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IDO-Blockers, Bile Acids, Hepcidin 25, Celiac Disease, EGF, Beta-Defensin, Lactoferrin, L-kynurenine, ADMA, Glutathione and Vitamins, Myostatin.
   

L-kynurenine is the main product of the degradation of L-tryptophan catalysed by indolamine-2,3-dioxigenase (IDO), and it is an up-coming and highly relevant marker in diff erent major diseases.

IDO - Blockers:

  • IMM-K7727 IDK IDO (Indolamin-2,3-Dioxygenase)
  • IMM-K7728 IDK L-Kynurenine
  • IMM-K3728 IDK L-Kynurenine High Sensitive (mouse/rat)
  • IMM-K7730 IDK Tryptophan
  • IMM-K3730 IDK Tryptophan High Sensitive (mouse/rat)

 

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CHOLOGENIC DIARRHEA / BILE ACIDS            

IDK® Bile Acids: An innovative assay for the in-vitro determination of bile acids in stool

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HEPCIDIN 25                                                                                                         

Immundiagnostik AG receives award at Falk Symposium in Frankfurt

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CELIAC DISEASE

Monitoring of gluten-free diet

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GENETIC CELIAC ANALYSIS

PCR tests for the determination of the specific HLA-DQ2/8 allele for predisposition

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NEFROLOGY - BLADDER CANCER

Bladder cancer, EGF receptor discovered as a possibile predictive biomarker for survival

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DERMATOLOGY - PSORIASIS

Psoriasis: beta-defensin, a serum marker for disease activity in psoriasis

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CARDIOVASCULAR:

- L-KYNURENINE

Coronary heart disease: L-kynurenine as a novel inflammation marker

 

- ADMA

ADMA concentration in blood correlates significantly with the degree of arteriosclerosis in dialysis patients

 

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INFECTIOUS DISEASES - MENINGITIS 

Differential diagnosis between bacterial and aseptic meningitis: Lactoferrin as a biomarker

 

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ENDOCRINOLOGY - GLUTATHIONE - DIABETES

Glutathione, a prognostic marker for diabetes mellitus type 2

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LABORATORY TIPS  

Stability of vitamins in blood samples

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Myostatin ELISA Kit

Worldwide exclusive test ELISA per la determinazione della Miostatina in siero e plasma.

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Secreted growth factor
Inhibitor of muscle growth

 

  • Myostatin levels increased in diseases associated with muscle waste
  • Diet and physical activity can change Myostatin levels
Article number: IMM-K1012
Tests: 96 Tests
Incubation time: 2h; 1h; 10-20 min
Volume: 20 µl
Matrix: Serum, Plasma
Standards: 0.4 - 32.5 ng/ml
Method: ELISA
Synonyms: Myostatin, GDF8, GDF-8, MSTN, Growth Differentiation Factor 8
GAMMA COMPLETA DEI PRODOTTI Clicca qui  
   

INTENDED USE

This enzyme immunoassay is intended for the quantitative determination of myostatin in human serum and plasma. For in vitro diagnostic use only.

SUMMARY

Myostatin belongs to the transforming growth differentiation factor-ß (TGF-ß) super family. The molecule is a negative regulator of muscle growth, but details about the actions of myostatin are uncertain (Roth and Walsh, 2004).

Myostatin was first identified in 1997 by McPherron et al. They found out that null-mutant knockout mice were significantly larger than wild-type animals and exhibited a large and widespread increase in skeletal muscle mass due to an increase of muscle fiber number (hyperplasia) and thickness (hypertrophy). Other groups identified mutations in the myostatin gene in naturally bred “double-muscles” cattle breeds.

Similar to the findings in animal models, increased myostatin immuno-reactivity or expression has been observed in HIV-infected men with muscle wasting (Gonzales-Cadavid et al. 1998), after prolonged bed rest in young men (Zachwieja et al. 1999) and in older men and women with muscle wasting (Yarasheski KE et al. 2002).   
Shi et al. (2007) and others have found that myostatin deficiency inhibits adipogenesis in vivo, even when mice are fed a high-fat diet. Transgenic overexpression of myostatin pro-peptide, which inhibits myostatin signaling, also inhibits body fat gain with a high-fat diet (Zhao et al. 2005). Similar alterations in myostatin signaling are associated with changes in body fat among humans.

