APOM Human, HEK

Apolipoprotein-M Human Recombinant, HEK
Cat. No.
BT12434
Source
HEK293.
Synonyms
G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.
Appearance
White lyophilized (freeze-dried) powder.
Purity
Greater than 90% as determined by SDS-PAGE.
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.
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Description

APOM HEK Human Recombinant Protein is 20 kDa protein containing 179 amino acid residues of the APOM Human and 13 additional amino acid residues of flag Tag.

Product Specs

Introduction
Apolipoprotein M (APOM) is a member of the lipocalin protein family and associates with high-density lipoproteins (HDL). It is also found, to a lesser extent, with low-density lipoproteins (LDL) and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it participates in lipid transport.
Description
Recombinant human APOM protein, expressed in HEK cells, is a 20 kDa protein. It comprises 179 amino acid residues of the human APOM sequence and an additional 13 amino acid residues at the C-terminus constituting a flag tag.
Physical Appearance
Sterile, white, lyophilized (freeze-dried) powder.
Formulation
Recombinant human APOM protein solution (0.5 mg/ml) was filtered through a 0.4 μm filter and subsequently lyophilized. The lyophilized protein is supplied in 20 mM TRIS and 50 mM NaCl, pH 7.5.
Solubility
To prepare a working stock solution, add deionized water to the lyophilized protein to achieve a concentration of approximately 0.5 mg/ml. Allow the lyophilized pellet to dissolve completely. The product is not sterile. Prior to using in cell culture, filter the reconstituted protein using an appropriate sterile filter.
Stability
Store lyophilized recombinant human APOM protein at -20°C. After reconstitution, aliquot the protein and store at -20°C to prevent repeated freeze/thaw cycles. Reconstituted protein can be stored at 4°C for a short period (up to two weeks) without noticeable degradation.
Applications
Recombinant human APOM protein is suitable for various research applications, including cell culture, animal studies, enzyme-linked immunosorbent assays (ELISA), and Western blotting.
Purity
The purity of recombinant human APOM protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.
Source
HEK293.
Amino Acid Sequence
HVDYKDDDDK PAGCPEHSQL TTLGVDGKEF PEVHLGQWYF IAGAAPTKEE LATFDPVDNI VFNMAAGSAP MQLHLRATIR MKDGLCVPRK WIYHLTEGST DLRTEGRPDM KTELFSSSCP GGIMLNETGQ GYQRFLLYNR SPHPPEKCVE EFKSLTSCLD SKAFLLTPRN QEACELSNN

Product Science Overview

Introduction

Apolipoprotein M (ApoM) is a member of the apolipoprotein family, which plays a crucial role in lipid metabolism and cardiovascular health. ApoM is predominantly associated with high-density lipoproteins (HDL) and, to a lesser extent, with low-density lipoproteins (LDL) and triglyceride-rich lipoproteins . The recombinant form of ApoM, expressed in Human Embryonic Kidney (HEK) cells, has been extensively studied for its biological properties and potential therapeutic applications.

Structure and Expression

ApoM is a lipocalin protein that is secreted through the plasma membrane but remains membrane-bound, participating in lipid transport . The human recombinant ApoM produced in HEK293 cells is a single, non-glycosylated polypeptide chain containing 166 amino acids, with a molecular mass of approximately 19-24 kDa . It is expressed without a signal peptide sequence and includes a His tag at the N-terminus for purification purposes .

Biological Functions

ApoM has several important biological functions, including:

  • Lipid Transport: ApoM is involved in the transport of lipids, particularly in association with HDL particles .
  • Binding to Retinoic Acid: ApoM can bind to all-trans-retinoic acid, a derivative of vitamin A, which is essential for various physiological processes .
  • Neuroprotection: ApoM secreted by HEK cells stably expressing apoE3 or apoE4 can bind amyloid-beta (Aβ) and inhibit Aβ-induced neurotoxicity, suggesting a potential role in neuroprotection .
Tissue Distribution

ApoM is primarily found in the liver and kidneys, where it is synthesized and secreted into the bloodstream. Its presence in HDL particles suggests a significant role in cholesterol metabolism and cardiovascular health .

Regulatory Mechanisms

The expression of ApoM is regulated by various factors, including:

  • Liver X Receptors (LXR): These nuclear receptors play a key role in the regulation of ApoM expression in response to lipid levels .
  • Peroxisome Proliferator-Activated Receptors (PPARs): These receptors are involved in the regulation of lipid metabolism and can influence ApoM expression .
Potential Therapeutic Applications

Given its role in lipid metabolism and neuroprotection, ApoM has been investigated as a potential therapeutic target for cardiovascular diseases and neurodegenerative disorders. Its ability to bind and transport retinoic acid also highlights its importance in vitamin A metabolism and related physiological processes .

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