Recombinant Mouse Retinal Dehydrogenase 2 (ALDH1A2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00139P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse Retinal Dehydrogenase 2 (ALDH1A2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00139P
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Product Overview

Description Recombinant Mouse Retinal Dehydrogenase 2 (ALDH1A2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Activity Not tested.
Uniprotkb Q62148
Target Symbol ALDH1A2
Synonyms (RALDH 2)(RalDH2)(Aldehyde dehydrogenase family 1 member A2)(Retinaldehyde-specific dehydrogenase type 2)(RALDH(II)
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence MTSSEIAMPGEVKADPAALMASLQLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVCNPATGEQVCEVQEADKVDIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRATLATMESLNGGKPFLQAFYIDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFTWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVKRSVERAKRRIVGSPFDPTTEQGPQIDKKQYNKVLELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALMVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
Expression Range 1-518aa
Protein Length Full Length
Mol. Weight 62.6 kDa
Research Area Neuroscience
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 Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Lacks activity with benzaldehyde, acetaldehyde and octanal. Displays complete lack of activity with citral.
Subcellular Location Cytoplasm.
Protein Families Aldehyde dehydrogenase family
Database References

KEGG: mmu:19378

STRING: 10090.ENSMUSP00000034723

UniGene: PMID: 29095919

  • these studies identify Notch signaling in dendritic cells as a crucial balancer of Th17/iTreg, which depends on the direct regulation of Aldh1a2 transcription in dendritic cells PMID: 28779023
  • ALDH2 mutation displays an inverse correlation of coronary collateral vessel formation in patients. PMID: 26315408
  • Data suggest that retinoic acid and GM-CSF-induced retinal dehydrogenase 2 (RALDH2) expression in dendritic cells requires cooperative binding of transcription factor Sp1 via the RA receptor/retinoid X receptor complex to the Aldh1a2 promoter. PMID: 24788806
  • Defects in interdigital programmed cell death and digit separation in Hoxa13 mutant mice may be caused in part by reduced levels of RA signaling stemming from a loss in the direct regulation of Aldh1a2 PMID: 23553814
  • Raldh1 and Raldh3 influence enteric nervous system structure and function and heterozygosity for Raldh2 causes ENS defects PMID: 23806210
  • ALDH1A2 expression was highest in ALDH(very-br) cells, intermediate in ALDH(dim) cells, and lowest in ALDH(br) cells. PMID: 23484127
  • Upregulation of retinal dehydrogenase 2 in alternatively activated macrophages during retinoid-dependent type-2 immunity to helminth infection in mice. PMID: 22927819
  • rendered Fgfr2IIIb(-/-) embryos haploinsufficient for the Raldh2 and examined these embryos for the incidence and severity of duodenal atresia PMID: 23021139
  • In Fgfr2IIIb-/- mouse embryos, a reduction of Raldh2 expression is observed within the duodenal region that is forming the atresia. PMID: 21492869
  • regulation of fat depots through the concerted action of Aldh1 enzymes establishes retinoic acid-dependent tandem regulation of transcription factors ZFP423 and PPARgamma in a depot-specific manner PMID: 21436255
  • Analysis of Ret, Gata3 or Raldh2 mutant mice at birth reveals hydronephrosis and defective ureter maturation, abnormalities that our results suggest are caused, at least in part, by delayed insertion of the nephric duct. PMID: 21521737
  • Wt1 controls retinoic acid signalling in embryonic epicardium through transcriptional activation of Raldh2. PMID: 21343363
  • The heart phenotypes of Raldh2 mutants are very similar and are characterized by a prominent defect in ventricular compact zone growth. PMID: 21138976
  • These findings suggest that an increasing expression of Raldh3 deregulates the balanced mechanisms of insulin and glucagon secretion in the pancreatic islets and may induce beta-cell dysfunction leading to the development of type 2 diabetes. PMID: 20833146
