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Key Documents

SAB1401130

Sigma-Aldrich

Anti-FABP5 antibody produced in rabbit

purified immunoglobulin, buffered aqueous solution

Synonym(s):

E-FABP, EFABP, PA-FABP, PAFABP

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

mouse, human

technique(s)

western blot: 1 μg/mL

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... FABP5(2171)

General description

This gene encodes the fatty acid binding protein found in epidermal cells, and was first identified as being upregulated in psoriasis tissue. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. The human genome contains many pseudogenes similar to this locus. (provided by RefSeq)

Immunogen

FABP5 (NP_001435.1, 1 a.a. ~ 135 a.a) full-length human protein.

Sequence
MATVQQLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCNFTDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNVTCTRIYEKVE

Biochem/physiol Actions

FABPs (fatty acid-binding proteins) bind saturated and unsaturated long-chain fatty acids reversibly and might be involved in the transport of lipids to specific cellular compartments. FABP5 (fatty acid binding protein 5) serves as a transporter for endocannabinoid. FABP5 is also known as epidermal FABP (E-FABP) or mal1. FABP5 is significantly associated with the development of insulin resistance and atherosclerosis. This gene was found to be overexpressed in cervical cancer and it serves as an important biomarker for cervical cancer. In vitro study proves that FABP5 is necessary for cell proliferation, colony formation, cell migration, and invasion of cervical cancer. FABP5 is associated with cancer types such as bladder, pancreas, prostate, breast cancer and glioblastoma.

Physical form

Solution in phosphate buffered saline, pH 7.4

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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FABP5 correlates with poor prognosis and promotes tumor cell growth and metastasis in cervical cancer.
Wang W
Tumour Biology : the Journal of the International Society For Oncodevelopmental Biology and Medicine, 37(11), 14873-14883 (2016)
The Antinociceptive Agent SBFI-26 Binds to Anandamide Transporters FABP5 and FABP7 at Two Different Sites.
Hsu HC
Biochemistry, 56(27), 3454-3462 (2017)
Hao-Chi Hsu et al.
Biochemistry, 56(27), 3454-3462 (2017-06-21)
Human FABP5 and FABP7 are intracellular endocannabinoid transporters. SBFI-26 is an α-truxillic acid 1-naphthyl monoester that competitively inhibits the activities of FABP5 and FABP7 and produces antinociceptive and anti-inflammatory effects in mice. The synthesis of SBFI-26 yields several stereoisomers, and
Wei Wang et al.
Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 37(11), 14873-14883 (2016-09-21)
Fatty acid-binding protein 5 (FABP5) was found in our previous study to be a potential biomarker for lymph node metastasis of cervical cancer. However, the roles of FABP5 in cervical cancer remain unclear. In the present study, FABP5 expression was
Tokunori Yamamoto et al.
PloS one, 11(12), e0167825-e0167825 (2016-12-10)
Adipose-derived stem cells (ADSC), which exist near adipocytes in adipose tissue, have been used as a potential tool of regenerative medicine. Lipid chaperones, fatty acid-binding protein 4 (FABP4) and 5 (FABP5), are abundantly expressed in adipocytes. FABP4 has recently been

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