You Searched For: alpha-Amino-gamma-butyrolactone+hydrobromide

Supplier: Thermo Scientific Chemicals

Description: Powder

Certificates

Catalog Number: (TCC2826-100MG)

Supplier: TCI America

Description: CAS Number: 511296-88-1
MDL Number: MFCD02683960
Molecular Formula: C16H16N2S
Molecular Weight: 349.29
Purity/Analysis Method: >98.0% (HPLC)
Form: Crystal
Storage Temperature: <0°C

SDS

Catalog Number: (89147-568)

Supplier: Enzo Life Sciences

Description: p53 inhibitor

Supplier: Enzo Life Sciences

Description: Chemical inhibitor of p53 that protects mice from the side effects of cancer therapy. Reversibly blocks p53-dependent transcriptional activation and apoptosis. Protects against neuronal death in models of stroke and neurodegenerative disorders. Suppresses self-renewal of embryonic stem cells.

Catalog Number: (CAAAJ64277-LB0)

Supplier: Thermo Scientific Chemicals

Description: Pale brown solid

Certificates

Catalog Number: (10782-488)

Supplier: Biosensis

Description: Human beta-Lipotropin is a 93 amino acid polypeptide that is cleaved from carboxy-terminal fragment of the precursor pro-opiomelanocortin (POMC). It stimulates melanocytes to produce melanin, and can also be cleaved into smaller peptides including opioid peptides: gamma-lipotropin, alpha-MSH, beta-MSH, gamma-MSH, alpha-endorphin, beta-endorphin, gamma-endorphin and met-enkephalin

Catalog Number: (10103-930)

Supplier: Prosci

Description: Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Structurally, each subunit is comprised of two distinct domains. The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. While adducins alpha and gamma are ubiquitously expressed, the expression of adducin beta is restricted to brain and hematopoietic tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Heterodimers consisting of alpha and gamma subunits have also been described. Structurally, each subunit is comprised of two distinct domains. The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Various adducin beta mRNAs, alternatively spliced at 3'end and/or internally spliced and encoding different isoforms, have been described. The functions of all the different isoforms are not known.

Catalog Number: (89418-820)

Supplier: Prosci

Description: TRIM5 gamma peptide is used for blocking the activity of the TRIM5 gamma antibody.

Catalog Number: (89361-020)

Supplier: Genetex

Description: Corticotropin (ACTH), synthesized by the anterior pituitary gland, stimulates the adrenal cortex. Human ACTH has a molecular weight of 4,541 and contains 39 amino acids . It has structural similarities to melanotropin (melanocyte-stimulating hormone; MSH). Human beta-melanotropin has 22 amino acid residues and a molecular weight of 2,661. Work on the structure of the ACTH gene by restriction enzyme techniques showed that 6 hormones are derived from one gene: ACTH, lipotropin, alpha-MSH, beta-MSH, endorphin, and one other. Thus, extensive amino acid differences between these hormones were not adequate evidence for their being distinct. ACTH and beta-lipotropin (beta-LPH) are derived from a large precursor peptide. Each of these hormones is known to include smaller peptides having distinct biologic activities: alpha-melanotropin (alpha-MSH) and corticotropin-like intermediate lobe peptide (CLIP) are formed from ACTH; gamma-LPH and beta-endorphin are peptide components of beta-LPH. Beta-MSH is contained within gamma-LPH. The precursor peptide was called proopiomelanocortin (POMC).

Catalog Number: (10086-528)

Supplier: Proteintech

Description: Enolases are cytoplasmic glycolytic enzymes that may be involved in differentiation. Three enolase isoenzymes, alpha, beta and gamma , phaare present in mammalian cells. The alpha form is expressed in most tissues, whereas the beta form is expressed in muscle tissue. The gamma enolase (ENO2), a homodimer, is found in mature neurons and cells of neuronal origin. A switch from alpha enolase to gamma enolase occurs inneural tissue during development.

Catalog Number: (10108-848)

Supplier: Prosci

Description: RGS18 is a member of the regulator of G-protein signaling family. This protein is contains a conserved, 120 amino acid motif called the RGS domain. The protein attenuates the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal.This gene encodes a member of the regulator of G-protein signaling family. This protein is contains a conserved, 120 amino acid motif called the RGS domain. The protein attenuates the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.

Catalog Number: (75789-132)

Supplier: Prosci

Description: Gamma-Glutamylaminecyclotransferase is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline which belongs to the gamma-glutamylcyclotransferase family. It shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and contributes to degradation of proteins cross-linked by transglutaminases. It degrades the cross-link between a lysine and a glutamic acid residue from two proteins that have been cross-linked by transglutaminases. This protein adopts the newly identified cyclotransferase fold, observed in Gamma-Glutamylcyclotransferase, an enzyme with activity toward gamma-glutamyl-alpha-amino acids.

Catalog Number: (10110-688)

Supplier: Prosci

Description: In eukaryotic cells, protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat proteins (COPs). Seven coat proteins have been identified, and they represent subunits of a complex known as coatomer. The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP, delta-COP, epsilon-COP, and zeta-COP. The alpha-COP, encoded by COPA, shares high sequence similarity with RET1P, the alpha subunit of the coatomer complex in yeast. Also, the N-terminal 25 amino acids of alpha-COP encode the bioactive peptide, xenin, which stimulates exocrine pancreatic secretion and may act as a gastrointestinal hormone.In eukaryotic cells, protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat proteins (COPs). Seven coat proteins have been identified, and they represent subunits of a complex known as coatomer. The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP, delta-COP, epsilon-COP, and zeta-COP. The alpha-COP, encoded by COPA, shares high sequence similarity with RET1P, the alpha subunit of the coatomer complex in yeast. Also, the N-terminal 25 amino acids of alpha-COP encode the bioactive peptide, xenin, which stimulates exocrine pancreatic secretion and may act as a gastrointestinal hormone. Alternative splicing results in multiple splice forms encoding distinct isoforms.

Catalog Number: (89350-910)

Supplier: Genetex

Description: Fibrinogen is the main protein of blood coagulation system. It is a large protein (MW 340 kDa) and it consists of two identical subunits that contain three polypeptide chains: alpha, beta and gamma. All chains are connected with each other by a number of disulfide bonds. Fibrinopeptides A (1-16 amino acids) and B (1-17 amino acids) are released by thrombin from the N-terminal parts of alpha- and beta-chains, respectively. In this way fibrinogen is converted into fibrin, which by means of polymerization forms a fibrin clot. Fibrinogen clotting underlies pathogenesis of MI, thromboembolism and thromboses of arteries and veins, since fibrin is the main substrate for thrombus formation. Fibrinogen activation is also involved in pathogenesis of inflammation, tumor growth and many other diseases.

Catalog Number: (10166-260)

Supplier: Genetex

Description: Rabbit Polyclonal antibody to FLJ11506 (alpha- and gamma-adaptin binding protein)

Catalog Number: (89367-368)

Supplier: Genetex

Description: Cyclic GMP-phosphodiesterase plays a key role in the normal functioning of retinal rod photoreceptor cells. The enzyme is composed of alpha- and beta-catalytic subunits which are inhibited by 2 identical gamma subunits. The PDE6 gamma subunit has been cloned and sequenced from human retina. The 1,012-bp cDNA had a coding region of 261 bp that was highly homologous to those of the corresponding cDNA from bovine and mouse retinas. Comparison of the deduced amino acid sequences from 3 species indicated evolutionary conservation.