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CYT-438

重組人結(jié)締組織生長因子（rHuCTGF）

2μg/10μg/1mg

Prospec

Background:
	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 exon5. It is the leasts conserved oneof 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.
	Description :
	The Human CTGF His-Tagged Fusion Protein, produced in E. coli, is 38.3 kDa protein containing 323 amino acid residues of the human CTGF and 23 additional amino acid residues - HisTag, Xa - cleavage site （bold）.
	Amino Acid Sequence:
	MGHHHHHHHH HHSSGHIEGR HMRQNCSGPC RCPDEPAPRC PAGVSLVLDG CGCCRVCAKQ LGELCTERDPCDPHKGLFCD FGSPANRKIG VCTAKDGAPC IFGGTVYRSG ESFQSSCKYQ CTCLDGAVGC MPLCSMDVRLPSPDCPFPRR VKLPGKCCEE WVCDEPKDQT VVGPALAAYR LEDTFGPDPT MIRANCLVQT TEWSACSKTCGMGISTRVTN DNASCRLEKQ SRLCMVRPCE ADLEENIKKG KKCIRTPKIS KPIKFELSGC TSMKTYRAKF CGVCTDGRCCTPHRTTTLPV EFKCPDGEVM KKNMMFIKTC ACHYNCPGDN DIFESLYYRK MYGDMA.
	Physical Appearance:
	Sterile Filtered White lyophilized （freeze-dried） powder.
	Protein Content:
	0.1 mg （determined by BCA method）.
	Formulation:
	Sterile filtered and lyophilized from 0.5 mg/ml in 0.05 M Acetate buffer pH4.
	Specificity:
	The amino acid sequence of the recombinant human CTGF is 100% homologous to amino acid sequence of the human CTGF without signal sequence.
	Purification Method:
	Three-step procedure using affinity Ni-NTA chromatography and size exclusion chromatography before and after refolding.
	Solubility:
	Add 0.2 ml of 0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve compley. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
	Stability:
	Store lyophilized protein at -20°C. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized protein remains stable until the expiry date when stored at -20°C. Please prevent freeze-thaw cycles.
	Purity:
	Purity of recombinant human CTGF is >95% （SDS-PAGE analyzed）.
	Usage:
	Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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