Recombinant Human Transient Receptor Potential Cation Channel Subfamily M Member 1 (TRPM1) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00174P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Transient Receptor Potential Cation Channel Subfamily M Member 1 (TRPM1) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00174P
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Product Overview

Description Recombinant Human Transient Receptor Potential Cation Channel Subfamily M Member 1 (TRPM1) Protein (His&Myc) 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 Q7Z4N2
Target Symbol TRPM1
Synonyms (Long transient receptor potential channel 1)(LTrpC1)(Melastatin-1)
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence RCRKKREGDQEERDRGLKLFLSDEELKRLHEFEEQCVQEHFREKEDEQQSSSDERIRVTSERVENMSMRLEEINERETFMKTSLQTVDLRLAQLEELSNRMVNALENLAGIDRSDLIQARSRASSECEATYLLRQSSINSADGYSLYRYHFNGEELLFEDTSLSTSPGTGVRKKTCSFRIKEEKDVKTHLVPECQNSLHLSLGTSTSATPDGSHLAVDDLKNAEESKLGPDIGISKEDDERQTDSKKEETISPSLNKTDVIHGQDKSDVQNTQLTVETTNIEGTISYPLEETKITRYFPDETINACKTMKSRSFVYSRGRKLVGGVNQDVEYSSITDQQLTTEWQCQVQKITRSHSTDIPYIVSEAAVQAEHKEQFADMQDEHHVAEAIPRIPRLSLTITDRNGMENLLSVKPDQTLGFPSLRSKSLHGHPRNVKSIQGKLDRSGHASSVSSLVIVSGMTAEEKKVKKEKASTETEC
Expression Range 1127-1603aa
Protein Length Partial
Mol. Weight 61.5 kDa
Research Area Signal Transduction
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 Forms nonselective divalent cation-conducting channels which mediate the influx of Na(2+), Ca(2+), Mg(2+), Mn(2+), Ba(2+), and Ni(2+) into the cytoplasm, leading to membrane depolarization. Impermeable to zinc ions. In addition, forms heteromultimeric ion channels with TRPM3 which are permeable for calcium and zinc ions. Essential for the depolarizing photoresponse of retinal ON bipolar cells. It is part of the GRM6 signaling cascade. May play a role in metastasis suppression. May act as a spontaneously active, calcium-permeable plasma membrane channel.
Subcellular Location Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell projection, axon.
Protein Families Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM1 sub-subfamily
Database References

HGNC: 7146

OMIM: 603576

KEGG: hsa:4308

STRING: 9606.ENSP00000380897

UniGene: PMID: 28726569

  • These results show that joint tests of main effects and gene-gene interaction reveal associations at some novel loci that were missed when considering main effects alone. PMID: 28813576
  • Loss of TRPM1 mRNA expression appears to be a crucial event in the progression of melanoma to a more malignant, metastatic phenotype. PMID: 27987328
  • This study reveals the structural underpinnings of TRPML1's regulation, assembly and pathogenesis. PMID: 28112729
  • Affected family members harboured the homozygous 1-bp deletion c.2394delC in exon 18 of the TRPM1 gene, whereas their unaffected parents were heterozygous carriers. PMID: 27084085
  • genotype-phenotype correlations showed that this eye phenotype was secondary to homozygous deletion of TRPM1, the gene responsible for autosomal recessive congenital stationary night blindness. The main differential diagnosis is ceroid lipofuscinosis. PMID: 24668847
  • these data indicate that purified TRPM1 is mostly dimeric. The three-dimensional structure of TRPM1 dimers is characterized by a small putative transmembrane domain and a larger domain with a hollow cavity. PMID: 25112866
  • visual deficits in melanoma associated retinopathy are caused by the uptake of TRPM1 autoantibodies into ON-bipolar cells PMID: 23936334
  • This is the first reported case of a melanoma-associated retinopathy diagnosed utilizing the innovative approach of testing for serum TRPM1 autoantibodies. PMID: 24053997
  • These data suggest differences in coupling of TRPM1 function to mGluR6 signaling explain different cellular responses to glutamate in the retina and the skin. PMID: 23452348
  • We found 13 different mutations in the TRPM1 gene in congenital stationary night blindness. PMID: 23714322
  • The results expand the mutation spectrum of NYX, CACNA1F and GRM6. They also suggest that NYX mutations are a common cause of congenital stationary night blindness (CSNB),No variations were found in TRPM1. PMID: 22735794
  • present investigation found no evidence for an association between sequence variation at the TRPM1 gene and albumin-to-creatinine ratio in Mexican Americans, although it appears to have modest influence on T2DM risk factors PMID: 21439949
  • In the human retina TRPM1 is expressed on ON-bipolar cell dendrites that invaginate photoreceptor terminals and is also expressed on the synaptic ribbons of a subclass of rods, suggesting a dual function for TRPM1 in the ON-pathway. PMID: 21896854
  • A proteomic search for proteins associated with nyctalopin in the retina identifies TRPM1 as the binding partner. PMID: 21832182
  • This study reveals TRPM1 to be one of the autoantigens targeted by autoantibodies in at least some patients with cancer-associated retinopathy or melanoma-associated retinopathy associated with retinal ON bipolar cell dysfunction. PMID: 21611200
  • Data demonstrate that TRPM1 proteins are bona fide ion-conducting plasma membrane channels. PMID: 21278253
  • summarize and discuss our present knowledge of TRPM1: its discovery, expression, regulation, and proposed functions in skin and eye PMID: 21290293
  • This review covers the significant discoveries related to the physiological function and regulatory mechanism of the TRPM1 channel in retinal ON bipolar cells and the association of human TRPM1 mutations. PMID: 20846719
  • TRPM1 is mutated in patients with autosomal-recessive congenital stationary night blindness. PMID: 20346272
  • Human TRPM1 mutations are associated with the complete form of congenital stationary night blindness in Japanese patients. PMID: 20300565
  • studies identify MITF as a major transcriptional regulator of TRPM1 and suggest that its prognostic value may be linked to MITF-mediated regulation of cellular differentiation PMID: 14744763
  • These findings suggest that the pattern of TRPM1 mRNA expression may be helpful in the differentiation of Spitz nevi and nodular melanomas. PMID: 19396153
  • Data suggest that TRPM1 is an ion channel whose function is critical to normal melanocyte pigmentation and is thus a potential target for pigmentation disorders. PMID: 19436059
  • The regulation of TRPM1 by ultraviolet and its role in melanogenesis in epidermal melanocytes are reported. PMID: 19587221
  • Recessive mutations of TRPM1 abrogate ON bipolar cell function and cause complete congenital stationary night blindness. PMID: 19878917
  • [REVIEW] TRPM1 and TRPM2, are localized in intracellular compartments and are involved in melanin synthesis and oxidative stress-induced cell death PMID: 19887679
  • Mutations in TRPM1 are a common cause of complete congenital stationary night blindness. PMID: 19896109
  • TRPM1 is mutated in patients with autosomal-recessive complete congenital stationary night blindness. PMID: 19896113
  • FAQs

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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.

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