You Searched For: Z-Leu-Leu-Glu-7-amino-4-methylcoumarin

Supplier: Bachem Americas

Description: Sequence: Z-Leu-Leu-Glu-AMC

Catalog Number: (CAAAJ64613-LB0)

Supplier: Thermo Scientific Chemicals

Description: A fluorogenic substrate for the peptidylglutamyl-peptide hydrolysing (caspase-like) activity of the proteasome which may be stimulated in the presence of Mg2+ ions and rapidly inactivated by N-acetylimidazole

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Catalog Number: (CAAAJ64796-LB0)

Supplier: Thermo Scientific Chemicals

Description: Molecular Formula: C28H32N4O7
Formula Weight: 536.57
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White to pale yellow
MDL No.: MFCD00152029

Catalog Number: (I-1820.0005BA)

Supplier: Bachem Americas

Description: Sequence: Ac-Leu-Glu-His-Asp-AFC
Synonym(s): Ac-LEHD-AFC#Caspase 9 Substrate 1f, fluorogenic

Catalog Number: (H-7316.0500BA)

Supplier: Bachem Americas

Description: The protein dermcidin expressed in the sweat glands is secreted into the sweat and transported to the epidermal surface. The concomitant processing of the protein yields a broad-spectrum antimicrobial 47 amino acid peptide, dermcidin-1 (DCD-1).

Catalog Number: (10782-050)

Supplier: Biosensis

Description: The Myc tag contains the amino acids Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu (E-Q-K-L-I-S-E-E-D-L) corresponding to amino acids 410-419 of human Myc. This tag is widely used for monitoring expression of recombinant proteins in bacteria, insect and mammalian cells.

Catalog Number: (10782-450)

Supplier: Biosensis

Description: The Myc tag contains the amino acids Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu (E-Q-K-L-I-S-E-E-D-L) corresponding to amino acids 410-419 of human Myc. This tag is widely used for monitoring expression of recombinant proteins in bacteria, insect and mammalian cells.

Catalog Number: (CA76299-648)

Supplier: New England Biolabs (NEB)

Description: TEV Protease is a highly specific cysteine protease that recognizes the amino-acid sequence Glu-Asn-Leu-Tyr-Phe-Gln-(Gly/Ser) and cleaves between the Gln and Gly/Ser residues.

Supplier: Bachem Americas

Description: Sequence: H-Leu-AMC

Catalog Number: (10092-902)

Supplier: Proteintech

Description: PSMB1(Proteasome subunit beta type-1) is also named as PSC5 and belongs to the peptidase T1B family. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The gene encodes a 241 amino acid protein with a 28 amino acid propeptide and two glycosylation sites.

Catalog Number: (10091-880)

Supplier: Proteintech

Description: PSMB4(Proteasome subunit beta type-4) is also named as PROS26 and belongs to the peptidase T1B family. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The human protein PSMB4 is known mainly as an interaction partner for several proteins, suggesting an important function of binding not only to the lid, but also to the 20 S core of the proteasome. PSMB4 might be a major site for proteasome regulation, where signals from the outside might be transduced to the protease activities inside. The full length 30 kDa protein has a propeptide of 45 amino acid.

Catalog Number: (10111-078)

Supplier: Prosci

Description: Chemokines are a group of small (approximately 8 to 14 kD), mostly basic, structurally related molecules that regulate cell trafficking of various types of leukocytes through interactions with a subset of 7-transmembrane, G protein-coupled receptors. Chemokines also play fundamental roles in the development, homeostasis, and function of the immune system, and they have effects on cells of the central nervous system as well as on endothelial cells involved in angiogenesis or angiostasis. Chemokines are divided into 2 major subfamilies, CXC and CC, based on the arrangement of the first 2 of the 4 conserved cysteine residues; the 2 cysteines are separated by a single amino acid in CXC chemokines and are adjacent in CC chemokines. CXC chemokines are further subdivided into ELR and non-ELR types based on the presence or absence of a glu-leu-arg sequence adjacent and N terminal to the CXC motif.Chemokines are a group of small (approximately 8 to 14 kD), mostly basic, structurally related molecules that regulate cell trafficking of various types of leukocytes through interactions with a subset of 7-transmembrane, G protein-coupled receptors. Chemokines also play fundamental roles in the development, homeostasis, and function of the immune system, and they have effects on cells of the central nervous system as well as on endothelial cells involved in angiogenesis or angiostasis. Chemokines are divided into 2 major subfamilies, CXC and CC, based on the arrangement of the first 2 of the 4 conserved cysteine residues; the 2 cysteines are separated by a single amino acid in CXC chemokines and are adjacent in CC chemokines. CXC chemokines are further subdivided into ELR and non-ELR types based on the presence or absence of a glu-leu-arg sequence adjacent and N terminal to the CXC motif.[supplied by OMIM]. 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.

Catalog Number: (75788-814)

Supplier: Prosci

Description: Human Chemokine (C-X-C motif) Ligand 7 (CXCL7), also known as neutrophil activating peptide 2 (NAP-2), is a member of the CXC chemokines containing an ELR domain (Glu-Leu-Arg tripeptide motif). Similar to other ELR domain containing CXC chemokines, such as IL-8 and the GRO proteins, CXCL7 binds CXCR2, chemoattracts and activates neutrophils. CXCL7, Connective Tissue Activating Protein III (CTAPIII) and beta thrombogulin ( beta TG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. Although CTAPIII, beta TG, and PBP represent amino-terminal extended variants of NAP2 and possess the same CXC chemokine domains, these proteins do not exhibit CXCL7/NAP2 activity. CXCL7 induces cell migration through the G-protein-linked receptor CXCR-2.

Supplier: Bachem Americas

Description: Sequence: Z-Phe-Leu-Glu-pNA

Catalog Number: (89359-700)

Supplier: Genetex

Description: Calnexin, also referred to as IP90, p88 and p90, is an ~90 kDa integral membrane protein of the endoplasmic reticulum (ER). Many resident ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into multisubunit proteins. Studies indicate that calnexin associates with the major histocompatability complex (MHC) class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin, but not with completed receptor complexes. It has been shown that calnexin is a chaperone that retains incompletely or improperly folded proteins in the ER. The sequence Lys-Asp-Glu-Leu (KDEL) or a closely related sequence, is present at the carboxy-terminus of soluble ER resident proteins such as GRP 78 and GRP 94 and protein disulfide isomerase. Integral membrane ER resident proteins, like calnexin, often lack this KDEL sequence but contain positively charged cytosolic residues that ensure ER retention. Calnexin contains a large ER luminal domain (461 amino acids), a transmembrane segment (22 amino acids), and a cytoplasmic tail (89 amino acids).

Catalog Number: (89359-702)

Supplier: Genetex

Description: Calnexin, also referred to as IP90, p88 and p90, is an ~90 kDa integral membrane protein of the endoplasmic reticulum (ER). Many resident ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into multisubunit proteins. Studies indicate that calnexin associates with the major histocompatability complex (MHC) class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin, but not with completed receptor complexes. It has been shown that calnexin is a chaperone that retains incompletely or improperly folded proteins in the ER. The sequence Lys-Asp-Glu-Leu (KDEL) or a closely related sequence, is present at the carboxy-terminus of soluble ER resident proteins such as GRP 78 and GRP 94 and protein disulfide isomerase. Integral membrane ER resident proteins, like calnexin, often lack this KDEL sequence but contain positively charged cytosolic residues that ensure ER retention. Calnexin contains a large ER luminal domain (461 amino acids), a transmembrane segment (22 amino acids), and a cytoplasmic tail (89 amino acids).