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CTGF N-terminus Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Hypertrophic chondrocyte-specific protein 24, Insulin-like growth factor-binding protein 8, IGF-binding protein 8, IGFBP-8, IBP-8, CCN family member 2, CTGF, CCN2, HCS24
  • Species:Human
Cat. No. Size Price
1 - 4 pcs / 5 - 9 pcs / 10+ pcs


New RD172592100 0.1 mg $405 / $355 / On request
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 154 AA. MW 16.7 kDa (calculated). UniProtKB acc. No. P29279 (Gln27-Thr173). N-terminal His-tag (7 extra AA). Protein identity confirmed by MS.

Amino Acid Sequence

MHHHHHHQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSCKYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQT

Source

E. coli

Purity

˃ 90 % by SDS-PAGE

SDS-PAGE Gel

14 % SDS-PAGE separation of Human CTGF N-terminus:

  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

< 1.0 EU/µg

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/ml solution in 20 mM Tris buffer, 50 mM NaCl, 5% w/v trehalose, pH 8.

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.25 mg/ml and let the lyophilized pellet dissolve completely.

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. Endotoxin level determination.

Note

This product is intended for research use only.

Summary

Research topic

Apoptosis, Bone and cartilage metabolism, Cardiovascular disease, Coronary artery disease, Extracellular matrix, Oncology, Others, Pulmonary diseases, Renal disease

Summary

Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane. CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumourigenesis. Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full-length protein consists of four modules: - Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs). - Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC). - Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. - Module IV, also designated CT, is encoded by exon 5. It is the least conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's fac­tor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain. Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumours. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.In agreement with CCN2 playing a role in brain tumour angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumour cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high-grade tumours, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells. CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

Summary References (17)

References to Connective Tissue Growth Factor

  • Abdel-Wahab N, Weston BS, Roberts T, Mason RM. Connective tissue growth factor and regulation of the mesangial cell cycle: role in cellular hypertrophy. J Am Soc Nephrol. 2002 Oct;13 (10):2437-45
  • Chen MM, Lam A, Abraham JA, Schreiner GF, Joly AH. CTGF expression is induced by TGF- beta in cardiac fibroblasts and cardiac myocytes: a potential role in heart fibrosis. J Mol Cell Cardiol. 2000 Oct;32 (10):1805-19
  • Gerritsen KG, Leeuwis JW, Koeners MP, Bakker SJ, van Oeveren W, Aten J, Tarnow L, Rossing P, Wetzels JF, Joles JA, Kok RJ, Goldschmeding R, Nguyen TQ. Elevated Urinary Connective Tissue Growth Factor in Diabetic Nephropathy Is Caused by Local Production and Tubular Dysfunction. J Diabetes Res. 2015;2015:539787
  • Gravning J, Orn S, Kaasboll OJ, Martinov VN, Manhenke C, Dickstein K, Edvardsen T, Attramadal H, Ahmed MS. Myocardial connective tissue growth factor (CCN2/CTGF) attenuates left ventricular remodeling after myocardial infarction. PLoS One. 2012;7 (12):e52120
  • Gressner AM, Yagmur E, Lahme B, Gressner O, Stanzel S. Connective tissue growth factor in serum as a new candidate test for assessment of hepatic fibrosis. Clin Chem. 2006 Sep;52 (9):1815-7
  • Gressner OA, Fang M, Li H, Lu LG, Gressner AM, Gao CF. Connective tissue growth factor (CTGF/CCN2) in serum is an indicator of fibrogenic progression and malignant transformation in patients with chronic hepatitis B infection. Clin Chim Acta. 2013 Jun 05;421:126-31
  • Gressner OA, Gressner AM. Connective tissue growth factor: a fibrogenic master switch in fibrotic liver diseases. Liver Int. 2008 Sep;28 (8):1065-79
  • Gygi D, Zumstein P, Grossenbacher D, Altwegg L, Luscher TF, Gehring H. Human connective tissue growth factor expressed in Escherichia coli is a non-mitogenic inhibitor of apoptosis. Biochem Biophys Res Commun. 2003 Nov 21;311 (3):685-90
  • Honsawek S, Yuktanandana P, Tanavalee A, Chirathaworn C, Anomasiri W, Udomsinprasert W, Saetan N, Suantawee T, Tantavisut S. Plasma and synovial fluid connective tissue growth factor levels are correlated with disease severity in patients with knee osteoarthritis. Biomarkers. 2012 Jun;17 (4):303-8
  • Kato M, Fujisawa T, Hashimoto D, Kono M, Enomoto N, Nakamura Y, Inui N, Hamada E, Miyazaki O, Kurashita S, Maekawa M, Suda T. Plasma connective tissue growth factor levels as potential biomarkers of airway obstruction in patients with asthma. Ann Allergy Asthma Immunol. 2014 Sep;113 (3):295-300
  • Koitabashi N, Arai M, Niwano K, Watanabe A, Endoh M, Suguta M, Yokoyama T, Tada H, Toyama T, Adachi H, Naito S, Oshima S, Nishida T, Kubota S, Takigawa M, Kurabayashi M. Plasma connective tissue growth factor is a novel potential biomarker of cardiac dysfunction in patients with chronic heart failure. Eur J Heart Fail. 2008 Apr;10 (4):373-9
  • Kovalenko E, Tacke F, Gressner OA, Zimmermann HW, Lahme B, Janetzko A, Wiederholt T, Berg T, Muller T, Trautwein C, Gressner AM, Weiskirchen R. Validation of connective tissue growth factor (CTGF/CCN2) and its gene polymorphisms as noninvasive biomarkers for the assessment of liver fibrosis. J Viral Hepat. 2009 Sep;16 (9):612-20
  • Lam S, van der Geest RN, Verhagen NA, van Nieuwenhoven FA, Blom IE, Aten J, Goldschmeding R, Daha MR, van Kooten C. Connective tissue growth factor and igf-I are produced by human renal fibroblasts and cooperate in the induction of collagen production by high glucose. Diabetes. 2003 Dec;52 (12):2975-83
  • Leask A, Abraham DJ. The role of connective tissue growth factor, a multifunctional matricellular protein, in fibroblast biology. Biochem Cell Biol. 2003 Dec;81 (6):355-63
  • Lombet A, Planque N, Bleau AM, Li CL, Perbal B. CCN3 and calcium signaling. Cell Commun Signal. 2003 Aug 15;1 (1):1
  • Rachfal AW, Brigstock DR. Connective tissue growth factor (CTGF/CCN2) in hepatic fibrosis. Hepatol Res. 2003 May;26 (1):1-9
  • Riser BL, Cortes P, DeNichilo M, Deshmukh PV, Chahal PS, Mohammed AK, Yee J, Kahkonen D. Urinary CCN2 (CTGF) as a possible
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