CALML5 Protein, Human (His)

CALML5 Protein, known for its calcium-binding capacity, potentially participates in keratinocyte terminal differentiation, indicating a role in skin cell maturation. Its association with transglutaminase 3 suggests collaboration in skin development functions. CALML5's calcium-binding property likely contributes to its regulatory role in keratinocyte differentiation, emphasizing its significance in intricate molecular mechanisms governing skin cell maturation. CALML5 Protein, Human (His-GST) is the recombinant human-derived CALML5 protein, expressed by E. coli, with N-His, N-GST labeled tag. The total length of CALML5 Protein, Human (His-GST) is 146 a.a., with molecular weight of ~43 kDa.

The CALML5 Protein is characterized by its calcium-binding capacity and may play a role in the terminal differentiation of keratinocytes. This suggests a potential involvement in key processes associated with the maturation and specialization of these skin cells. Notably, CALML5 associates with transglutaminase 3, indicating a possible collaborative role in cellular functions related to skin development and maintenance. The calcium-binding property of CALML5 likely contributes to its regulatory functions in these processes, underscoring its significance in the intricate molecular mechanisms governing keratinocyte differentiation.

Human

E. coli

N-His

Q9NZT1 (M1-E146)

51806  [NCBI]

MAGELTPEEEAQYKKAFSAVDTDGNGTINAQELGAALKATGKNLSEAQLRKLISEVDSDGDGEISFQEFLTAAKKARAGLEDLQVAFRAFDQDGDGHITVDELRRAMAGLGQPLPQEELDAMIREADVDQDGRVNYEEFARMLAQE

Approximately 15-18 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.