Recombinant Human Regulator Of Microtubule Dynamics Protein 3 (RMDN3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10189P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Regulator Of Microtubule Dynamics Protein 3 (RMDN3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10189P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Regulator Of Microtubule Dynamics Protein 3 (RMDN3) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q96TC7
Target Symbol RMDN3
Synonyms RMDN3; FAM82A2; FAM82C; PTPIP51; hucep-10; UNQ3122/PRO10274; Regulator of microtubule dynamics protein 3; RMD-3; hRMD-3; Cerebral protein 10; Protein FAM82A2; Protein FAM82C; Protein tyrosine phosphatase-interacting protein 51; TCPTP-interacting protein 51
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence MSRLGALGGARAGLGLLLGTAAGLGFLCLLYSQRWKRTQRHGRSQSLPNSLDYTQTSDPGRHVMLLRAVPGGAGDASVLPSLPREGQEKVLDRLDFVLTSLVALRREVEELRSSLRGLAGEIVGEVRCHMEENQRVARRRRFPFVRERSDSTGSSSVYFTASSGATFTDAESEGGYTTANAESDNERDSDKESEDGEDEVSCETVKMGRKDSLDLEEEAASGASSALEAGGSSGLEDVLPLLQQADELHRGDEQGKREGFQLLLNNKLVYGSRQDFLWRLARAYSDMCELTEEVSEKKSYALDGKEEAEAALEKGDESADCHLWYAVLCGQLAEHESIQRRIQSGFSFKEHVDKAIALQPENPMAHFLLGRWCYQVSHLSWLEKKTATALLESPLSATVEDALQSFLKAEELQPGFSKAGRVYISKCYRELGKNSEARWWMKLALELPDVTKEDLAIQKDLEELEVILRD
Expression Range 1-470aa
Protein Length Full Length
Mol. Weight 56.1kDa
Research Area Apoptosis
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 Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis.
Subcellular Location Mitochondrion outer membrane; Single-pass membrane protein. Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole.
Protein Families RMDN family
Database References
Tissue Specificity Present at high level in epidermis and seminiferous epithelium: while basal cells in the epidermis and spermatogonia show no perceptible amount, keratinocytes of suprabasal layers and differentiating first-order spermatocytes up to spermatids exhibit high

Gene Functions References

  1. Study shows that the VAPB-PTPIP51 tethers regulate autophagy and demonstrates that overexpression of VAPB or PTPIP51 to tighten endoplasmic reticulum-mitochondria contacts impairs, whereas small interfering RNA-mediated loss of VAPB or PTPIP51 to loosen contacts stimulates, autophagosome formation. PMID: 28132811
  2. the latest findings concerning PTPIP51 protein function, regulation and protein complex formation with regard to the involved signaling pathways and subcellular compartments (review) PMID: 27734150
  3. High PTPIP51 expression is associated with glioblastoma. PMID: 25862004
  4. PTPIP51 is regulated by its phosphorylation status combined with a thereby induced subcellular redistribution. PMID: 24501773
  5. The presented data confirms a tyrosine phosphorylation-dependent interaction of PTPIP51 with 14-3-3beta and Raf-1 in vivo and a tyrosine-dependent interaction profile with DAGKalpha and PKA. PMID: 22544307
  6. In glioblastoma PTPIP51 expression increases with the grade of malignancy and PTPIP51 interacts in situ with 14-3-3ss and PTP1B. PMID: 21972092
  7. PTPIP51 is phosphorylated by Lyn and c-Src kinases lacking dephosphorylation by PTP1B in acute myeloid leukemia. PMID: 21513978
  8. PTPIP51 expression was restricted to myeloid precursor cells undergoing differentiation. In blood cells therefore, PTPIP51 expression is restricted to differentiating and mature neutrophil granulocytes. PMID: 20627780
  9. PTPIP51 might be involved in the regulation of cellular processes associated with differentiation, movement, or cytoskeletal organization PMID: 15609043
  10. PTPIP51 is a mitochondrial protein with apoptosis-inducing function and that the N-terminal TM domain is required for both the correct targeting of the protein to mitochondria and its apoptotic functions. PMID: 16820967
  11. PTPIP51 and PTP1B, play a role in differentiation and apoptosis of the cytotrophoblast and syncytiotrophoblast, respectively. Moreover, PTPIP51 may also serve as a cellular signaling partner in angiogenesis and vascular remodeling. PMID: 18854601
  12. FAM82A2 is expressed in keratinocyte carcinoma and their surrounding stroma. PMID: 19012732
  13. The results clearly point toward a strong association between PTPIP51 expression and differentiation in human muscle cells. PMID: 19124842
  14. The promoter methylation status of PTPIP51 seems to influence the expression of PTPIP51, which was seen as elevated in the prostate carcinoma. PMID: 19691131

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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