Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Biotium

Recognizes a single chain glycoprotein of 70 kDa, identified as CD55 (also known as decay accelerating factor, DAF). This MAb was clustered in Kobe at the Sixth International Workshop on Human Leukocyte Differentiation Antigens as F429D-9 (N-L120). CD55/DAF is widely expressed on cells throughout the body including leukocytes, erythrocytes, epithelium, endothelium, and fibroblasts. It is a Glycosyl phosphatidylinositol anchored (GPI-anchored) member of the membrane bound complement regulatory proteins that inhibit autologous complement cascade activation. It prevents the amplification steps of the complement cascade by interfering with the assembly of the C3-convertases, C4b2a and C3bBb, and the C5-convertase, C4b2a3b and C3bBb3b. CD55 also serves as receptor for CD97 and for echovirus and Coxsackie B virus. Anti-CD55 can be used as marker for paroxysmal nocturnal hemoglobinuria (PNH).

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Biotium

Recognizes a single chain glycoprotein of 70 kDa, identified as CD55 (also known as decay accelerating factor, DAF). This MAb was clustered in Kobe at the Sixth International Workshop on Human Leukocyte Differentiation Antigens as F429D-9 (N-L120). CD55/DAF is widely expressed on cells throughout the body including leukocytes, erythrocytes, epithelium, endothelium, and fibroblasts. It is a Glycosyl phosphatidylinositol anchored (GPI-anchored) member of the membrane bound complement regulatory proteins that inhibit autologous complement cascade activation. It prevents the amplification steps of the complement cascade by interfering with the assembly of the C3-convertases, C4b2a and C3bBb, and the C5-convertase, C4b2a3b and C3bBb3b. CD55 also serves as receptor for CD97 and for echovirus and Coxsackie B virus. Anti-CD55 can be used as marker for paroxysmal nocturnal hemoglobinuria (PNH).

Supplier: Biotium

Recognizes a single chain glycoprotein of 70 kDa, identified as CD55 (also known as decay accelerating factor, DAF). This MAb was clustered in Kobe at the Sixth International Workshop on Human Leukocyte Differentiation Antigens as F429D-9 (N-L120). CD55/DAF is widely expressed on cells throughout the body including leukocytes, erythrocytes, epithelium, endothelium, and fibroblasts. It is a Glycosyl phosphatidylinositol anchored (GPI-anchored) member of the membrane bound complement regulatory proteins that inhibit autologous complement cascade activation. It prevents the amplification steps of the complement cascade by interfering with the assembly of the C3-convertases, C4b2a and C3bBb, and the C5-convertase, C4b2a3b and C3bBb3b. CD55 also serves as receptor for CD97 and for echovirus and Coxsackie B virus. Anti-CD55 can be used as marker for paroxysmal nocturnal hemoglobinuria (PNH).

Supplier: Biotium

Recognizes a single chain glycoprotein of 70 kDa, identified as CD55 (also known as decay accelerating factor, DAF). This MAb was clustered in Kobe at the Sixth International Workshop on Human Leukocyte Differentiation Antigens as F429D-9 (N-L120). CD55/DAF is widely expressed on cells throughout the body including leukocytes, erythrocytes, epithelium, endothelium, and fibroblasts. It is a Glycosyl phosphatidylinositol anchored (GPI-anchored) member of the membrane bound complement regulatory proteins that inhibit autologous complement cascade activation. It prevents the amplification steps of the complement cascade by interfering with the assembly of the C3-convertases, C4b2a and C3bBb, and the C5-convertase, C4b2a3b and C3bBb3b. CD55 also serves as receptor for CD97 and for echovirus and Coxsackie B virus. Anti-CD55 can be used as marker for paroxysmal nocturnal hemoglobinuria (PNH).

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Biotium

Recognizes a single chain glycoprotein of 70 kDa, identified as CD55 (also known as decay accelerating factor, DAF). This MAb was clustered in Kobe at the Sixth International Workshop on Human Leukocyte Differentiation Antigens as F429D-9 (N-L120). CD55/DAF is widely expressed on cells throughout the body including leukocytes, erythrocytes, epithelium, endothelium, and fibroblasts. It is a Glycosyl phosphatidylinositol anchored (GPI-anchored) member of the membrane bound complement regulatory proteins that inhibit autologous complement cascade activation. It prevents the amplification steps of the complement cascade by interfering with the assembly of the C3-convertases, C4b2a and C3bBb, and the C5-convertase, C4b2a3b and C3bBb3b. CD55 also serves as receptor for CD97 and for echovirus and Coxsackie B virus. Anti-CD55 can be used as marker for paroxysmal nocturnal hemoglobinuria (PNH).

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Bioss

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

Supplier: Corning

Corning® Stripwell™ microplates may be used in a variety of laboratory assays. The flat bottom strips are designed to easily break apart and are pre-assembled in an ‘egg-crate’ style strip holder that allows everyone well to be positioned back into the microplate once broken.

Supplier: 3M

The 3M™ S-series headcovers offer head and face protection, as well as providing eye and face protection from liquid splash and low energy impact (grade F). They are suitable for applications that require frequent replacement of the entire headgear assembly, such as pharmaceutical manufacturing and laboratory work, or in situations where there is less soiling of the outer fabric. All headcovers can be used in conjunction with 3M Powered and Supplied Air systems (e.g. Jupiter™ and Dustmaster™), thus offering respiratory protection.

Supplier: Merck

ZHE (Zero Head Space Extractor) hazardous waste filtration system, which is approved by the US Environmental Protection Agency (EPA) as an apparatus for Toxicity Characteristic Leaching Procedure (TCLP) measurement. The system cannot pressurise unless completely assembled; this eliminates accidentally 'shooting the piston' out of the unit and assures safe operation. Choose both manual and automatic venting modes.

Supplier: Corning

Corning® Stripwell™ microplates may be used in a variety of laboratory assays. The flat bottom strips are designed to easily break apart and are pre-assembled in an 'egg-crate' style strip holder that allows each individual well to be positioned back into the microplate once broken.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Supplier: Bioss

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.