Analytical Data
-
Gene name
CALML5
-
简介
The CALML5 protein is known for its calcium-binding ability and may be involved in terminal differentiation of keratinocytes, suggesting a role in skin cell maturation. Its association with transglutaminase 3 suggests cooperation in skin development function. CALML5 Protein, Human (His-GST) is the recombinant human-derived CALML5 protein, expressed by E. coli , with N-His, N-GST labeled tag.
- Application
-
Alternative Names
Calmodulin-like protein 5; Calmodulin-like skin protein; CLSP
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NZT1
-
Expression Region
M1-E146
-
Protein Length
Full Length
-
Molecular Weight
15-18 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
CALML5, a member of the calmodulin-like (CALM) protein family, has garnered significant interest in recent years due to its potential role in various biological processes, including calcium signaling, protein interactions, and cellular responses to stress. Initial studies indicated that CALML5 is highly expressed in specific tissues, suggesting its involvement in tissue-specific functions. Furthermore, its unique structural properties, which include EF-hand motifs that bind calcium, position CALML5 as a critical regulator in calcium-mediated signaling pathways. Recent research has indicated that CALML5 may play a pivotal role in cell proliferation, differentiation, and apoptosis, thereby influencing cancer progression and other diseases. Investigating the recombinant expression of CALML5 can provide insights into its functional mechanisms and interactions with other cellular components. Understanding its role could lead to the identification of novel therapeutic targets and biomarker development for diseases where CALML5 expression is altered. Given its potential implications in human health and disease, ongoing research into the recombinant protein properties of CALML5 is vital for elucidating its functions and applications in biomedical science.
