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Lithium+chloride


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Supplier:  Rockland Immunochemical
Description:   Secondary Donkey Anti-IgG (H&L) Reacts with Goat

Supplier:  Rockland Immunochemical
Description:   Secondary Goat Anti-IgG (H&L) Reacts with Hamster
Supplier:  Rockland Immunochemical
Description:   Secondary Goat Anti-IgG (H&L) Reacts with Hamster
Supplier:  Invitrogen
Description:   Imject<sup>® </sup>Maleimide-activated mcKLH and PEGylated mcKLH enable conjugation of sulfhydryl-containing peptide haptens to elicit an immune response and antibody production against the hapten
Catalog Number: (RL616-1102)

Supplier:  Rockland Immunochemical
Description:   Secondary Goat Anti-IgG (H&L) Reacts with Donkey
Catalog Number: (RL610-9102)

Supplier:  Rockland Immunochemical
Description:   Secondary Chicken Anti-IgG (H&L) Reacts with Mouse
Supplier:  Bioss
Description:   Phosphatidylethanolamine (PtdEtn) is a major membrane phospholipid which serves to play a primary role in cell membrane structure and is also involved in cell division, cell signaling, activation, phagocytosis and autophagy. PCYT2 (Phosphorylethanolamine transferase), also known as Ethanolamine-phosphate cytidylyltransferase, is a 389 amino acid protein that catalyzes the formation of CDP-ethanolamine from ethanolamine. This product combined with diacylglycerol form phosphatidylethanolamine via the de novo Kennedy pathway. PCYT2 is expressed at highest levels in heart, liver and skeletal muscle. Elevated levels of MyoD, reduced content of Sp1 and a changed ratio of Sp1 to Sp3 all together stimulate upregulation of PCTY2 transcription during C2C12 muscle cell differentiation. Disruption of the PCYT2 gene in mice leads to death after embryo implantation, establishing the necessity of PCYT2 for murine development.
Supplier:  Biolegend
Description:   Purified anti-STAT1 [10C4B40]; Isotype: Mouse IgG1, κ; Reactivity: Human; Apps: WB; Size: 100 μg
Catalog Number: (76171-046)

Supplier:  Boster Biological Technology
Description:   Rabbit IgG polyclonal antibody for CAD detection. Tested with WB, Direct ELISA in Human;Mouse.
Supplier:  Rockland Immunochemical
Description:   Secondary Rabbit Anti-IgG F(c) Reacts with Guinea Pig
Supplier:  Rockland Immunochemical
Description:   Secondary Goat Anti-λ lambda chain Reacts with Human
Supplier:  Bioss
Description:   Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.

Supplier:  Bioss
Description:   Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
Supplier:  Bioss
Description:   Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.

Supplier:  Biolegend
Description:   Purified anti-mouse GITR Ligand [5F1]; Isotype: Rat IgG2a, κ; Reactivity: Mouse; Apps: FC; Size: 100 μg
Supplier:  Rockland Immunochemical
Description:   Secondary Goat Anti-IgG (gamma chain) Reacts with Monkey
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
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1,841 - 1,856  of 11,542