ala-gln — TargetMol Chemicals

Cat No.	Product Name	Synonyms	Targets
TP2305	PGlu-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val		Others
	pGlu-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val is a peptides		Others
T74040	Boc-Gln-Ala-Arg-AMC hydrochloride
	Boc-Gln-Ala-Arg-AMC hydrochloride is a fluorescent compound that serves as a substrate for trypsin and is also used to determine the protein hydrolysis activity of TMPRSS2.
T36339	Abz-Ala-Pro-Glu-Glu-Ile-Met-Arg-Arg-Gln-EDDnp
	Abz-Ala-Pro-Glu-Glu-Ile-Met-Arg-Arg-Gln-EDDnp is a fluorescence-quenched peptide substrate for human neutrophil elastase (kcat/Km = 531 mM-1s-1). Enzymatic peptide hydrolysis disrupts the Abz:EDDnp donor-acceptor pair al...
T36340	Abz-Val-Ala-Asp-Nva-Arg-Asp-Arg-Gln-EDDnp (trifluoroacetate salt)
	Abz-Val-Ala-Asp-Nva-Arg-Asp-Arg-Gln-EDDnp is a fluorescence-quenched peptide substrate for human proteinase 3 (kcat/Km = 1,570 mM-1s-1). Enzymatic peptide hydrolysis disrupts the Abz:EDDnp donor-acceptor pair allowing fl...
T5593	L-Alanyl-L-glutamine	Ala-Gln	Others , Endogenous Metabolite
	L-Alanyl-L-glutamine (Ala-Gln), a dipeptide composed of alanine and Gln, is an alternative supplement to L-glutamine in the production of biopharmaceuticals with better solubility and stability than glutamine (Gln).		Others , Endogenous Metabolite
T31609	Eisenin	Pglu-gln-ala,Pyroglutamyl-glutaminyl-alanine
	Eisenin shows the activity as a biological response modifier isolated from brown marine algae, Eisenia bicyclis Setchell.
T76376	Lys-Gln-Ala-Gly-Asp-Val
	Lys-Gln-Ala-Gly-Asp-Val (KQAGDV), the six carboxyl-terminal amino acids of the fibrinogen γ-chain, serves as a cell adhesion peptide via the α2bβ3 integrin. It is a potent adhesion ligand for smooth muscle cells (SMCs) [...
T78402	Boc-Gln-Ala-Arg-AMC acetate
	Boc-Gln-Ala-Arg-AMC acetate is a fluorogenic substrate primarily used for assaying trypsin activity and additionally suitable for evaluating the proteolytic function of TMPRSS2[1][2].
T6990	SNAP8	Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-Nh2,SNAP 8,SNAP-8	Others
	SNAP8 (Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-Nh2) is a mimic of the N-terminal end of SNAP-25 which competes with SNAP-25 for a position in the SNARE complex, thereby modulating its formation.		Others
TP2480	Locustamyotropin	Lom-MT,Locustamyotropin I,Lom MT,LomMT,Gly-ala-val-pro-ala-ala-gln-phe-ser-pro-arg-leu-NH2
	Locustamyotropin is a novel peptide isolated from Leucophae maderae; stimulates the spontaneous contractions of the hindgut of Leucophaea maderae.
T70609	Bisnafide mesylate
	Bisnafide is a Naphthalimide Analogue that acts as DNA intercalator and topo II inhibitor. It is also an antiangiogenic agent. Antiangiogenic agents can normalize tumor vessels and promote the delivery of cytotoxic agent...
T36405	Pro-Adrenomedullin (153-185), human	Pro-Adrenomedullin (153-185), human,H2N-Ser-Leu-Pro-Glu-Ala-Gly-Pro-Gly-Arg-Thr-Leu-Val-Ser-Ser-Lys-Pro-Gln-Ala-His-Gly-Ala-Pro-Ala-Pro-Pro-Ser-Gly-Ser-Ala-Pro-His-Phe-Leu-OH
	Pro-Adrenomedullin(153-185),human, (C143H224N42O43), a peptide with the sequence H2N-SLPEAGPGRTLVSSKPQAHGAPAPPSGSAPHFL-OH, MW= 3219.6. Adrenomedullin (AM) is a ubiquitously expressed peptide initially isolated from phaec...
T21798L	Dynamin inhibitory peptide Acetate	Dynamin inhibitory peptide Acetate(251634-21-6 Free base)	GTPase
	Dynamin inhibitory peptide Acetate is a peptide with the sequence Gln-Val-Pro-Ser-Arg-Pro-Asn-Arg-Ala-Pro that inhibit the GTPase dynamin.		GTPase
TP2199	Rhodopsin peptide		Others
	Rhodopsin peptide is a peptide with the sequence H2N-Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala-OH, MW= 1217.33. Rhodopsin is a biological pigment in photoreceptor cells of the retina that is responsible for the fir...		Others
TP2257	Histone-H2A-(107-122)-Ac-OH		Others
	Histone-H2A-(107-122)-Ac-OH is a peptide with the sequence Ac-Gly-Val-Leu-Pro-Asn-Ile-Gln-Ala-Val-Leu-Leu-Pro-Lys-Lys-Thr-Glu-OH, MW= 1762.1. Histone H2A is one of the five main histone proteins involved in the structure...		Others
TP2182	Lamin fragment		Others
	Lamin fragment has a peptide sequence of Lys-Ala-Gly-Gln-Val-Val-Thr-Ile-Trp. Lamin polypeptides have an almost complete α-helical conformation with multiple α-helical domains separated by non-α-helical linkers that are ...		Others