LGALSL Protein, Human (His)

The LGALSL protein was identified as a member of the galectin family, exhibits no affinity for lactose, and may not be involved in carbohydrate binding. This unique feature distinguishes LGALSL from typical galectins, which are known for their carbohydrate recognition domain and interaction with specific sugar moieties. LGALSL Protein, Human (His) is the recombinant human-derived LGALSL protein, expressed by E. coli , with C-6*His labeled tag.

LGALSL protein, based on available information, does not exhibit lactose-binding activity and may not bind carbohydrates. Lactose is a disaccharide sugar found in milk, and the lack of binding to lactose suggests a distinct functional role for LGALSL. Furthermore, LGALSL is described as a monomeric protein, indicating that it exists as a single, independent unit without forming complexes with other molecules. The absence of lactose binding and a potential lack of carbohydrate binding highlight the specificity and uniqueness of LGALSL's molecular interactions. Further investigations are warranted to elucidate the precise functions and biological significance associated with LGALSL, shedding light on its role within cellular processes and potential implications in various physiological contexts. (

Human

E. coli

C-6*His

Q3ZCW2 (A2-G172)

29094  [NCBI]

Full Length of Mature Protein

AGSVADSDAVVKLDDGHLNNSLSSPVQADVYFPRLIVPFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDSEDPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAIPYFPFIPDQPFRVEILCEHPRFRVFVDGHQLFDFYHRIQTLSAIDTIKINGDLQITKLG

Approximately 18.0 kDa

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.