NEW APPLICATION

Biochem J. 2012 May 23. [Epub ahead of print]

Myostatin is a novel tumoral factor that induces cancer cachexia.

Lokireddy S, Wijesoma IW, Bonala S, Wei M, Sze SK, McFarlane C, Kambadur R, Sharma M.

Abstract

Humoral and tumoral factors collectively promote cancer-induced skeletal muscle wasting by increasing protein degradation. While several humoral proteins, namely TNF-α and IL-6, have been shown to induce skeletal muscle wasting, there is dearth of information regarding the tumoral factors that contribute to the atrophy of muscle during cancer cachexia. Therefore, we have characterized the secretome of C26 colon cancer cells to identify the tumoral factors involved in cancer-induced skeletal muscle wasting. In this report, we show that Myostatin, a procachectic TGF-β superfamily member, is abundantly secreted by C26 cells. Consistent with Myostatin signaling during cachexia, treating differentiated C2C12 myotubes with C26 conditioned medium (CM) resulted in myotubular atrophy due to the up-regulation of muscle-specific E3 ligases, Atrogin-1 and MuRF1, and enhanced activity of the ubiquitin-proteasome pathway. Furthermore, the C26 CM also activated ActRIIB/Smad and NF-κB signaling, and reduced activity of the IGF-1/PI3K/Akt pathway, three salient molecular features of Myostatin action in skeletal muscles. Antagonists to Myostatin prevented C26 CM-induced wasting in muscle cell cultures, further confirming that tumoral Myostatin may be a key contributor in the pathogenesis of cancer cachexia. Finally, we show that treatment with C26 CM induced the autophagy-lysosome pathway and reduced mitochondria number in myotubes. These two previously unreported observations were recapitulated in skeletal muscles collected from C26 tumor-bearing mice.

INDICATIONS

Regulation of muscle growth

Muscle atrophy

Muscle wasting

 
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IMM-K1012 Myostatin ELISA Protocol

 

Myostatin Flyer

 

Richiedi Offerta 

PUBLICATIONS:

Myostatin and obesity/insulin resistance

      Ehehalt et al. (2011). "Investigation of Myostatin Serum Levels Before and After a 6-Month Lifestyle Intervention Program in Obese Children." Exp Clin Endocrinol Diabetes 119(4): 238-42.

Hittel et al. (2010). "Myostatin decreases with aerobic exercise and associates with insulin resistance." Med Sci Sports Exerc 42(11): 2023-9.

Myostatin and heart failure

Wintgens, K.F., et al. (2012) , Plasma myostatin measured by a competitive ELISA using a highly specifi c antiserum. Clin Chim Acta, 413(15-16): p. 1288-94

Breitbart, A., et al. (2011), "Myostatin from the heart: local and systemic actions in cardiac failure and muscle wasting". Am J Physiol Heart Circ Physiol, 300(6): p. H1973-82.

      Wintgens et al. (2012). "Plasma myostatin measured by a competitive ELISA using a highly specific antiserum." Clin Chim Acta 413(15-16): 1288-94.

        Gruson et al. (2011). "Increased plasma myostatin in heart failure." European Journal of Heart Failure 13 (7): 734-736.

      Zamora et al. (2010). "Serum myostatin levels in chronic heart failure." Rev Esp Cardiol 63(8): 992-6.

        Myostatin and kidney failure

      Cheung et al. (2008). "Modulation of melanocortin signaling ameliorates uremic cachexia." Kidney International 74(2): 180-186.

        Myostatin and cancer

      Lokireddy et al. (2012). "Myostatin is a novel tumoral factor that induces cancer cachexia." Biochem J. May 23 [Epub ahead of print].

 
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