ERCC

ERCC

ERCC

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    Description:

    Excision Repair Cross-Complementing 1 Human Recombinant

    Excision Repair Cross-complementing rodent repair deficiency complementation group 1 (includes overlapping antisense sequence), RAD10, COFS4, UV20, DNA excision repair protein ERCC-1.

    Product # :

    PRO-1106

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    • description
    • source
    • formulation
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    • More Info

    Description

    ERCC1 Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (1-273) and having a molecular mass of 32.5kDa.ERCC1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ERCC1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ERCC1 polypeptide is essential for nucleotide excision repair (NER) of damaged DNA and is homologous to Saccharomyces cerevisiae RAD10, which takes part in repair and mitotic intra-chromosomal recombination. NER mechanism includes dual incisions on both sides of the damage catalyzed by two nucleases. In mammalian cells XPG cleaves 3' of the DNA lesion while the ERCC1-XPF complex makes the 5' incision.

    • Synonyms

      Excision Repair Cross-complementing rodent repair deficiency complementation group 1 (includes overlapping antisense sequence), RAD10, COFS4, UV20, DNA excision repair protein ERCC-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMDPGKD KEGVPQPSGP PARKKFVIPL DEDEVPPGVA KPLFRSTQSL PTVDTSAQAA PQTYAEYAIS QPLEGAGATC PTGSEPLAGE TPNQALKPGA KSNSIIVSPR QRGNPVLKFV RNVPWEFGDV IPDYVLGQST CALFLSLRYH NLHPDYIHGR LQSLGKNFAL RVLLVQVDVK DPQQALKELA KMCILADCTL ILAWSPEEAG RYLETYKAYE QKPADLLMEK LEQDFVSRSL EQLIAASRED LALCPGLGPQ KARRLFDVLH EPFLKVP

    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.

    Ercc1 Human

About ERCC:

ERCC is also known as DNA excision repair protein ERCC-1 and is found in humans. The ERCC4, with this protein, forms the ERCC1-XPF enzyme complex, which is responsible for DNA repair and recombination. ERCC1-XPF nuclease is an indispensable activity in the pathway of nucleotide excision repair (NER) of DNA. It also functions in pathways to restore "crosslink" damage and repair double-strand breaks in DNA.

ERCC Function
A constituent of a structure-specific DNA mend endonuclease that is non-catalytic is accountable for the 5' slit during DNA restoration. With the SLX4, the ERCC1-XPF enzyme complex is the trigger for repairing interstrand crosslinks (ICL). It also acts in the anaphase, bridge-generating DNA arrangements consisting of partly processed DNA lesions during the S or G2 phases. This may cause cytokinesis failure. ERCC is also needed for homology-directed repair (HDR) of double-strand DNA breaks with SLX4.

ERCC Structure
The ERCC1–XPF complex is an example of a structure-specific endonuclease. Rather than cutting DNA that is solely single-stranded or double-stranded, ERCC1-XPF cleaves the DNA phosphodiester backbone precisely at the junctions between double-stranded and single-stranded DNA. It does this by introducing a cut in double-stranded DNA. This cut is on the 5′ side of such a junction by a distance of approximately two nucleotides.

ERCC Interaction
The interactions of XPF and the hydrophobic helix–hairpin–helix patterns in the C-terminal areas of ERCC1 stimulate the bonding of the two proteins. Without bonding, there can be no catalytic action. ERCC1 is invaluable to the complex's action, although on its own, ERCC1 is catalytically inactive, and the catalytic domain is found solely in XPF.