Thermo Fisher Scientific Human NOV Recombinant Protein, PeproTech

Applications

Tested Dilution

Publications

Western Blot (WB)

Assay-dependent

-

ELISA (ELISA)

Assay-dependent

-

Functional Assay (Functional)

Assay-dependent

-

In vitro Assay (IV)

-

View 2 publications 2 publications

Miscellaneous PubMed (Misc)

-

View 2 publications 2 publications

Product Specifications

Species

Human

Published species

Chicken, Human, Mouse

Expression System

E. coli

Amino acid sequence

MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M

Molecular weight

36.2 kDa

Class

Recombinant

Type

Protein

Purity

≥ 95% by SDS-PAGE gel and HPLC analyses.

Endotoxin concentration

<1 EU/µg

Activity

Determined by a cell proliferation assay using BALB/c 3T3 cells. The expected ED50 for this effect is 1.0-2.0 ug/ml

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

purified

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Ambient

Product Specific Information

Recombinant Human NOV is a 36.2 kDa protein containing 331 amino acid residues. It is composed of four distinct structural domains (modules): the IGF binding protein (IGFBP) domain; the von Willebrand Factor C (VWFC) domain; the Thrombospondin type-I (TSP type-1) domain; and a C-terminal cysteine knot-like domain (CTCK).

This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Target Information

NOV is a member of the CCN family of secreted, cysteine-rich regulatory proteins. The full-length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm`s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorigenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell-surface integrins, and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.