ZIP4 Antibody
(Synonyms: ZIP4, SLC39A4, Zinc transporter ZIP4, Solute carrier family 39 member 4, Zrt- and Irt-like protein 4, ZIP-4)ZIP4 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to ZIP4.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 |
Product Details
ZIP4 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to ZIP4.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 75 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 68 kDa
Purified recombinant protein of human ZIP4.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
ZIP4 is a Selective transporter that mediates the uptake of Zn(2+). Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability. Also exhibits polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(2+) but at higher concentrations[1][2][3][4][5][6][7][8][9][10].
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Subcellular Localization
Cell membrane; Recycling endosome membrane; Apical cell membrane
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Expression
Tissue_Specificity: Highly expressed in kidney, small intestine, stomach, colon, jejunum and duodenum. -
Isoforms & Post-Translational Modification
ZIP4 has 2 isoforms, Q6P5W5-1: amino acid length is 647, molecular weight is 68408 Da (predicted); Q6P5W5-2: amino acid length is 622, molecular weight is 66178 Da (predicted).细胞缺锌时，胞外 N 端胞外域会被切割，N 端被切割后的 SLC39A4 的内吞速率会加快ZIP4 存在 2 个异构体，Q6P5W5-1：氨基酸个数为 647 个，分子量为 68408 Da (预测)；Q6P5W5-2：氨基酸个数为 622 个，分子量为 66178 Da (预测)。The extracellular N-terminal ectodomain is cleaved when cells are Zn(2+) deficient, N-terminally cleaved SLC39A4 is internalized at a faster rate
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Subunit
Homodimer; homodimerization is mediated by the transmembrane domain
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SwissProt ID
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Synonyms
ZIP4, SLC39A4, Zinc transporter ZIP4, Solute carrier family 39 member 4, Zrt- and Irt-like protein 4, ZIP-4
Documentation
[1]. Mao X, et al. A histidine-rich cluster mediates the ubiquitination and degradation of the human zinc transporter, hZIP4, and protects against zinc cytotoxicity. J Biol Chem. 2007 Mar 9;282(10):6992-7000. [Content Brief]
[2]. Antala S, et al. The human ZIP4 transporter has two distinct binding affinities and mediates transport of multiple transition metals. Biochemistry. 2012 Feb 7;51(5):963-73. [Content Brief]
[3]. Zhang T, et al. Structural insights of ZIP4 extracellular domain critical for optimal zinc transport. Nat Commun. 2016 Jun 20;7:11979. [Content Brief]
[4]. Zhang T, et al. Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway. Sci Adv. 2017 Aug;3(8):e1700344. [Content Brief]
[5]. Zhang T, et al. The histidine-rich loop in the extracellular domain of ZIP4 binds zinc and plays a role in zinc transport. Biochem J. 2019 Jun 28;476(12):1791-1803. [Content Brief]
[6]. Zhang T, et al. Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4. FASEB J. 2020 Jan;34(1):237-247. [Content Brief]
[7]. Hoch E, et al. Elucidating the H(+) Coupled Zn(2+) Transport Mechanism of ZIP4; Implications in Acrodermatitis Enteropathica. Int J Mol Sci. 2020 Jan 22;21(3):. [Content Brief]
[8]. Kuliyev E, et al. Zinc transporter mutations linked to acrodermatitis enteropathica disrupt function and cause mistrafficking. J Biol Chem. 2021 Jan-Jun;296:100269. [Content Brief]
[9]. Liu Y, et al. The transmembrane domains mediate oligomerization of the human ZIP4 transporter in vivo. Sci Rep. 2022 Dec 6;12(1):21083. [Content Brief]
[10]. Zhang C, et al. Molecular Basis of Zinc-Dependent Endocytosis of Human ZIP4 Transceptor. Cell Rep. 2020 Apr 28;31(4):107582. [Content Brief]
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