You Searched For: Glycine

Catalog Number: (BOSSBS-12947R-CY5)

Supplier: Bioss

Description: CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

UOM: 1 * 100 µl

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Supplier: Biotium

Description: This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.

Supplier: Biotium

Description: This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.

Catalog Number: (BOSSBS-9095R-CY5.5)

Supplier: Bioss

Description: Members of the class-III pyridoxal-phosphate-dependent aminotransferase family, such as AGXT2, catalyze the conversion of glyoxylate to glycine using L-alanine as the amino donor. AGXT2 protects from asymmetric dimethylarginine (ADMA)-induced inhibition in nitric oxide (NO) production. Elevated blood concentrations of ADMA, a methyl derivate of the amino acid arginine and an endogenous inhibitor of nitric oxide (NO) synthase, is produced by the physiological degradation of methylated proteins and is found in association with diabetes, hypertension, congestive heart failure and atherosclerosis. AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) is a 450 amino acid pyridoxal phosphate that exists as a homotetramer. Belonging to the class-III pyridoxal-phosphate-dependent aminotransferase family, AGXT2L2 localizes to the mitochondria and exists as three alternatively spliced isoforms. Encoded by a gene located on human chromosome 5q35.3, AGXT2L2 may have similar functions as AGXT2.

UOM: 1 * 100 µl

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Catalog Number: (PRSI26-325)

Supplier: ProSci Inc.

Description: GATM is a mitochondrial enzyme that belongs to the amidinotransferase family. This enzyme is involved in creatine biosynthesis, whereby it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine. Mutations in this gene cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.This gene encodes a mitochondrial enzyme that belongs to the amidinotransferase family. This enzyme is involved in creatine biosynthesis, whereby it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine. Mutations in this gene cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-12947R-CY3)

Supplier: Bioss

Description: CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12947R-A488)

Supplier: Bioss

Description: CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12947R-A647)

Supplier: Bioss

Description: CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12947R-CY7)

Supplier: Bioss

Description: CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

UOM: 1 * 100 µl

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Supplier: Lovibond

Description: Test kit, DPD Glycine tablet (for CI separation), Range: 0,01 - 0,2 mg/l ClO₂, For unit: MD100, MD600 MultiDirect and Spectrodirect

MSDS

Supplier: Thermo Fisher Scientific

Description: BupH packs are pre-blended and pre-measured dry mixtures of buffers that are easy to prepare and used in protein purification and common laboratory techniques.

Supplier: Hach

Description: Reagents for photometric analysis either in field conditions or in the laboratory.

Supplier: MP Biomedicals

Description: β-Alanine is an N-blocked form of alanine. A nonselective endogenous glycine receptor agonist; a taurine analogue; an electrolyte.

Catalog Number: (USBI133326)

Supplier: US Biological

Description: Anti-SHMT2 Mouse Polyclonal Antibody

UOM: 1 * 50 µG

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Supplier: SCHUELKE MAYR

Description: Liquid concentrate for disinfection and cleaning based on a combination of aromatic alcohols, quaternary ammonium compounds, amphoteric glycine derivatives, and non ionic surfactants.

Certificates

Catalog Number: (BOSSBS-9851R-A680)

Supplier: Bioss

Description: The formation of the spliceosome includes the assembly of Sm proteins in an ordered manner onto snRNAs. This process is mediated by the survival of motor neuron (SMN) protein, and is enhanced by modification of specific arginine residues in the Sm proteins to symmetrical dimethylarginines (sDMAs). sDMA modification of Sm proteins is catalysed by the methylosome, a complex comprised of the type II methyltransferase PRMT5 (also designated Jak-binding protein 1, JBP1), pICln, and two novel factors. PRMT5 binds the Sm proteins via their arginine- and glycine-rich (RG) domains, while pICln binds the Sm domains. pICln also acts as an inhibitor of SnRNP assembly by preventing specific interactions between Sm proteins required for the formation of the Sm core. pICln is a highly conserved, ubiquitously expressed protein that localizes primarily to the cytoplasm, and may play a role as a swelling-activated anion channel or a channel regulator in addition to its function in the methylosome. The gene encoding human pICln maps to chromosome 11q14.1.

UOM: 1 * 100 µl

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