OCM Human

Oncomodulin-1 Human Recombinant
Cat. No.
BT2600
Source
Escherichia Coli.
Synonyms
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
Appearance
Purity
Usage

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

Shipped with Ice Packs
In Stock

Description

The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.

Product Specs

Introduction
Oncomodulin is a calcium-binding protein belonging to the calmodulin superfamily, also known as EF-hand proteins. It exhibits high affinity for calcium ions. As an oncodevelopmental protein, oncomodulin is present in early embryonic cells, the placenta, and tumor tissues.
Description
Recombinant Human Oncomodulin-1, expressed in E.coli, has a molecular weight of 13.21 kDa. It comprises 117 amino acid residues of the human Oncomodulin-1 protein and a 9 amino acid His tag fused at the N-terminus.
Formulation
Oncomodulin-1 was subjected to filtration (0.4 µm) and lyophilized at a concentration of 0.5 mg/ml in a buffer solution of 20mM Tris and 50mM NaCl, pH 7.5.
Solubility
To prepare a working stock solution, reconstitute the lyophilized pellet by adding deionized water to achieve a concentration of approximately 0.5 mg/ml. Ensure complete dissolution. Prior to cell culture applications, sterilize the product by filtration using an appropriate sterile filter, as it is not supplied sterile.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. The reconstituted protein remains stable at 4°C for a limited period and exhibits no noticeable changes for up to two weeks at this temperature.
Applications
Western blotting.
Synonyms
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
Source
Escherichia Coli.
Amino Acid Sequence

MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.

Product Science Overview

Structure and Characteristics

The recombinant human Oncomodulin-1 is produced in E. coli and has a molecular mass of approximately 13.21 kDa. It consists of 117 amino acid residues and is fused to a 9 amino acid His tag at the N-terminus . Oncomodulin-1 contains two EF-hand domains, which are helix-loop-helix structural domains capable of binding calcium ions with high affinity .

Biological Functions

Oncomodulin-1 serves several important biological functions:

  1. Calcium Binding: As a high-affinity calcium ion-binding protein, Oncomodulin-1 plays a crucial role in calcium signaling pathways.
  2. Growth Regulation: It exhibits calmodulin-like activity, which is involved in enzyme activation and growth regulation .
  3. Axon Regeneration: Oncomodulin-1 acts as a macrophage-derived growth factor that promotes axon regeneration in retinal ganglion cells (RGCs). It is secreted by activated macrophages in the vitreous and retina in response to inflammatory conditions that promote optic nerve regeneration .
Applications

Recombinant human Oncomodulin-1 is used in various research applications, including:

  • Western Blotting: It is commonly used as a protein marker in Western blotting experiments.
  • Cancer Research: Due to its presence in tumors, Oncomodulin-1 is studied for its potential role in cancer development and progression .
  • Neuroscience Research: Its ability to promote axon regeneration makes it a valuable tool in neuroscience research, particularly in studies related to optic nerve injuries .
Storage and Stability

The recombinant human Oncomodulin-1 is typically lyophilized and stored at -20°C. After reconstitution, it should be aliquoted to avoid repeated freezing and thawing cycles. The reconstituted protein can be stored at 4°C for a limited period without significant changes in its properties .

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