CALML5 Human

Calmodulin Like 5 Human Recombinant
Cat. No.
BT2593
Source
Escherichia Coli.
Synonyms

CLSP, Calmodulin-like skin protein, CALML5, Calmodulin-like protein 5. 

Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Shipped with Ice Packs
In Stock

Description

CALML5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-146) containing 155 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 17.0kDa (calculated). 

Product Specs

Introduction

Calmodulin Like 5, also known as CALML5, belongs to the calmodulin family of calcium-binding proteins. Upon binding calcium, CALML5 undergoes a conformational change. This protein plays a role in the terminal differentiation of keratinocytes. The gene encoding CALML5 is expressed in the epidermis.

Description

Recombinant human CALML5, expressed in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 2-146. It includes a 10-amino acid N-terminal His tag, resulting in a total of 155 amino acids. The calculated molecular mass is 17.0 kDa.

Physical Appearance
Lyophilized powder with a white, filtered appearance.
Formulation

CALML5 is subjected to filtration (0.4 µm) and lyophilization from a solution of 20 mM Tris buffer (pH 7.5) containing 50 mM NaCl and 5% w/v trehalose at a concentration of 0.5 mg/ml.

Solubility

To prepare a working stock solution, it is recommended to reconstitute the lyophilized pellet with deionized water to an approximate concentration of 0.5 mg/ml. Allow the pellet to dissolve completely. Please note that CALML5 is not sterile. Before using in cell culture, filter the product through an appropriate sterile filter.

Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to prevent repeated freeze-thaw cycles. Reconstituted protein exhibits stability at 4°C for a limited period; no changes are observed after two weeks at this temperature.
Purity

Purity exceeds 95.0%, as determined by SDS-PAGE analysis.

Synonyms

CLSP, Calmodulin-like skin protein, CALML5, Calmodulin-like protein 5. 

Source
Escherichia Coli.
Amino Acid Sequence

MKHHHHHHAS AGELTPEEEA QYKKAFSAVD TDGNGTINAQ ELGAALKATG KNLSEAQLRK LISEVDSDGD GEISFQEFLT AAKKARAGLE DLQVAFRAFD QDGDGHITVD ELRRAMAGLG QPLPQEELDA MIREADVDQD GRVNYEEFAR MLAQE.

Product Science Overview

Structure and Function

CALML5 is a member of the calmodulin family of calcium-binding proteins. These proteins play crucial roles in various cellular processes by binding calcium ions and undergoing conformational changes that allow them to interact with other proteins . The CALML5 protein is specifically expressed in the epidermis, the outermost layer of the skin, and is involved in the terminal differentiation of keratinocytes, which are the predominant cell type in the epidermis .

Expression and Localization

The expression of CALML5 is abundant in reconstructed epidermis and is restricted to differentiating keratinocytes . This specific expression pattern suggests that CALML5 plays a significant role in skin biology, particularly in the formation and maintenance of the skin barrier .

Interaction with Other Proteins

CALML5 has been shown to associate with transglutaminase 3 (TGM3), an enzyme that is key to the terminal differentiation of keratinocytes . This interaction is essential for the formation of the cornified envelope, a structure that provides mechanical strength and water resistance to the skin .

Recombinant CALML5

Recombinant CALML5 refers to the protein that is produced through recombinant DNA technology. This involves inserting the CALML5 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. Recombinant CALML5 is used in various research applications to study its structure, function, and interactions with other proteins.

Clinical Significance

Mutations or dysregulation of the CALML5 gene have been associated with certain skin disorders, such as crater-like holes of the optic disc and otomycosis . Understanding the role of CALML5 in skin biology can provide insights into the mechanisms underlying these conditions and potentially lead to the development of targeted therapies.

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