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Manufactured by BioVendor

Visfatin Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant
  • Source:E. coli
  • Other names:NAMPT, Pre-B cell colony-enhancing factor, PBEF, Nicotinamide phosphoribosyltransferase, NAmPRTase, EC=2.4.2.12, Pre-B-cell colony-enhancing factor 1, PBEF1, NAMPT
  • Species:Human
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Cat. No. Size Price


New RD172098100-B 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant

Description

Total 347 AA. MW: 39.5 kDa (calculated). UniProtKB acc. no. P43490 (Pro27–Glu363). N-terminal His-tag (10 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence

MKHHHHHHASPPNTSKVYSYFECREKKTENSKLRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQE

Source

E. coli

Purity

Purity as determined by densitometric image analysis: > 90%

SDS-PAGE Gel

14 % SDS-PAGE separation of Human Visfatin:

  1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
  2. Reduced and boiled sample, 2.5 μg/lane
  3. Non-reduced and non-boiled sample, 2.5 μg/lane

Endotoxin

< 0.1 EU/µg

Formulation

Filtered (0.4 μm) and lyophilized in 0.03 M Acetate buffer pH=4.0; 5% Trehalose

Reconstitution

Add 0.1 M acetate buffer pH 4.0 to prepare a working stock solution of 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value is possible to dissolve in 20 mM Tris buffer, 50 mM NaCl, pH 7.5

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store lyophilized protein at –80°C. Lyophilized protein remains stable until the expiry date when stored at –80°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

Cytokines and chemokines and related molecules, Energy metabolism and body weight regulation

Summary

Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-α, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks , and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity. Visfatin exerts insulin-mimetic effects that are dose-dependent and quantitatively similar to those of insulin in stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its insulin-mimetic effects, visfatin was as effective as insulin in reducing hyperglycemia in insulin-deficient diabetic mice. Visfatin was also found to be bound to and activate insulin receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin and insulin did not compete for binding to the insulin receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes.

References to Summary

References to Visfatin

  • Arner P. Visfatin--a true or false trail to type 2 diabetes mellitus. J Clin Endocrinol Metab. 2006 Jan;91 (1):28-30
  • Beltowski J. Apelin and visfatin: unique "beneficial" adipokines upregulated in obesity?. Med Sci Monit. 2006 Jun;12 (6):RA112-9
  • Berndt J, Kloting N, Kralisch S, Kovacs P, Fasshauer M, Schon MR, Stumvoll M, Bluher M. Plasma visfatin concentrations and fat depot-specific mRNA expression in humans. Diabetes. 2005 Oct;54 (10):2911-6
  • Bottcher Y, Teupser D, Enigk B, Berndt J, Kloting N, Schon MR, Thiery J, Bluher M, Stumvoll M, Kovacs P. Genetic variation in the visfatin gene (PBEF1) and its relation to glucose metabolism and fat-depot-specific messenger ribonucleic acid expression in humans. J Clin Endocrinol Metab. 2006 Jul;91 (7):2725-31
  • Chen MP, Chung FM, Chang DM, Tsai JC, Huang HF, Shin SJ, Lee YJ. Elevated plasma level of visfatin/pre-B cell colony-enhancing factor in patients with type 2 diabetes mellitus. J Clin Endocrinol Metab. 2006 Jan;91 (1):295-9
  • Curat CA, Wegner V, Sengenes C, Miranville A, Tonus C, Busse R, Bouloumie A. Macrophages in human visceral adipose tissue: increased accumulation in obesity and a source of resistin and visfatin. Diabetologia. 2006 Apr;49 (4):744-7
  • Fukuhara A, Matsuda M, Nishizawa M, Segawa K, Tanaka M, Kishimoto K, Matsuki Y, Murakami M, Ichisaka T, Murakami H, Watanabe E, Takagi T, Akiyoshi M, Ohtsubo T, Kihara S, Yamashita S, Makishima M, Funahashi T, Yamanaka S, Hiramatsu R, Matsuzawa Y, Shimomura I. Visfatin: a protein secreted by visceral fat that mimics the effects of insulin. Science. 2005 Jan 21;307 (5708):426-30
  • Haider DG, Mittermayer F, Schaller G, Artwohl M, Baumgartner-Parzer SM, Prager G, Roden M, Wolzt M. Free fatty acids normalize a rosiglitazone-induced visfatin release. Am J Physiol Endocrinol Metab. 2006 Nov;291 (5):E885-90
  • Haider DG, Schindler K, Schaller G, Prager G, Wolzt M, Ludvik B. Increased plasma visfatin concentrations in morbidly obese subjects are reduced after gastric banding. J Clin Endocrinol Metab. 2006 Apr;91 (4):1578-81
  • Pagano C, Pilon C, Olivieri M, Mason P, Fabris R, Serra R, Milan G, Rossato M, Federspil G, Vettor R. Reduced plasma visfatin/pre-B cell colony-enhancing factor in obesity is not related to insulin resistance in humans. J Clin Endocrinol Metab. 2006 Aug;91 (8):3165-70
  • Pfutzner A, Forst T. Comment on: Haider DG, Schaller G, Kapiotis S, Maier C, Luger A, Wolzt M (2006) the release of the adipocytokine visfatin is regulated by glucose and insulin. Diabetologia 49:1909-1914. Diabetologia. 2006 Nov;49 (11):2795; author reply 2796
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