Recombinant Human Metal Cation Symporter Zip14 (SLC39A14) Protein (His)

Name: Recombinant Human Metal Cation Symporter Zip14 (SLC39A14) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00110P
Price: 240.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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100ug

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Product Overview

Description	Recombinant Human Metal Cation Symporter Zip14 (SLC39A14) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q15043
Target Symbol	SLC39A14
Synonyms	(LIV-1 subfamily of ZIP zinc transporter 4)(LZT-Hs4)(Solute carrier family 39 member 14)(Zrt- and Irt-like protein 14)(ZIP-14)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	SSLGAPAISAASFLQDLIHRYGEGDSLTLQQLKALLNHLDVGVGRGNVTQHVQGHRNLSTCFSSGDLFTAHNFSEQSRIGSSELQEFCPTILQQLDSRACTSENQENEENEQTEEGRPSAVEVWGYG
Expression Range	31-157aa
Protein Length	Partial
Mol. Weight	20.8 kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity. Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions. Beside these endogenous cellular substrates, can also import cadmium a non-essential metal which is cytotoxic and carcinogenic. Controls the cellular uptake by the intestinal epithelium of systemic zinc, which is in turn required to maintain tight junctions and the intestinal permeability. Modifies the activity of zinc-dependent phosphodiesterases, thereby indirectly regulating G protein-coupled receptor signaling pathways important for gluconeogenesis and chondrocyte differentiation. Regulates insulin receptor signaling, glucose uptake, glycogen synthesis and gluconeogenesis in hepatocytes through the zinc-dependent intracellular catabolism of insulin. Through zinc cellular uptake also plays a role in the adaptation of cells to endoplasmic reticulum stress. Major manganese transporter of the basolateral membrane of intestinal epithelial cells, it plays a central role in manganese systemic homeostasis through intestinal manganese uptake. Also involved in manganese extracellular uptake by cells of the blood-brain barrier. May also play a role in manganese and zinc homeostasis participating in their elimination from the blood through the hepatobiliary excretion. Also functions in the extracellular uptake of free iron. May also function intracellularly and mediate the transport from endosomes to cytosol of iron endocytosed by transferrin. Plays a role in innate immunity by regulating the expression of cytokines by activated macrophages.
Subcellular Location	Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein.
Protein Families	ZIP transporter (TC 2.A.5) family
Database References	HGNC: 20858 OMIM: 608736 KEGG: hsa:23516 STRING: 9606.ENSP00000289952 UniGene: PMID: 27231142 These results suggest that the wild type p53 plays a role in regulating ZIP14, but not DMT1 in HepG2 cells. PMID: 29292794 Zip14 activity is needed for adaptation to endoplasmic reticulum stress in liver. PMID: 28673968 Polymorphisms in SLC39A14 and SLC39A8 seemed to affect blood cadmium concentrations, for SLC39A14 this effect may occur via differential gene expression. PMID: 24514587 These results suggest that both the up-regulation of ZIP14 and the down-regulation of ZnT10 by IL-6 might have enhanced the accumulation of manganese in SH-SY5Y cells. PMID: 24576911 Asparagine-linked (N-linked) glycosylation of ZIP14, particularly the glycosylation at N102, was required for efficient membrane extraction of ZIP14 and therefore is necessary for its iron sensitivity. PMID: 24927598 Zip14 expression induced by lipopolysaccharides in macrophages attenuates inflammatory response PMID: 23052185 Data show the role of ZIP14 in the hepatocyte is multi-functional since zinc and iron trafficking are altered in the Zip14(-/-) mice and their phenotype shows defects in glucose homeostasis. PMID: 23110240 the SLC39A14-exon4B transcript variant is a colorectal cancer biomarker with high sensitivity and organ-confined specificity. PMID: 22173985 Data suggest that Zip-14 mRNA level in enterocytes increases with iron or zinc depletion; Zip-14 transcript level in enterocytes decreases with zinc supplementation. PMID: 22137264 Observations indicate that ZIP14 and ZIP8 are both broad-scope metal-ion transporters that can mediate the cellular uptake of nutritionally important metals as well as the toxic heavy metal cadmium. PMID: 22318508 ZIP14 downregulation is likely involved in the depletion of zinc in the hepatoma cells in Hepatocellular cancer PMID: 21373779 The transporter ZIP14 is up-regulated along the entire gastrointestinal tract by proinflammatory conditions. PMID: 21462106 Alternative splicing of SLC39A14 was identified in colorectal tumors and found to be regulated by the Wnt pathway. PMID: 20938052 These results suggest that endosomal ZIP14 participates in the cellular assimilation of iron from transferrin, thus identifying a potentially new role for ZIP14 in iron metabolism. PMID: 20682781 ZIP14 (SLC39A14)was shown to function as a zinc influx transporter in a temperature-dependant manner. PMID: 15642354 Zip14 expression is up-regulated through IL-6 PMID: 15863613 HFE decreases the stability of Zip14 and therefore reduces the iron loading in HepG2 cells PMID: 18524764

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.