful in vaccine study, antibody test and other functional research.

CRYGD is a member of the beta/gamma-crystallin family. Crystallins are the principal structural components of the vertebrate eye lens. The mammalian lens crystallins are divided into alpha, beta, and gamma families. Gamma-crystallins are involved in cataract formation. Defects in the CRYGD gene are responsible for cataract autosomal dominant (ADC), cataract congenital non-nuclear polymorphic autosomal dominant (CCP), cataract congenital cerulean type 3 (CCA3) and cataract crystalline aculeiform (CACA).

S100A4 is part of the S100 super-family of proteins containing 2 EF-hand calcium binding domains. S100A4 is ubiquitously overexpressed and is localized in the cytoplasm and/or nucleus. S100A4 is involved in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.

S100b is a member of the S100 family of proteins which are a family of EF-hand calcium binding proteins that exist mostly as dimers of the 20 currently identified individual S100 monomers. The S100B homodimer is expressed in cells of the central nervous system, glial cells and in certain peripheral cells e.g. Schwann cells, melanocytes, adipocytes and chondrocytes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21; however, S100b is located at 21q22.3. The determination of S100B in serum levels may be used to monitor the extent of brain injury and malignant melanoma. S100b proteins may have a role in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of the S100b gene are implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.

DEAD Box Protein 56 (DDX56) belongs to the DEAD box protein family. DEAD box proteins, categorized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based upon their distribution patterns, certain members of this family are assumed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX56 exhibits ATPase activity in the presence of polynucleotides and associates with nucleoplasmic 65S preribosomal particles.

CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.

GNB3 belongs to the WD repeat G protein beta family. GNB3 is an important regulator of alpha subunit, as well as of certain signal transduction receptor and effector. A single-nucleotide polymorphism (C825T) in GNB3 is linked with essential hypertension and obesity. In addition, this polymorphism is also linked with the occurrence of the splice variant GNB3-s, which seems to have increased activity. GNB3-s is an example of alternative splicing caused by a nucleotide change outside of the splice donor and acceptor sites. Further splice variants may exist for GNB3, however they have not been fully described. Among the diseases associated with GNB3 are syncope, and aortic coarctation.

GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.

CKS1B protein which binds to the catalytic subunit of cyclin dependent kinases is vital for their biological function. The CKS1B mRNA is expressed in HeLa cells during the course of cell cycle in several forms which suggests that the encoded protein has a particular function. Two transcript variants were identified for this gene however it seems that only one of them encodes a protein.

Crystallins are the main structural proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into 3 fprotein families, α, β, & γ families. Because lens central fiber cells lose their nuclei during development, these crystallins are prepared and then retained throughout life, making them extremely stable proteins. CRYBB1 is a beta basic group member and undergoes extensive cleavage at its N-terminal extension during lens maturation.

Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.

Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.

Defensins (alpha & beta) are cationic peptides with a wide spectrum of antimicrobial activity which include a significant arm of the innate immune system. There are 6 human beta-defensins, BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6 which are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, beta-defensins can act as chemoattractants towards immature dendritic cells and memory T cells. Beta-defensins contain a 6-cysteine motif which forms 3 intra-molecular disulfide bonds.

CDC34 takes part in the control of cell cycle and DNA replication. Cdc34 in association with different E3 complexes, including SCF, targets many different substrates for ubiquitination and degradation during cell division, signal transduction, and development. Cdc34 substrates that have been characterized include B-Myb, Wee1, MyoD, ATF5, p27Xic1, and p27Kip1. Additionally, substrates such as p21Cip1, E2F, cyclin E, and cyclin D are putative substrates of Cdc34 by virtue of their SCF requirement for proteolysis. Cdc34 is self-associate through a domain in the C-terminus, and is phosphorylated and ubiquitinylated in vivo. CDC34is useful for in vitro ubiquitinylation reactions.

The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

XCL1 is a small cytokine belongs to the XC chemokine family that is also known as lymphotactin. XCL1 is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.

S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.

CD57 also called B3GAT1is part of the glucuronyltransferase gene family. CD57 exhibits strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. CD57 takes part in the glucuronyl transfer reaction during the biosynthesis of the carbohydrate epitope HNK-1.

DCXR catalyzes the NADPH-dependent reduction of numerous pentoses, tetroses, trioses, alpha-dicarbonyl molecules and L-xylulose. DCXR takes part in the uronate cycle of glucose metabolism. DCXR participates in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thus preventing osmolytic stress from occurring in the renal tubules.