Recombinant Human Adp-Ribose Glycohydrolase Macrod1 (MACROD1) Protein (His&Myc)

Name: Recombinant Human Adp-Ribose Glycohydrolase Macrod1 (MACROD1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01392P
Price: 299.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Price Save $1,105

Size

100ug

Product Overview

Description	Recombinant Human Adp-Ribose Glycohydrolase Macrod1 (MACROD1) Protein (His&Myc) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9BQ69
Target Symbol	MACROD1
Synonyms	MACRO domain-containing protein 1O-acetyl-ADP-ribose deacetylase MACROD1Protein LRP16[Protein ADP-ribosylaspartate] hydrolase MACROD1[Protein ADP-ribosylglutamate] hydrolase MACROD1
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	MSLQSRLSGRLAQLRAAGQLLVPPRPRPGHLAGATRTRSSTCGPPAFLGVFGRRARTSAGVGAWGAAAVGRTAGVRTWAPLAMAAKVDLSTSTDWKEAKSFLKGLSDKQREEHYFCKDFVRLKKIPTWKEMAKGVAVKVEEPRYKKDKQLNEKISLLRSDITKLEVDAIVNAANSSLLGGGGVDGCIHRAAGPLLTDECRTLQSCKTGKAKITGGYRLPAKYVIHTVGPIAYGEPSASQAAELRSCYLSSLDLLLEHRLRSVAFPCISTGVFGYPCEAAAEIVLATLREWLEQHKDKVDRLIICVFLEKDEDIYRSRLPHYFPVA
Expression Range	1-325aa
Protein Length	Full Length
Mol. Weight	39.5 kDa
Research Area	Cancer
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	Removes ADP-ribose from asparatate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation. Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction. Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated transcription activity.
Subcellular Location	Nucleus.
Database References	HGNC: 29598 OMIM: 610400 KEGG: hsa:28992 STRING: 9606.ENSP00000255681 UniGene: Hs.602898
Associated Diseases	A chromosomal aberration involving MACROD1 is found in acute leukemia. Translocation t(11;21)(q13;q22) that forms a RUNX1-MACROD1 fusion protein.

Gene Functions References

Here, the authors report that LRP16 selectively interacts and activates double-stranded RNA-dependent kinase (PKR), and also acts as scaffolds to assist the formation of a ternary complex of PKR and IKKbeta, prolonging the polymers of ADP-ribose (PAR)-dependent nuclear factor kappa B (NF-kappaB) transactivation caused by DNA-damaging agents and confers acquired chemoresistance. PMID: 28820388
The results indicate that abnormal LRP16 expression is noted in neuroendocrine lung tumors and the expression can give insight into the pathogenesis of the disease. PMID: 26261536
LRP16, through its constitutive interactions with PARP1 and IKKgamma, functions to facilitate the lesion-specific recruitment of PARP1 and IKKgamma and, ultimately, the concomitant recruitment of PIASy to IKKgamma in response to DNA damage. PMID: 25735744
LRP16 gene overexpression shows a promotive effect on proliferation of K562 cells. PMID: 19840441
LRP16 may play an important role in leukemia progression by promoting cell proliferation, regulating cell cycle, and antagonizing radiation-induced DNA damage. PMID: 19958623
Findings not only indicate that LRP16 is a crucial regulator for NF-kappaB activation inside the nucleus, but also suggest that LRP16 may be an important contributor to the aberrant activation of NF-kappaB in tumors. PMID: 21483817
lrp16 is a leukemic oncogene and closely relates to genesis and progression of leukemia. PMID: 19698216
LRP16 expression is related to the degree of differentiation, invasiveness, metastasis and prognosis of colorectal carcinoma. PMID: 20355243
K18 attenuates estrogen receptor alpha-mediated signaling by sequestering LRP16 in cytoplasm. PMID: 20035625
LRP16 may have a role in invasion, metastasis and prognosis of gastric cancer PMID: 19824120
ERalpha and Sp1 play a role in activation of the promoter PMID: 15691879
LRP16 overexpression is closely correlated to the positive rates of estrogen receptor and progesterone receptor, Ki-67 level, tumor diameter, and axillary lymph node metastasis of breast cancer. PMID: 16831279
identified a novel RUNX1 fusion partner, LRP16 on 11q13 involving t(11;21)(q13;q22) PMID: 17532767
A role for estrogenically regulated LRP16 as an ERalpha coactivator, providing a positive feedback regulatory loop for ERalpha signal transduction. PMID: 17914104
the single macro domain in LRP16 can serve as the androgen receptor coactivator PMID: 19022849
The unliganded ERalpha upregulated LRP16 expression and enhanced LRP16 promoter activity in SKOV3 cells; however, this induction was blocked by estrogen stimulation. PMID: 19403568

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.