  • Drastic down-regulation of Aldh1a2 observed at both E16 and E18; RT-PCR revealed post-natal reduction in expression (Aldh1a2, 1/13). Results suggest down-regulation of gene is important factor in normal odontogenesis in dental papillae. PMID: 20448247
  • limited to the digit-interdigit junction rather than being expressed throughout the interdigital zone PMID: 20034106
  • raldh2 is expressed in dorsal interneurons throughout the agnathan spinal cord, suggesting ancestral roles for RA signaling in the ontogenesis of intraspinal proprioception. PMID: 20081195
  • Raldh2 and Raldh3 are selectively expressed in cortical stroma and in the ureteric bud during kidney development. Renal development depends mainly on Raldh2. PMID: 20040494
  • Three retinaldehyde dehydrogenases (RALDH1, RALDH2 and RALDH3), show differential expression patterns throughout later mouse organogenesis PMID: 11744377
  • Aldh1a2 haploinsufficiency prevents the appearance of spina bifida and rescues the development of posterior structures. PMID: 11953746
  • Novel retinoic acid generating activities in the neural tube and heart identified by conditional rescue of Raldh2 null mutant mice. PMID: 11959834
  • RALDH2 is responsible for most of the patterns of reporter transgene activity in the spinal cord and trunk mesodermal derivatives. Independent pathways of retinoic acid synthesis may also exist. PMID: 12454286
  • RALDH2 plays a crucial role in producing RA (retinoic acid) required for pharyngeal development, and RA is one of the diffusible mesodermal signals that pattern the pharyngeal endoderm. PMID: 12702665
  • In knockout mice, retinoic acid plays a crucial role in mammalian vascular development; it is required to control endothelial cell proliferation and vascular remodeling during vasculogenesis. PMID: 14627725
  • Expression of retinaldehyde dehydrogenase II in the embryonic mouse caudal hindbrain. PMID: 15053971
  • Raldh2 has a role in retinoic acid synthesis for limb bud initiation and then later as a proximodistal signal during apical ectodermal ridge formation PMID: 15069081
  • The expression patterns of aldh1a2 and aldh1a3 retinoic acid synthesizing enzymes at specific follicular sites suggest that they mediate and are regulated by different epithelial proliferation and differentiation signaling pathways. PMID: 15245423
  • catalysis study of retinaldehyde dehydrogenase type II PMID: 15299009
  • Data show that retinaldehyde dehydrogenase (Raldh)2-/- embryos lacking retinoic acid synthesis in the optic vesicle exhibit a failure in retina invagination needed to develop an optic cup. PMID: 15366004
  • Raldh2 has a role in posterior neural transformation through generation of mesodermal retinoic acid PMID: 15652703
  • Mutant embryos display an early embryonic loss of a subset of Lim1+ brachial motoneurons PMID: 15753214
  • Raldh2 and Cyp26 generate shifting boundaries of retionic acid activity, controlling hindbrain segmental gene expression. PMID: 15872003
  • RALDH-2-deficient mice do not develop a dorsal pancreatic bud. PMID: 16026781
  • We have identified the retinoic acid synthesis enzyme Aldh1a2 gene as a principal target of bone morphogenetic protein (BMP) signaling; prochondrogenic BMPs or growth-differentiation factors attenuate Aldh1a2 expression and the retinoid signaling pathway PMID: 16818722
  • Aldh1a2 transcripts and its protein RALDH2 began to increase in the testis at postnatal day 10, and remained at a high level through postnatal day 20 to adulthood. PMID: 18478160
  • RARalpha/retinoid X receptor beta (RXRbeta) complex binds to the mouse retinaldehyde dehydrogenase 1 (Raldh1) promoter at a non-consensus retinoic acid response element. PMID: 18992716
  • Restricted expression during ontogenesis may correspond to specific sites of RA synthesis during inner ear morphogenesis. PMID: 11472854
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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.

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