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TCI

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Integrin (1) Ras (1) TRP Channel (1)
By Research Areas:	Cancer (1) Cardiovascular Disease (1) Neurological Disease (1)

Inhibitors & Agonists

Screening Libraries

Recombinant Proteins

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-107588

TC-I 15 1 Publications Verification	Integrin	Cardiovascular Disease
TC-I 15 (TC-I-15) is a type of allosteric collagen-binding integrin α2β1 inhibitor, and it also inhibits α1β1 and α11β1. TC-I 15 inhibits platelet adhesion to collagen and thrombus deposition. TC-I 15 prevents the formation of a pre-metastatic microenvironment by inhibiting the uptake of cancer-associated fibroblast (CAF) extracellular vesicles (EVs) by lung fibroblasts, which reduces the metastasis of salivary gland adenocystic carcinoma (SACC) to the lungs in mouse models, .

HY-110199

TC-I 2014	TRP Channel	Neurological Disease
TC-I 2014 (compound 5) is a potent and orally active Benzimidazole-containing transient receptor potential melastatin 8 (TRPM8) antagonist, with IC₅₀ values of 0.8 nM, 3.0 nM and 4.4 nM for canine, human and rat channels respectively. TC-I 2014 exhibits antiallodynic properties in pain models .

HY-124944

APS6-45	Ras	Cancer
APS6-45 is an orally active tumor-calibrated inhibitor (TCI). APS6-45 inhibits RAS/MAPK signaling and exhibits antitumor activity .

Cat. No.	Product Name

HY-L915

Lysine Focused Covalent Fragment Library	445 compounds
Lysine is the second most common target residue used in the design of TCIs and related covalent ligands. Its appeal lies in its abundance in human proteins, which is approximately three times higher than that of cysteine (5.8% vs. 1.9%). This significantly increases the number of proteins suitable for covalent targeting, especially given that many human proteins lack ligandable cysteine residues. Moreover, it has been suggested that functional lysines have a lower probability of being replaced by mutation, as they often play a crucial role in catalysis by acting as bases or nucleophiles. Additionally, lysines are essential for maintaining the structural integrity of proteins and for regulating post-translational modifications (PTMs). Consequently, targeting lysine has garnered significant interest in recent years. Through careful selection, we constructed a structural filter containing over 110 electrophilic groups. By analyzing the electrophilic fragments selected by the structural filter, we removed any molecules with trivial or undesirable structural features. Ultimately, we obtained 445 fragment molecules which can target lysine residue and can be used for fragment-based covalent drug discovery.

Lysine Focused Covalent Fragment Library

445 compounds

Lysine is the second most common target residue used in the design of TCIs and related covalent ligands. Its appeal lies in its abundance in human proteins, which is approximately three times higher than that of cysteine (5.8% vs. 1.9%). This significantly increases the number of proteins suitable for covalent targeting, especially given that many human proteins lack ligandable cysteine residues. Moreover, it has been suggested that functional lysines have a lower probability of being replaced by mutation, as they often play a crucial role in catalysis by acting as bases or nucleophiles. Additionally, lysines are essential for maintaining the structural integrity of proteins and for regulating post-translational modifications (PTMs). Consequently, targeting lysine has garnered significant interest in recent years.

Through careful selection, we constructed a structural filter containing over 110 electrophilic groups. By analyzing the electrophilic fragments selected by the structural filter, we removed any molecules with trivial or undesirable structural features. Ultimately, we obtained 445 fragment molecules which can target lysine residue and can be used for fragment-based covalent drug discovery.

Species:	Human (2) Mouse (1)
Tag:	His (2) Fc (1)
Source:	HEK293 (1) E. coli (2)

Cat. No.	Compare	Product Name	Species	Source

HY-P73268

	Latexin Protein, Mouse (His) Latexin; ECI; TCI; Lxn	Mouse	E. coli
	Latexin protein, possessing notable properties, highly potently inhibits CPA1, CPA2, and CPA4 enzymes in a hardly reversible, non-competitive manner.Its potential role in inflammation regulation is suggested.Latexin Protein, Mouse (His) is the recombinant mouse-derived Latexin protein, expressed by E.coli , with N-His labeled tag.

HY-P73841

	Latexin Protein, Human (His) ECI; ECIMUM; Latexin; LXN; TCI	Human	E. coli
	Latexin, a protein, powerfully inhibits CPA1, CPA2, and CPA4, playing a crucial role in controlling carboxypeptidase activity. It may also regulate inflammation, expanding its physiological significance beyond enzyme inhibition. Latexin Protein, Human (His) is the recombinant human-derived Latexin protein, expressed by E. coli , with N-His labeled tag. The total length of Latexin Protein, Human (His) is 221 a.a., with molecular weight of 30-35 kDa.

HY-P73842

	Latexin Protein, Human (HEK293, Fc) ECI; ECIMUM; Latexin; LXN; TCI	Human	HEK293
	Latexin, a protein, powerfully inhibits CPA1, CPA2, and CPA4, playing a crucial role in controlling carboxypeptidase activity. It may also regulate inflammation, expanding its physiological significance beyond enzyme inhibition. Latexin Protein, Human (HEK293, Fc) is the recombinant human-derived Latexin protein, expressed by HEK293 , with N-hFc labeled tag. The total length of Latexin Protein, Human (HEK293, Fc) is 221 a.a., with molecular weight of 60-65 kDa.

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