CTGF, HEK

Alternative Names: CTGF, CCN2, NOV2, HCS24, IGFBP8, MGC102839

Connective Tissue Growth Factor, a member of the CCN family of proteins, plays a crucial role in regulating various cellular functions such as proliferation, differentiation, and adhesion. The CCN family consists of six members in humans, including Cyr61, CTGF, Nov, WISP-1, WISP-2, and WISP-3, all of which encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane. CCN proteins are matricellular proteins involved in the development of various tissues and organs during embryonic development, including the kidney, nervous system, and bone. In adulthood, these proteins play a role in wound healing, bone fracture repair, and the pathogenesis of several diseases such as fibrosis and tumorigenesis. Full-length CCN proteins exhibit antiproliferative activity, while truncated isoforms are known to stimulate proliferation and act as oncogenes. The protein structure of CCN proteins consists of four modules: Module I displays partial identity with the N-terminal part of Insulin-like Growth Factor Binding Proteins; Module II includes a sequence similar to the Von Willebrand Factor Type C repeat; Module III contains sequences sharing identity with Thrombospondin type 1 repeat, important for cell adhesion; and Module IV, designated CT, plays a crucial role in various biological functions of CCN proteins. Proteolysis of full-length CCN proteins results in the production of CCN-derived peptides with high

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  • Sku: PSB-cyt-687-2µg
  • Vendor: ProSpec-Tany
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Product Details

Product Description

Recombinant Human Connective Tissue Growth Factor, HEK is a protein belonging to the family of growth factors. It plays a role in promoting cell proliferation, migration, and differentiation in connective tissues. With a molecular weight of approximately 36 kDa, this protein is commonly used in research and therapeutic applications for studying cell growth and tissue regeneration processes.

Current Lead Time

7-14 Days

Product Specifications

Species
 Human
Expression System HEK 293
Purity 90% by SDS-PAGE
Activity
 Not Available
Activity Assay
Animal Component Free (ACF) No
Molecular Weight
 36.67 kDa
Structure Dimer
Endotoxin Concentration
 Not Available
Purification Method Not Available
Form
 Frozen
Formulation CTGF filtered (0.2µm) solution in 0.1M Citrate buffer pH 4.7and 20% (w/v) glycerol.

*For Research Use Only

Product Guarantee

If your product is within its expiration period, and has not performed according to expectations, fill out the sample return form. Return the unused sample frozen, with the auto generated packing slip to the address on the instructions. You will receive a full refund along with a replacement of the unused portion (inclusive of the failed test). Damages do not cover any additional costs incurred for failed experimentation. 

Amino Acid Sequence

QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

Storage Instruction

Reconstituted store at -20°C or -80°C.We recommend that single use aliquots are prepared to avoid freeze-thaw cycles.

Sample Prep Instruction

1. Thaw the vial on ice, spin briefly
2. Prepare single-use or stock aliquots. This stage will depend on your final application so please adapt as appropriate. All our proteins are supplied carrier protein-free. If compatible with your work and you are storing at lower concentrations (<50 ug/ml) adding carrier protein is highly advised (usually 1% w/v high purity BSA or equivalent – ensure all buffers are sterile-filtered).
3. Prepare single-use aliquots whenever possible to avoid freeze-thaw cycles which can damage the proteins and reduce bioactivity. Store aliquots at -70 °C (or -20 °C)
4. We recommend sterile filtering after dilution in media or the final working solution
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References

Not Available
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